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ATP + a protein
ADP + a phosphoprotein
ATP + CovR L-histidine
ADP + CovR N-phospho-L-histidine
ATP + CpdR-L-histidine
ADP + CpdR-N-phospho-L-histidine
-
-
-
-
?
ATP + CtrA-L-histidine
ADP + CtrA-N-phospho-L-histidine
-
-
-
-
?
ATP + DivK
?
-
DivJ is the main kinase of DivK
-
-
?
ATP + DraR L-histidine
ADP + DraR N-phospho-L-histidine
ATP + histidine kinase EnvZ
ADP + histidine kinase EnvZ N-phospho-L-histidine
autophosphorylation. Probing catalytically essential domain orientation in histidine kinase EnvZ by targeted disulfide crosslinking
-
-
?
ATP + histidine kinase Hik34
ADP + histidine kinase Hik34 N-phospho-L-histidine
ATP + histidine kinase HK2
ADP + histidine kinase HK2 N-phospho-L-histidine
ATP + PhoN protein L-histidine
ADP + PhoN protein N-phospho-L-histidine
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
ATP + Spo0A L-histidine
ADP + Spo0A N-phospho-L-histidine
ATP + Spo0A-L-histidine
ADP + Spo0A-N-phospho-L-histidine
ATP + Spo0F protein L-histidine
ADP + Spo0F protein N-phospho-L-histidine
-
-
-
-
?
ATP + VicR L-histidine
ADP + VicR N-phospho-L-histidine
ATP + VicR protein L-histidine
ADP + VicR protein N-phospho-L-histidine
ATP + VirG-L-histidine
ADP + VirG-N-phospho-L-histidine
-
-
-
-
?
ATP + YycF
ADP + phospho-YycF
CitB + ATP
?
a fusion protein MalE-CitAC is composed of the maltose-binding protein and the CitA kinase domain shows constitutive autokinase activity and transfers the gamma-phosphate group of ATP to its cognate response regulator CitB
-
-
?
DcuR + ATP
?
the phosphoryl group of DcuS is rapidly transferred to the response regulator DcuR. Upon phosphorylation, DcuR binds specifically to dcuB promoter DNA
-
-
?
EvgA + ATP
?
one hybrid histidine kinase consisting of the BvgS transmitter and HPt domains and of the EvgS receiver domain BvgS-TO-EvgS-R is able to phosphorylate BvgA but not EvgA. In contrast, the hybrid protein consisting of the BvgS transmitter and the EvgS receiver and HPt domains BvgS-T-EvgS-RO is unable to phosphorylate BvgA but efficiently phosphorylates EvgA
-
-
?
GTP + protein-L-histidine
GDP + protein N-phospho-L-histidine
GTP + Spo0F L-histidine
GDP + Spo0F N-phospho-L-histidine
Rcp1 + ATP
?
Cph1 is a light-regulated histidine kinase that mediates red, far-red reversible phosphorylation of the a small response regulator Rcp1
-
-
?
regulator protein OmpR + ATP
?
TorR + ATP
?
TorS is a sensor that contains three phosphorylation sites and transphosphorylates TorR via a four-step phosphorelay, His443 to Asp723 to His850 to Asp(TorR). TorS can dephosphorylate phospho-TorR when trimethylamine N-oxide is removed. Dephosphorylation probably occurs by a reverse phosphorelay, Asp(TorR) to His850 to Asp723
-
-
?
additional information
?
-
ArcA + ATP
?
ArcB undergoes autophosphorylation at the expense of ATP and subsequently transphosphorylates its cognate response regulator ArcA through a His to Asp to His to Asp phosphorelay pathway
-
-
?
ArcA + ATP
?
ArcB undergoes autophosphorylation at the expense of ATP and subsequently transphosphorylates its cognate response regulator ArcA through a His to Asp to His to Asp phosphorelay pathway
-
-
?
ArcA + ATP
?
the arcB gene encodes a sensor-regulator protein for anaerobic repression of the arc modulon
-
-
?
ArcA + ATP
?
the ArcB and ArcA proteins constitute a two-component signal transduction system that plays a broad role in transcriptional regulation. Under anoxic or environmentally reducing conditions, the sensor kinase ArcB is stimulated to autophosphorylate at the expense of ATP and subsequently transphosphorylates the response regulator ArcA
-
-
?
ArcA + ATP
?
phosphoryl group transfer from phosphorylated ArcB to ArcA, signal transmission occurs solely by His-Asp-His-Asp phosphorelay
-
-
?
ATP + a protein
ADP + a phosphoprotein
the two-component sensory transduction system chvG/chvI is required for virulence of Agrobacterium tumefaciens
-
-
?
ATP + a protein
ADP + a phosphoprotein
the two-component sensory transduction system chvG/chvI is required for virulence of Agrobacterium tumefaciens
-
-
?
ATP + a protein
ADP + a phosphoprotein
kinase of the alternate pathway for phosphorylating the SpoOF protein
-
-
?
ATP + a protein
ADP + a phosphoprotein
the essential two-component regulatory system yycF/yycG modulates expression of the ftsAZ operon in Bacillus subtilis
-
-
?
ATP + a protein
ADP + a phosphoprotein
the two-component signal transduction system yycF/yycG is essential for growth of Bacillus subtilis
-
-
?
ATP + a protein
ADP + a phosphoprotein
regulation of the levels of OmpF and OmpC is normally controlled by a multicomponent signal-transducing regulatory pair of proteins, EnvZ and OmpR. The effect RprX and RprY have on OmpF expression is mediated at the level of transcription. Thus, RprX and RprY may be interfering with the normal regulation of OmpF by OmpR and EnvZ
-
-
?
ATP + a protein
ADP + a phosphoprotein
the tyrosine kinase DivL function in cell cycle and developmental regulation is mediated, at least in part, by the global response regulator CtrA, the enzyme is essential for cell viability and division
-
-
?
ATP + a protein
ADP + a phosphoprotein
photosynthesis gene expression in Rhodobacter sphaeroides is controlled in part by the two-component regulatory system composed of a membrane-bound sensor kinase PrrB and a response regulator PrrA
-
-
?
ATP + a protein
ADP + a phosphoprotein
regB is part of a two-component system and encodes a sensor kinase involved in the global regulation of both anoxygenic light-dependent- and oxygenic light-independent CO2 fixation as well as anoxygenic photosystem biosynthesis
-
-
?
ATP + a protein
ADP + a phosphoprotein
enzyme is involved in chemotaxis
-
-
?
ATP + a protein
ADP + a phosphoprotein
PrrB is responsive to the removal of oxygen and functions through the response regulator PrrA. Together, prrB and prrA provide the major signal involved in synthesis of the specialized intracytoplasmic membrane, harboring components essential to the light reactions of photosynthesis. PrrB is a global regulator of photosynthesis gene expression
-
-
?
ATP + a protein
ADP + a phosphoprotein
the two-component regulatory system CzcS/CzcR is involved in transcriptional control of heavy-metal homoeostasis in Alcaligenes eutrophus
-
-
?
ATP + a protein
ADP + a phosphoprotein
Deinococcus radiodurans bacteriophytochrome functions as a light-regulated histidine kinase, which helps protect the bacterium from visible light
-
-
?
ATP + a protein
ADP + a phosphoprotein
the two-component regulatory system VanS-VanR activates a promoter used for cotranscription of the vanH, vanA, and vanX resistance genes
-
-
?
ATP + a protein
ADP + a phosphoprotein
the two-component regulatory system VanS-VanR activates a promoter used for cotranscription of the vanH, vanA, and vanX resistance genes
-
-
?
ATP + a protein
ADP + a phosphoprotein
enzyme is involved in signal transduction controlling chemotaxis
-
-
?
ATP + a protein
ADP + a phosphoprotein
enzyme is involved in chemotaxis
-
-
?
ATP + a protein
ADP + a phosphoprotein
enzyme is involved in chemotaxis
-
-
?
ATP + a protein
ADP + a phosphoprotein
enzyme is involved in early steps of competence regulation
-
-
?
ATP + CovR L-histidine
ADP + CovR N-phospho-L-histidine
-
-
-
-
?
ATP + CovR L-histidine
ADP + CovR N-phospho-L-histidine
-
-
-
-
?
ATP + DraR L-histidine
ADP + DraR N-phospho-L-histidine
-
-
-
?
ATP + DraR L-histidine
ADP + DraR N-phospho-L-histidine
autophosphorylation of DraK and subsequent phosphotransfer to its cognate response regulator protein DraR
-
-
?
ATP + DraR L-histidine
ADP + DraR N-phospho-L-histidine
-
-
-
?
ATP + DraR L-histidine
ADP + DraR N-phospho-L-histidine
autophosphorylation of DraK and subsequent phosphotransfer to its cognate response regulator protein DraR
-
-
?
ATP + histidine kinase Hik34
ADP + histidine kinase Hik34 N-phospho-L-histidine
-
histidine kinase Hik34 might negatively regulate the expression of certain heat shock genes that might by related to thermotolerance in Synechocystis
-
-
?
ATP + histidine kinase Hik34
ADP + histidine kinase Hik34 N-phospho-L-histidine
-
autophosphorylation, in vitro at physiological temperatures, but not at elevated temperatures, such as 44°C
-
-
?
ATP + histidine kinase HK2
ADP + histidine kinase HK2 N-phospho-L-histidine
-
-
-
-
?
ATP + histidine kinase HK2
ADP + histidine kinase HK2 N-phospho-L-histidine
-
-
-
-
?
ATP + PhoN protein L-histidine
ADP + PhoN protein N-phospho-L-histidine
-
-
-
-
?
ATP + PhoN protein L-histidine
ADP + PhoN protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
AtBphP1 contains a typical two-component histidine kinase domain at its C-terminus whose activity is repressed after photoconversion to Pfr
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
AtBphP2 is repressed after photoconversion to Pr
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
the two-component histidine kinase alrO117 is involved in heterocyst development
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
canonical histidine kinase activity of the transmitter domain of the ETR1 ethylene receptor from Arabidopsis is not required for signal transmission
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA1351
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA1356 is capable of inducing sporulation
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA1478
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA2291 acts as a phosphatase on the sporulation phosphorelay
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA2636
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA2644
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA3702
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA4223 is capable of inducing sporulation in Bacillus anthracis
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA5029
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinases DivJ and PleC initiate signal transduction pathways that regulate an early cell division cycle step and the gain of motility later in the Caulobacter crescentus cell cycle
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
RodK may regulate multiple temporally separated events during fruiting body formation including stimulation of early developmental gene expression, inhibition of A-signal production and inhibition of the intercellular C-signal transduction pathway
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
the gene-disrupted mutant is unable to produce normal mature fruiting bodies and produces fewer spores
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
induced by dehydration and CaCl2. NTHK2 possesses Ser/Thr kinase activity in presence of Mn2+ and histidine kinase activity in presence of Ca2+
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase CikA resets the circadian clock
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
the circadian clock-associated histidine kinase SasA is necessary for rubustness of the circadian rhythm of gene expression and involved in clock output
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
the circadian clock-associated histidine kinase SasA is necessary for rubustness of the circadian rhythm of gene expression and involved in clock output
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
in Synechocystis sp. PCC 6803 four histidine kinases, Hik16, Hik33, Hik34, and Hik41, perceive and transduce salt signals
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
in Synechocystis sp. PCC 6803 four histidine kinases, Hik16, Hik33, Hik34, and Hik41, perceive and transduce salt signals. The Hik16/Hik41 system responds only to NaCl
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
the three-component system of histidine kinases and response regulator, His16-Hik41-Rre17, acts as transducer of hyperosmotic stress
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
the two-component system of histidine kinase and response regulator, His10-Rre3, acts as transducer of hyperosmotic stress
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
the two-component system of histidine kinase and response regulator, His33-Rre31, acts as transducer of hyperosmotic stress
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
the two-component systes of histidine kinase and response regulator, His34-Rre1, acts as transducer of hyperosmotic stress
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
the two active sites of CheA homodimers exhibit large differences in their interactions with ATP
-
-
?
ATP + Spo0A L-histidine
ADP + Spo0A N-phospho-L-histidine
-
-
-
?
ATP + Spo0A L-histidine
ADP + Spo0A N-phospho-L-histidine
-
-
-
?
ATP + Spo0A-L-histidine
ADP + Spo0A-N-phospho-L-histidine
-
-
-
?
ATP + Spo0A-L-histidine
ADP + Spo0A-N-phospho-L-histidine
-
-
-
?
ATP + VicR L-histidine
ADP + VicR N-phospho-L-histidine
-
-
-
?
ATP + VicR L-histidine
ADP + VicR N-phospho-L-histidine
-
-
-
?
ATP + VicR protein L-histidine
ADP + VicR protein N-phospho-L-histidine
-
-
-
?
ATP + VicR protein L-histidine
ADP + VicR protein N-phospho-L-histidine
-
-
-
?
ATP + YycF
ADP + phospho-YycF
the formation of the division septum is necessary for YycG phosphorylation of YycF
-
-
?
ATP + YycF
ADP + phospho-YycF
a response regulator/transcription factor
-
-
?
BvgA + ATP
?
-
-
-
?
BvgA + ATP
?
the phosphorylated, purified C-terminal domain alone is sufficient for phosphotransfer to BvgA
-
-
?
BvgA + ATP
?
the cytoplasmic portion of BvgS ('BvgS)
-
-
?
BvgA + ATP
?
one hybrid histidine kinase consisting of the BvgS transmitter and HPt domains and of the EvgS receiver domain BvgS-TO-EvgS-R is able to phosphorylate BvgA but not EvgA. In contrast, the hybrid protein consisting of the BvgS transmitter and the EvgS receiver and HPt domains BvgS-T-EvgS-RO is unable to phosphorylate BvgA but efficiently phosphorylates EvgA
-
-
?
GTP + protein-L-histidine
GDP + protein N-phospho-L-histidine
the enzyme is involved the transition between the vegetative cycle and sporulation, multiple sensor histidine kinases are induced to autophosphorylate in response to sporulation specific signals in the phosphorelay, the BA2291 protein may act as a phosphatase on the sporulation phosphorelay when present at elevated levels, overview
-
-
r
GTP + protein-L-histidine
GDP + protein N-phospho-L-histidine
BA2291 is absolutely specific for guanine nucleotides in both the forward and reverse reactions, nucleotide specificity of BA2291, overview
-
-
r
GTP + protein-L-histidine
GDP + protein N-phospho-L-histidine
the enzyme is involved the transition between the vegetative cycle and sporulation, multiple sensor histidine kinases are induced to autophosphorylate in response to sporulation specific signals in the phosphorelay, the BA2291 protein may act as a phosphatase on the sporulation phosphorelay when present at elevated levels, overview
-
-
r
GTP + protein-L-histidine
GDP + protein N-phospho-L-histidine
BA2291 is absolutely specific for guanine nucleotides in both the forward and reverse reactions, nucleotide specificity of BA2291, overview
-
-
r
GTP + Spo0F L-histidine
GDP + Spo0F N-phospho-L-histidine
a protein purified from Bacillus subtilis
-
-
r
GTP + Spo0F L-histidine
GDP + Spo0F N-phospho-L-histidine
a protein purified from Bacillus subtilis
-
-
r
protein + ATP
?
autophosphorylation
-
-
?
protein + ATP
?
the cytoplasmic portion of BvgS autophosphorylates with the gamma-phosphate from [gamma-32P]ATP
-
-
?
protein + ATP
?
autophosphorylation
-
-
?
protein + ATP
?
DivL protein is homologous to the ubiquitous bacterial histidine protein kinases, it differs from previously studied members of this protein kinase family in that it contains a tyrosine residue Tyr550 in the conserved H-box instead of a histidine residue, which is the expected site of autophosphorylation. DivL is autophosphorylated on Tyr-550 in vitro, and this tyrosine residue is essential for cell viability and regulation of the cell division cycle
-
-
?
protein + ATP
?
autophosphorylation
-
-
?
protein + ATP
?
autophosphorylation
-
-
?
protein + ATP
?
autophosphorylation
-
-
?
protein + ATP
?
autophosphorylation
-
-
?
protein + ATP
?
-
autophosphorylation
-
-
?
protein + ATP
?
autophosphorylation
-
-
?
protein + ATP
?
-
autophosphorylation
-
-
?
protein + ATP
?
autophosphorylation
-
-
?
protein + ATP
?
autophosphorylation
-
-
?
protein + ATP
?
H243 is a site of autophosphorylation as well as transphosphorylation to the conserved D55 residue of response regulator OmpR
-
-
?
protein + ATP
?
autophosphorylation
-
-
?
protein + ATP
?
a model of the mechanism of FrzE phosphorylation: autophosphorylation initially occurs at a conserved His residue within the "CheA" domain and then, via an intramolecular transphosphorylation, is transferred to a conserved aspartate residue within the "CheY" domain
-
-
?
protein + ATP
?
autophosphorylation
-
-
?
protein + ATP
?
autophosphorylation
-
-
?
regulator protein OmpR + ATP
?
-
-
-
?
regulator protein OmpR + ATP
?
H243 is the a site of autophosphorylation as well as transphosphorylation to the conserved D55 residue of response regulator OmpR
-
-
?
additional information
?
-
it is proposed that VirA acts as an environmental sensor of plant-derived inducer molecules and transmits this information to the level of vir gene expression
-
-
?
additional information
?
-
it is proposed that VirA acts as an environmental sensor of plant-derived inducer molecules and transmits this information to the level of vir gene expression
-
-
?
additional information
?
-
membrane-bound sensor of plant signal molecules
-
-
?
additional information
?
-
membrane-bound sensor of plant signal molecules
-
-
?
additional information
?
-
AaHSK1 may interact with AaHOG1 at post-translational levels
-
-
?
additional information
?
-
-
AaHSK1 may interact with AaHOG1 at post-translational levels
-
-
?
additional information
?
-
AaHSK1 may interact with AaHOG1 at post-translational levels
-
-
?
additional information
?
-
AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
-
-
?
additional information
?
-
AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
-
-
?
additional information
?
-
AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
-
-
?
additional information
?
-
AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
-
-
?
additional information
?
-
AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
-
-
?
additional information
?
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AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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additional information
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AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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additional information
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AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
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additional information
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histidine kinase domain and response regulator domain form a two-component system
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additional information
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histidine kinase domain and response regulator domain form a two-component system
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additional information
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histidine kinase domain and response regulator domain form a two-component system
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additional information
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histidine kinase domain and response regulator domain form a two-component system
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additional information
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histidine kinase domain and response regulator domain form a two-component system
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additional information
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histidine kinase domain and response regulator domain form a two-component system
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additional information
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histidine kinase domain and response regulator domain form a two-component system
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additional information
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histidine kinase domain and response regulator domain form a two-component system
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additional information
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ETR1 acts as an ethylene receptor
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additional information
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ETR1 acts as an ethylene receptor
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additional information
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ETR1 acts as an ethylene receptor
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additional information
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ETR1 acts as an ethylene receptor
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additional information
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ETR1 acts as an ethylene receptor
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additional information
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ETR1 acts as an ethylene receptor
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additional information
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histidine kinases are part of two-component signal transduction systems that act to integrate environmental stimuli into a cellular response via a phosphotransfer relay mechanism, e.g. involved in stomatal guard cell response to H2O2, regulation of the physiological function, overview
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additional information
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the enzyme performs regulatory autophosphorylation
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additional information
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CKI1 interacts with proteins AHP2 and AHP3, but CKI1 is incapable of binding to cytokinins
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additional information
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CKI1 interacts with proteins AHP2 and AHP3, but CKI1 is incapable of binding to cytokinins
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additional information
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the two-component regulatory system, NtrY/NtrX is involved in nitrogen fixation and metabolism. NtrY is likely to represent the transmembrane sensor protein element in a two-component regulatory system
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additional information
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genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay
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additional information
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genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay
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additional information
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BA2291 performs GTP-dependent autophosphorylation
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additional information
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BA2291 performs GTP-dependent autophosphorylation
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additional information
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genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay
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additional information
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BA2291 performs GTP-dependent autophosphorylation
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additional information
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mediates the transfer of phosphate to the Spo0A and Spo0F sporulation regulatory proteins. Spo0F protein is a much better phosphoreceptor for this kinase than Spo0A protein in vitro
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additional information
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two-component regulatory system CssR-CssS, is required for the cell to survive the severe secretion stress caused by a combination of high-level production of the alpha-amylase AmyQ and reduced levels of the extracytoplasmic folding factor PrsA. The Css system is required to degrade misfolded exported proteins at the membrane-cell wall interface. CssS represents the first identified sensor for extracytoplasmic protein misfolding in a Gram-positive eubacterium
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additional information
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the CitST two-component system regulates the expression of the Mg-citrate transporter in Bacillus subtilis
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additional information
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mediates the transfer of phosphate to the Spo0A and Spo0F sporulation regulatory proteins
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additional information
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the enzyme is a regulator of chemotaxis
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additional information
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the enzyme is a regulator of chemotaxis
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additional information
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enzyme is responsible for regulation of subtilin biosynthesis
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additional information
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enzyme is responsible for regulation of subtilin biosynthesis
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additional information
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activation role for ResD, and to a lesser extent ResE, in global regulation of aerobic and anaerobic respiration in Bacillus subtilis
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additional information
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the N-terminal Per-ARNT-Sim domain plays a critical role in the catalytic activity of this enzyme, a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking this domain
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additional information
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the N-terminal Per-ARNT-Sim domain plays a critical role in the catalytic activity of this enzyme, a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking this domain
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additional information
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The sensor histidine kinase YycG acts in a two-component system with response regulator/transcription factor YycF in Bacillus subtilis controling the synthesis of autolysins and autolysin inhibitors, that function in cell wall remodelling and cell separation, YycG sensor histidine kinase is a component of and perceives infirmation at the division septum in growing cells constituting a positive feedback loop, that serves to co-ordinate cell division with cell wall homeostasis, overview
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additional information
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The sensor histidine kinase YycG acts in a two-component system with response regulator/transcription factor YycF in Bacillus subtilis controling the synthesis of autolysins and autolysin inhibitors, that function in cell wall remodelling and cell separation, YycG sensor histidine kinase is a component of and perceives infirmation at the division septum in growing cells constituting a positive feedback loop, that serves to co-ordinate cell division with cell wall homeostasis, overview
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additional information
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KinA performs autophosphorylation
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additional information
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KinA performs autophosphorylation
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additional information
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the enzyme performs catalytic autophosphorylation, mechanism and kinetics, overview. DesK displays a compact structure at the ATP-binding pocket: the ATP lid loop is short with no secondary structural organization and becomes ordered upon ATP loading. Sequence conservation mapping onto the molecular surface, semi-flexible protein-protein docking simulations, and structure-based point mutagenesis present a specific domain-domain geometry during autophosphorylation catalysis. In vitro, DesKC catalyzes three different reactions depending on the phosphorylation states of the partners: its own phosphorylation, phosphotransfer to DesR, and dephosphorylation of phospho-DesR. Protein-protein docking and modelling of the enzyme in autophosphorylation state, residues involved in domain-domain interaction modulate catalysis, overview
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additional information
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the enzyme performs catalytic autophosphorylation, mechanism and kinetics, overview. DesK displays a compact structure at the ATP-binding pocket: the ATP lid loop is short with no secondary structural organization and becomes ordered upon ATP loading. Sequence conservation mapping onto the molecular surface, semi-flexible protein-protein docking simulations, and structure-based point mutagenesis present a specific domain-domain geometry during autophosphorylation catalysis. In vitro, DesKC catalyzes three different reactions depending on the phosphorylation states of the partners: its own phosphorylation, phosphotransfer to DesR, and dephosphorylation of phospho-DesR. Protein-protein docking and modelling of the enzyme in autophosphorylation state, residues involved in domain-domain interaction modulate catalysis, overview
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additional information
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YycG interacts with the latter stage cell division proteins DivIB, Pbp2B and FtsL
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additional information
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YycG interacts with the latter stage cell division proteins DivIB, Pbp2B and FtsL
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additional information
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the enzyme performs catalytic autophosphorylation, mechanism and kinetics, overview. DesK displays a compact structure at the ATP-binding pocket: the ATP lid loop is short with no secondary structural organization and becomes ordered upon ATP loading. Sequence conservation mapping onto the molecular surface, semi-flexible protein-protein docking simulations, and structure-based point mutagenesis present a specific domain-domain geometry during autophosphorylation catalysis. In vitro, DesKC catalyzes three different reactions depending on the phosphorylation states of the partners: its own phosphorylation, phosphotransfer to DesR, and dephosphorylation of phospho-DesR. Protein-protein docking and modelling of the enzyme in autophosphorylation state, residues involved in domain-domain interaction modulate catalysis, overview
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additional information
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the N-terminal Per-ARNT-Sim domain plays a critical role in the catalytic activity of this enzyme, a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking this domain
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additional information
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KinA performs autophosphorylation
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additional information
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YycG interacts with the latter stage cell division proteins DivIB, Pbp2B and FtsL
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additional information
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bvgS and bvgA control the expression of the virulence-associated genes in Bordetella species by a system similar to the two-component systems used by a variety of bacterial species to respond to environmental stimuli
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additional information
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NodV and NodW proteins are members of the family of two-component regulatory systems, NodV responds to an environmental stimulus and, after signal transduction, NodW may be required to positively regulate the transcription of one or several unknown genes involved in the nodulation process
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additional information
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the enzyme is a biological oxygen sensors that restricts the expression of specific genes to hypoxic conditions
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additional information
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the enzyme is a biological oxygen sensors that restricts the expression of specific genes to hypoxic conditions
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additional information
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FixL and FixJ proteins are members of the two-component sensor/regulator family
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additional information
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upon illumination in the presence of ATP, the enzyme undergoes autophosphorylation
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additional information
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LOVHK is able to phosphotransfer to the central regulator of the GSR system in Brucella, specific interaction with its cognate response regulators
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additional information
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LOVHK is able to phosphotransfer to the central regulator of the GSR system in Brucella, specific interaction with its cognate response regulators
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additional information
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LOVHK is able to phosphotransfer to the central regulator of the GSR system in Brucella, specific interaction with its cognate response regulators
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additional information
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upon illumination in the presence of ATP, the enzyme undergoes autophosphorylation
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additional information
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autophosphorylation occurs when the ATP molecule bound to the the catalytic and ATP-binding subdomain phosphorylates the histidine residue in the dimerization/histidine phosphoacceptor subdomain. Histidine kinase dimerization implies that the directionality of the autophosphorylation reaction can proceed either in a cis (intramolecular) or in a trans (intermolecular) manner. Autophosphorylation occurs in cis in the dimer. Intramolecular interactions in the enzyme, overview. Arg321 from the alpha2 helix of the dimerization/histidine phosphoacceptor subdomain contacts Glu384, Tyr383 and the gamma phosphate from non-hydrolyzable ATP analogue AMP-PCP, closing the binding pocket
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additional information
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the two-component regulatory system irlR-irlS is involved in invasion of eukaryotic cells and heavy-metal resistance in Burkholderia pseudomallei
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additional information
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the two-component regulatory system irlR-irlS is involved in invasion of eukaryotic cells and heavy-metal resistance in Burkholderia pseudomallei
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additional information
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Cek1p phosphorylation via Sho1p does not require histidine kinase Chk1p
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additional information
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Cek1p phosphorylation via Sho1p does not require histidine kinase Chk1p
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additional information
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measurement of the enzyme's ATPase activity
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additional information
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measurement of the enzyme's ATPase activity
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additional information
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autophosphorylation of MtrB-Strep in proteoliposomes in the presence of ATP
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additional information
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Cm-ETR1 mRNA is very high in the seeds and placenta. Marked increase of Cm-ETR1 mRNA parallels climacteric ethylene production. Cm-ETR1 plays a specific role not only in ripening but also in the early development of melon fruit
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additional information
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Cm-ETR1 mRNA is very high in the seeds and placenta. Marked increase of Cm-ETR1 mRNA parallels climacteric ethylene production. Cm-ETR1 plays a specific role not only in ripening but also in the early development of melon fruit
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additional information
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the VanR B-VanS B two-component regulatory system activates a promoter located immediately downstream from the vanS B gene
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additional information
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the sensory histidine kinase acts in the two-component system with the response regulator as RR-HK17, EF1633-EF1632, in the regulation of ethanolamine utilization, which can be the sole carbon source for the organism, mechanism, overview
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additional information
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upon illumination in the presence of ATP, the enzyme undergoes autophosphorylation
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additional information
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BarA/UvrY system activated biofilm formation. UvrY resides downstream from csrA in a signaling pathway for csrB and CsrA stimulates UvrY-dependent activation of csrB expression by BarA-dependent and BarA-independent mechanisms
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additional information
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E. coli BarA-UvrY two-component system is required for efficient switching between glycolytic and gluconeogenic carbon sources
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additional information
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E. coli BarA-UvrY two-component system is required for efficient switching between glycolytic and gluconeogenic carbon sources
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additional information
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purified BarA protein is able to autophosphorylate when incubated with [gamma-(32)P]ATP but not with [alpha-(32)P]ATP or [gamma-(32)P]GTP. Phosphorylated BarA, in turn, acts as an efficient phosphoryl group donor to UvrY. BarA and UvrY constitute a new two-component system for gene regulation in Escherichia coli
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additional information
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purified BarA protein is able to autophosphorylate when incubated with [gamma-(32)P]ATP but not with [alpha-(32)P]ATP or [gamma-(32)P]GTP. Phosphorylated BarA, in turn, acts as an efficient phosphoryl group donor to UvrY. BarA and UvrY constitute a new two-component system for gene regulation in Escherichia coli
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additional information
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enzyme is involved in adaptive responses in E. coli
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additional information
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enzyme is involved in adaptive responses in E. coli
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additional information
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CpxA functions as a transmembrane sensory protein
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additional information
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EnvZ modulates expression of the ompF and ompC genes through phosphotransfer signal transduction in Escherichia coli
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additional information
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enzyme controls the osmoregulated biosynthesis of the porin proteins OmpF and OmpC
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additional information
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the enzyme plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions
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additional information
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the enzyme plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions
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additional information
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the enzyme plays an important role in coupling signals received from membrane-bound receptors to changes in the swimming behavior of the cells in order to respond appropriately to environmental signals
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additional information
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the enzyme plays an important role in coupling signals received from membrane-bound receptors to changes in the swimming behavior of the cells in order to respond appropriately to environmental signals
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additional information
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a complex of the proteins CheA (CheAL and CheAS) and CheW constitutes a functional unit that responds to the signaling state of the chemoreceptors. The autophosphorylation rate of CheAL is much greater when CheAL and CheAS are complexed with CheW. Moreover, the presence of mutant chemoreceptors that cause cells to tumble increases this rate. At wild-type levels of expression, the isolated CheAL/CheAS/CheW complex accounts for about 10% of the total number of CheAL, CheAS, and CheW molecules and exists in a 1:1:1 stoichiometry. This complex is also required for CheAL/CheAS and CheW binding to the phosphorylation substrate, CheY
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additional information
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the protein is involved in osmoregulation of OmpF and OmpC. EnvZ is considered to be an osmosensor which transmits signals across the membrane to OmpR, a transcriptional activator for ompF and ompC
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additional information
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UhpB and perhaps UhpC play both positive and negative roles in the control of uhpT transcription
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additional information
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enzyme has an enhancing effect on the transcription of phoA, primary function may not be connected to the phosphate regulon
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additional information
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RcsC is the sensor components of the two-component regulatory system which regulates expression of the slime polysaccharide colanic acid. rcs system is essential for expression of high levels of the group I capsular polysaccharide in lon+ E. coli K30
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additional information
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colanic acid capsule synthesis in Escherichia coli K-12 is regulated by RcsB and RcsC. RcsC acts as the sensor and RcsB acts as the receiver or effector to stimulate capsule synthesis from cps genes
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additional information
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the HydH/G system senses high periplasmic Zn2+ and Pb2+ concentrations and contributes to metal tolerance by activating the expression of zraP
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additional information
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narL and narX mediate nitrate induction of nitrate reductase synthesis and nitrate repression of fumarate reductase synthesis
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additional information
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enzyme is involved in signal transduction
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additional information
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either of two functionally redundant sensor proteins, NarX and NarQ, is sufficient for nitrate regulation in Escherichia coli K-12. NarQ and NarX may have subtle functional differences
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additional information
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narQ is a nitrate sensor for nitrate-dependent gene regulation in Escherichia coli
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additional information
?
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the two-component sensor-effector system KdpD /KdpE controls expression of the kdpABC operon
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additional information
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the two-component sensor-effector system KdpD /KdpE controls expression of the kdpABC operon
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additional information
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the two-component sensor-effector system KdpD /KdpE controls expression of the kdpABC operon
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additional information
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the TorS/TorR two-component system induces the expression of the tor structural operon encoding the trimethylamine N-oxide reductase respiratory system in response to substrate availability. TorS belongs to a sensor subfamily that includes a classical transmitter domain, a receiver, and a C-terminal alternative transmitter domain
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additional information
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TorS is a sensor that contains three phosphorylation sites and transphosphorylates TorR via a four-step phosphorelation, His443--Asp723--His850--Asp(TorR)
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?
additional information
?
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QseBC is a two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli strains EHEC and K-12
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additional information
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QseBC is a two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli strains EHEC and K-12
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additional information
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QseBC is a two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli strains EHEC and K-12
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additional information
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TorS mediates the induction of the tor structural genes in response to trimethylamine N-oxide
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additional information
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TorS mediates the induction of the tor structural genes in response to trimethylamine N-oxide
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?
additional information
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the two-component regulatory system DcuSR of Escherichia coli controls the expression of genes of C4-dicarboxylate metabolism in response to extracellular C4-dicarboxylates such as fumarate or succinate. The phosphoryl group of DcuS is rapidly transferred to the response regulator DcuR. Upon phosphorylation, DcuR binds specifically to dcuB promoter DNA
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additional information
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the two-component regulatory system DcuSR of Escherichia coli controls the expression of genes of C4-dicarboxylate metabolism in response to extracellular C4-dicarboxylates such as fumarate or succinate. The phosphoryl group of DcuS is rapidly transferred to the response regulator DcuR. Upon phosphorylation, DcuR binds specifically to dcuB promoter DNA
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additional information
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the genes encoding the anaerobic fumarate respiratory system are transcriptionally regulated by C4-dicarboxylates. The regulation is effected by a two-component regulatory system, DcuSR, consisting of a sensory histidine kinase DcuS and a response regulator DcuR
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additional information
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the genes encoding the anaerobic fumarate respiratory system are transcriptionally regulated by C4-dicarboxylates. The regulation is effected by a two-component regulatory system, DcuSR, consisting of a sensory histidine kinase DcuS and a response regulator DcuR
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additional information
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periplasmic loop of DcuS serves as a C4-dicarboxylate sensor. The cytosolic region of DcuS contains two domains: a central PAS domain possibly acting as a second sensory domain and a C-terminal transmitter domain
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additional information
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expression of cusC is induced by high concentrations of copper ions, the cusRS two-component signal transduction system is required for copper-induced expression of pcoE, a plasmid-borne gene from the E. coli copper resistance operon pco. The genes cusRS are also required for the copper-dependent expression of at least one chromosomal gene, designated cusC, which is allelic to the recently identified virulence gene ibeB in E. coli K1. The cus locus may comprise a copper ion efflux system
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additional information
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the antizyme is a bifunctional protein serving as both an inhibitor of polyamine biosynthesis as well as a transcriptional regulator of an as yet unknown set of genes
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?
additional information
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the antizyme is a bifunctional protein serving as both an inhibitor of polyamine biosynthesis as well as a transcriptional regulator of an as yet unknown set of genes
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?
additional information
?
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the two-component systemDpiA/DpiB is involved in regulation of plasmid inheritance
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?
additional information
?
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the two-component systemDpiA/DpiB is involved in regulation of plasmid inheritance
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?
additional information
?
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deletion of PilS results in a non-pilated phenotype
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?
additional information
?
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DcuS is the C4-dicarboxylate sensor of Escherichia coli catalyzing transmembrane sensing
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?
additional information
?
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a chemical or other stimulus is detected by the periplasmic sensor domain of a transmembrane histidine kinase sensor, which in turn relays a signal through a phosphotransfer cascade to the cognate cytoplasmic response regulator. Such systems lead ultimately to changes in gene expression or cell motility. Mechanisms of ligand binding and signal transduction through the cell membrane, overview
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?
additional information
?
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RcsC is the sensor components of the two-component regulatory system which regulates expression of the slime polysaccharide colanic acid. rcs system is essential for expression of high levels of the group I capsular polysaccharide in lon+ E. coli K30
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?
additional information
?
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the enzyme HP0244 is not only required to regulate flagellar gene expression via its cognate response regulator, HP0703, but also to generate a response to declining medium pH. Although not required for survival at pH 4.5, HP0244 is required for survival at pH 2.5, overview
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?
additional information
?
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the enzyme HP0244 is not only required to regulate flagellar gene expression via its cognate response regulator, HP0703, but also to generate a response to declining medium pH. Although not required for survival at pH 4.5, HP0244 is required for survival at pH 2.5, overview
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?
additional information
?
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the HydH/G system senses high periplasmic Zn2+ and Pb2+ concentrations and contributes to metal tolerance by activating the expression of zraP
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?
additional information
?
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enzyme is involved in regulation of the phosphate regulon
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?
additional information
?
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citrate, Na+, and oxygen exert their regulatory effects via the CitA/CitB system. In the presence of these signals, the citAB gene products induce their own synthesis. The positive autoregulation occurs via co-transcription of citAB with citS and oadGAB
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?
additional information
?
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citrate, Na+, and oxygen exert their regulatory effects via the CitA/CitB system. In the presence of these signals, the citAB gene products induce their own synthesis. The positive autoregulation occurs via co-transcription of citAB with citS and oadGAB
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?
additional information
?
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the periplasmic domain of the histidine autokinase CitA functions as a highly specific citrate receptor
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?
additional information
?
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the periplasmic domain of the histidine autokinase CitA functions as a highly specific citrate receptor
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?
additional information
?
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DNA sequences of plnB reveals that the product closely resembles members of bacterial two-component signal transduction systems. The finding that plnABCD are transcribed from a common promoter suggests that the biological role played by the bacteriocin is somehow related to the regulatory function of the two-component system located on the same operon
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additional information
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DNA sequences of plnB reveals that the product closely resembles members of bacterial two-component signal transduction systems. The finding that plnABCD are transcribed from a common promoter suggests that the biological role played by the bacteriocin is somehow related to the regulatory function of the two-component system located on the same operon
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?
additional information
?
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neither HK1 nor HK2 is able to autophosphorylate itself, HK1 is an ATP binding protein, acts as a functional kinase and phosphorylates HK2 by interacting with it, transfer of a phosphoryl group from HK2 to the response regulator TcrA
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?
additional information
?
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neither HK1 nor HK2 is able to autophosphorylate itself, HK1 is an ATP binding protein, acts as a functional kinase and phosphorylates HK2 by interacting with it, transfer of a phosphoryl group from HK2 to the response regulator TcrA
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?
additional information
?
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FrzE is a second messenger that relays information between the signaling protein FrzCD and the gliding motor
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-
?
additional information
?
-
-
no autophosphorylation of wild-type, is caused by the rate of dephosphorylation being higher than the rate of autophosphorylation
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?
additional information
?
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Myxococcus xanthus undergoes a complex starvation-induced developmental program that results in cells forming multicellular fruiting bodies by aggregating into mounds and then differentiating into spores. This developmental program involves EspA, which plays a key role in the timing of expression of genes necessary for progression of cells through the developmental program, overview
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additional information
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Myxococcus xanthus undergoes a complex starvation-induced developmental program that results in cells forming multicellular fruiting bodies by aggregating into mounds and then differentiating into spores. This developmental program involves EspA, which plays a key role in the timing of expression of genes necessary for progression of cells through the developmental program, overview
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additional information
?
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FrzE autophosphorylates the kinase domain at His-49, and phosphoryl groups are transferred to aspartate residues (Asp-52 and Asp-220) in the two receiver domains of FrzA. The FrzE receiver domain inhibits autophosphorylation of the FrzE kinase domain
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additional information
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moxY is part of the two-component regulatory system controlling methanol dehydrogenase synthesis
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additional information
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PilS/PilR is a two-component transcriptional regulatory system controlling expression of type 4 fimbriae in Pseudomonas aeruginosa. PilS is a sensor protein which when stimulated by the appropriate environmental signals activates PilR through kinase activity. PilR then activates transcription of pilA, probably by interacting with RNA polymerase containing RpoN
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additional information
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PilS/PilR is a two-component transcriptional regulatory system controlling expression of type 4 fimbriae in Pseudomonas aeruginosa. PilS is a sensor protein which when stimulated by the appropriate environmental signals activates PilR through kinase activity. PilR then activates transcription of pilA, probably by interacting with RNA polymerase containing RpoN
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additional information
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the two-component regulatory system PfeR/PfeS is involved in the expression of the ferric enterobactin receptor PfeA
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additional information
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deletion of PilS results in a non-pilated phenotype
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additional information
?
-
signal transduction mechanism in the bacteriophytochrome, overview
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additional information
?
-
-
signal transduction mechanism in the bacteriophytochrome, overview
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-
?
additional information
?
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structure-function relationship: the bacteriophytochrome possesses a histidine kinase domain and undergoes conformational changes during photoconversion, local structural changes originating in the photosensory domain modulate interactions between long, crossdomain signaling helices at the dimer interface and are transmitted to the spatially distant effector domain, thereby regulating its histidine kinase activity, overview
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additional information
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structure-function relationship: the bacteriophytochrome possesses a histidine kinase domain and undergoes conformational changes during photoconversion, local structural changes originating in the photosensory domain modulate interactions between long, crossdomain signaling helices at the dimer interface and are transmitted to the spatially distant effector domain, thereby regulating its histidine kinase activity, overview
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additional information
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A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
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additional information
?
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A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
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additional information
?
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A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
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?
additional information
?
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a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
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additional information
?
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a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
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additional information
?
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a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
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additional information
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in vitro transphosphorylation of GacS H2 domain by LadS histidine kinase. The enzyme performs autophosphorylation using ATP
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additional information
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in vitro transphosphorylation of GacS H2 domain by LadS histidine kinase. The enzyme performs autophosphorylation using ATP
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additional information
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in vitro transphosphorylation of GacS H2 domain by LadS histidine kinase. The enzyme performs autophosphorylation using ATP
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additional information
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significant number of genes are influenced directly or indirectly by the RoxSR two-component system. 173 genes are found showing reduced expression in EU58 (RoxSR mutant strain) in comparison to the wild type, whereas 84 genes are upregulated in the mutant
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additional information
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significant number of genes are influenced directly or indirectly by the RoxSR two-component system. 173 genes are found showing reduced expression in EU58 (RoxSR mutant strain) in comparison to the wild type, whereas 84 genes are upregulated in the mutant
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additional information
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The two-component system is implicated in redox signaling and cytochrome oxidase activity, in expression of the cell density-dependent gene ddcA and in bacterial colonization of plant surfaces. The RoxS/RoxR regulon includes genes involved in sugar and amino acid metabolism and the sulfur starvation response and elements of the respiratory chain (a cbb3 cytochrome oxidase, Fe-S clusters, and cytochrome c-related proteins) or genes participating in the maintenance of the redox balance. The RoxS/RoxR system controls a broad set of functions that have an influence on energy metabolism, such as formaldehyde and formate dehydrogenases.
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additional information
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The two-component system is implicated in redox signaling and cytochrome oxidase activity, in expression of the cell density-dependent gene ddcA and in bacterial colonization of plant surfaces. The RoxS/RoxR regulon includes genes involved in sugar and amino acid metabolism and the sulfur starvation response and elements of the respiratory chain (a cbb3 cytochrome oxidase, Fe-S clusters, and cytochrome c-related proteins) or genes participating in the maintenance of the redox balance. The RoxS/RoxR system controls a broad set of functions that have an influence on energy metabolism, such as formaldehyde and formate dehydrogenases.
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additional information
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significant number of genes are influenced directly or indirectly by the RoxSR two-component system. 173 genes are found showing reduced expression in EU58 (RoxSR mutant strain) in comparison to the wild type, whereas 84 genes are upregulated in the mutant
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additional information
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The two-component system is implicated in redox signaling and cytochrome oxidase activity, in expression of the cell density-dependent gene ddcA and in bacterial colonization of plant surfaces. The RoxS/RoxR regulon includes genes involved in sugar and amino acid metabolism and the sulfur starvation response and elements of the respiratory chain (a cbb3 cytochrome oxidase, Fe-S clusters, and cytochrome c-related proteins) or genes participating in the maintenance of the redox balance. The RoxS/RoxR system controls a broad set of functions that have an influence on energy metabolism, such as formaldehyde and formate dehydrogenases.
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additional information
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two-component regulatory system CopR/CopS is required for copper-inducible expression of the copper resistance operon
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additional information
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upon illumination in the presence of ATP, the enzyme undergoes autophosphorylation
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additional information
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upon illumination in the presence of ATP, the enzyme undergoes autophosphorylation
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additional information
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required for the activation of the C4-dicarboxylate transport structural gene dctA in free-living Rhizobium leguminosarum
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additional information
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the gene regulates transcription of the nifHDK operon and so limits the expression of nitrogen fixation activity to periods of low environmental concentrations of both oxygen and fixed nitrogen
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additional information
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role of the C-terminal domains in the photocycle of a light sensor histidine kinase Ppr having a photoactive yellow protein, PYP, domain as the photosensor domain, photocycles of the PYP domain of Ppr and of the full-length Ppr. The, overview
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additional information
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the two-component system regulates an osmosensing MAP kinase cascade
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additional information
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the two-component system regulates an osmosensing MAP kinase cascade
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additional information
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ompR-envZ is a two component regulatory system that plays an important role in the regulation of Vi polysaccharide synthesis in Salmonella typhi. One of the environmental signals for this regulation may be osmolarity
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additional information
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UhpB and perhaps UhpC play both positive and negative roles in the control of uhpT transcription
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additional information
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during bacterial chemotaxis, the binding of stimulatory ligands to chemoreceptors at the cell periphery leads to a response at the flagellar motor. Three proteins appear to be required for receptor-mediated control of swimming behavior, the products of the cheA, cheW, and cheY genes
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additional information
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during bacterial chemotaxis, the binding of stimulatory ligands to chemoreceptors at the cell periphery leads to a response at the flagellar motor. Three proteins appear to be required for receptor-mediated control of swimming behavior, the products of the cheA, cheW, and cheY genes
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additional information
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enzyme is required for the proper expression of the outer membrane proteins OmpC and OmpF
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additional information
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the two-component regulatory system phoP/phoQ controls Salmonella typhimurium virulence
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additional information
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the PhoP-PhoQ system exerts a master regulatory function for preventing bacterial overgrowth within fibroblasts
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additional information
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enzyme is involved in the regulation of expression of phosphoglycerate transport in Salmonella typhimurium. pgtB and pgtC genes are involved in the induction of the pgtP expression by modulating derepressor activity
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additional information
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PgtB and PgtC polypeptides modulate PgtA activity
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additional information
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enzyme is involved in regulation of the phosphate regulon
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additional information
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regulation of nitrogen fixation genes in Rhizobium meliloti is mediated by two proteins, FixL and FixJ, in response to oxygen availability, oxygen sensor
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additional information
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FixL senses an environmental signal and transduces it to FixJ, a transcriptional activator of nif and fix genes
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additional information
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genes dctB and dctD form a two-component system which responds to the presence of C4-dicarboxylates to regulate expression of a transport protein encoded by dctA
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additional information
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in free-living cells, the regulatory dctBD genes are absolutely required for the expression of the dctA gene
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additional information
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dctB-encoded protein includes a putative periplasmic N-terminal domain that senses the presence of dicarboxylates and a C-terminal cytoplasmic domain that activates the dctD-encoded protein
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additional information
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the ExoS-ChvI two-component regulatory system regulates succinoglycan production. ChvG is the sensor protein of the ChvG-ChvI two-component regulatory system
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additional information
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the ExoS-ChvI two-component regulatory system regulates succinoglycan production. ChvG is the sensor protein of the ChvG-ChvI two-component regulatory system
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additional information
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in vitro autokinase activity of recombinant truncated enzyme mutant AgrCTM5-6C in N,N-dimethyldodecylamine N-oxide proteoliposomes
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additional information
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VicK performs autophosphorylation for self-activation. VicK can also act as a phosphatase dephosphorylating phosphorylated VicR
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additional information
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VicK performs autophosphorylation for self-activation. VicK can also act as a phosphatase dephosphorylating phosphorylated VicR
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additional information
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the two-component regulatory system afsQ1/afsQ2 is involved in secondary metabolism
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additional information
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the cutR-cutS operon regulates copper metabolism in Streptomyces
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additional information
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a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase
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additional information
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a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase
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additional information
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a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase
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additional information
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the SenS/SenR system of Streptomyces reticuli regulates the expression of the redox regulator FurS, the catalase-peroxidase CpeB and the heme-binding protein HbpS. SenS/SenR also participates in sensing redox changes, mediated by HbpS. The heme-binding protein HbpS regulates the activity of the Streptomyces reticuli iron-sensing histidine kinase SenS in a redox-dependent manner, presence of SenS/SenR leads to the synthesis of extracellular redox active proteins, overview
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additional information
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SenS performs autophosphorylation. HbpS/SenS interaction analysis, overview
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additional information
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the SenS/SenR system of Streptomyces reticuli regulates the expression of the redox regulator FurS, the catalase-peroxidase CpeB and the heme-binding protein HbpS. SenS/SenR also participates in sensing redox changes, mediated by HbpS. The heme-binding protein HbpS regulates the activity of the Streptomyces reticuli iron-sensing histidine kinase SenS in a redox-dependent manner, presence of SenS/SenR leads to the synthesis of extracellular redox active proteins, overview
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additional information
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SenS performs autophosphorylation. HbpS/SenS interaction analysis, overview
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additional information
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the enzyme is involved in chemical sensing
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additional information
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interaction of Hik2 with Rre1 and RppA, usage of recombinant N-terminally MBP-tagged proteins purified from Escherichia coli expression host
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additional information
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during autophosphorylation, histidine kinases catalyze transfer of only the gamma-phosphate from an ATP molecule to their conserved histidine residue
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additional information
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autophosphorylation activity
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additional information
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autophosphorylation activity
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additional information
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histidine kinase performs autophosphorylation. The His-containing substrate domain (P1) is sequestered by interactions that depend upon P1 of the adjacent subunit. Non-hydrolyzable ATP analogues (but not ATP or ADP) release P1 from the protein core (domains P3P4P5) and increase its mobility. Autophosphorylation is possible only when the subunit with a functional P4 domain trans phosphorylates a functional P1 domain of the opposing subunit
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additional information
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the enzyme is involved in chemotaxis
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additional information
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the enzyme is involved in regulation of density-dependent expression of luminescence in Vibrio harveyi
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additional information
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the enzyme is involved in regulation of density-dependent expression of luminescence in Vibrio harveyi
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additional information
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enzyme is involved in positive regulation of synthesis of extracellular enzymes and polysaccharide in Xanthomonas campestris pathovar campestris
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additional information
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full-length His-RaxH shows autophosphorylation activities
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additional information
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full-length His-RaxH shows autophosphorylation activities
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + a protein
ADP + a phosphoprotein
ATP + CovR L-histidine
ADP + CovR N-phospho-L-histidine
ATP + DraR L-histidine
ADP + DraR N-phospho-L-histidine
ATP + histidine kinase Hik34
ADP + histidine kinase Hik34 N-phospho-L-histidine
-
histidine kinase Hik34 might negatively regulate the expression of certain heat shock genes that might by related to thermotolerance in Synechocystis
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
ATP + Spo0A L-histidine
ADP + Spo0A N-phospho-L-histidine
ATP + VicR L-histidine
ADP + VicR N-phospho-L-histidine
ATP + YycF
ADP + phospho-YycF
the formation of the division septum is necessary for YycG phosphorylation of YycF
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-
?
GTP + protein-L-histidine
GDP + protein N-phospho-L-histidine
GTP + Spo0F L-histidine
GDP + Spo0F N-phospho-L-histidine
Rcp1 + ATP
?
Cph1 is a light-regulated histidine kinase that mediates red, far-red reversible phosphorylation of the a small response regulator Rcp1
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?
additional information
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-
ArcA + ATP
?
ArcB undergoes autophosphorylation at the expense of ATP and subsequently transphosphorylates its cognate response regulator ArcA through a His to Asp to His to Asp phosphorelay pathway
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?
ArcA + ATP
?
the arcB gene encodes a sensor-regulator protein for anaerobic repression of the arc modulon
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?
ArcA + ATP
?
the ArcB and ArcA proteins constitute a two-component signal transduction system that plays a broad role in transcriptional regulation. Under anoxic or environmentally reducing conditions, the sensor kinase ArcB is stimulated to autophosphorylate at the expense of ATP and subsequently transphosphorylates the response regulator ArcA
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?
ArcA + ATP
?
phosphoryl group transfer from phosphorylated ArcB to ArcA, signal transmission occurs solely by His-Asp-His-Asp phosphorelay
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?
ATP + a protein
ADP + a phosphoprotein
the two-component sensory transduction system chvG/chvI is required for virulence of Agrobacterium tumefaciens
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?
ATP + a protein
ADP + a phosphoprotein
the two-component sensory transduction system chvG/chvI is required for virulence of Agrobacterium tumefaciens
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?
ATP + a protein
ADP + a phosphoprotein
kinase of the alternate pathway for phosphorylating the SpoOF protein
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?
ATP + a protein
ADP + a phosphoprotein
the essential two-component regulatory system yycF/yycG modulates expression of the ftsAZ operon in Bacillus subtilis
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?
ATP + a protein
ADP + a phosphoprotein
the two-component signal transduction system yycF/yycG is essential for growth of Bacillus subtilis
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?
ATP + a protein
ADP + a phosphoprotein
regulation of the levels of OmpF and OmpC is normally controlled by a multicomponent signal-transducing regulatory pair of proteins, EnvZ and OmpR. The effect RprX and RprY have on OmpF expression is mediated at the level of transcription. Thus, RprX and RprY may be interfering with the normal regulation of OmpF by OmpR and EnvZ
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?
ATP + a protein
ADP + a phosphoprotein
the tyrosine kinase DivL function in cell cycle and developmental regulation is mediated, at least in part, by the global response regulator CtrA, the enzyme is essential for cell viability and division
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?
ATP + a protein
ADP + a phosphoprotein
photosynthesis gene expression in Rhodobacter sphaeroides is controlled in part by the two-component regulatory system composed of a membrane-bound sensor kinase PrrB and a response regulator PrrA
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ATP + a protein
ADP + a phosphoprotein
regB is part of a two-component system and encodes a sensor kinase involved in the global regulation of both anoxygenic light-dependent- and oxygenic light-independent CO2 fixation as well as anoxygenic photosystem biosynthesis
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ATP + a protein
ADP + a phosphoprotein
enzyme is involved in chemotaxis
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-
?
ATP + a protein
ADP + a phosphoprotein
PrrB is responsive to the removal of oxygen and functions through the response regulator PrrA. Together, prrB and prrA provide the major signal involved in synthesis of the specialized intracytoplasmic membrane, harboring components essential to the light reactions of photosynthesis. PrrB is a global regulator of photosynthesis gene expression
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?
ATP + a protein
ADP + a phosphoprotein
the two-component regulatory system CzcS/CzcR is involved in transcriptional control of heavy-metal homoeostasis in Alcaligenes eutrophus
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?
ATP + a protein
ADP + a phosphoprotein
Deinococcus radiodurans bacteriophytochrome functions as a light-regulated histidine kinase, which helps protect the bacterium from visible light
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?
ATP + a protein
ADP + a phosphoprotein
the two-component regulatory system VanS-VanR activates a promoter used for cotranscription of the vanH, vanA, and vanX resistance genes
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?
ATP + a protein
ADP + a phosphoprotein
the two-component regulatory system VanS-VanR activates a promoter used for cotranscription of the vanH, vanA, and vanX resistance genes
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?
ATP + a protein
ADP + a phosphoprotein
enzyme is involved in signal transduction controlling chemotaxis
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?
ATP + a protein
ADP + a phosphoprotein
enzyme is involved in chemotaxis
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-
?
ATP + a protein
ADP + a phosphoprotein
enzyme is involved in chemotaxis
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-
?
ATP + a protein
ADP + a phosphoprotein
enzyme is involved in early steps of competence regulation
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-
?
ATP + CovR L-histidine
ADP + CovR N-phospho-L-histidine
-
-
-
-
?
ATP + CovR L-histidine
ADP + CovR N-phospho-L-histidine
-
-
-
-
?
ATP + DraR L-histidine
ADP + DraR N-phospho-L-histidine
-
-
-
?
ATP + DraR L-histidine
ADP + DraR N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
AtBphP1 contains a typical two-component histidine kinase domain at its C-terminus whose activity is repressed after photoconversion to Pfr
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-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
AtBphP2 is repressed after photoconversion to Pr
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-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
the two-component histidine kinase alrO117 is involved in heterocyst development
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-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
canonical histidine kinase activity of the transmitter domain of the ETR1 ethylene receptor from Arabidopsis is not required for signal transmission
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-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA1351
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-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA1356 is capable of inducing sporulation
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-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA1478
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-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA2291 acts as a phosphatase on the sporulation phosphorelay
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-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA2636
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA2644
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA3702
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA4223 is capable of inducing sporulation in Bacillus anthracis
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-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase BA5029
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-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinases DivJ and PleC initiate signal transduction pathways that regulate an early cell division cycle step and the gain of motility later in the Caulobacter crescentus cell cycle
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
RodK may regulate multiple temporally separated events during fruiting body formation including stimulation of early developmental gene expression, inhibition of A-signal production and inhibition of the intercellular C-signal transduction pathway
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
the gene-disrupted mutant is unable to produce normal mature fruiting bodies and produces fewer spores
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
induced by dehydration and CaCl2. NTHK2 possesses Ser/Thr kinase activity in presence of Mn2+ and histidine kinase activity in presence of Ca2+
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinase CikA resets the circadian clock
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
the circadian clock-associated histidine kinase SasA is necessary for rubustness of the circadian rhythm of gene expression and involved in clock output
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
the circadian clock-associated histidine kinase SasA is necessary for rubustness of the circadian rhythm of gene expression and involved in clock output
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
in Synechocystis sp. PCC 6803 four histidine kinases, Hik16, Hik33, Hik34, and Hik41, perceive and transduce salt signals
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
in Synechocystis sp. PCC 6803 four histidine kinases, Hik16, Hik33, Hik34, and Hik41, perceive and transduce salt signals. The Hik16/Hik41 system responds only to NaCl
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
the three-component system of histidine kinases and response regulator, His16-Hik41-Rre17, acts as transducer of hyperosmotic stress
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
the two-component system of histidine kinase and response regulator, His10-Rre3, acts as transducer of hyperosmotic stress
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
the two-component system of histidine kinase and response regulator, His33-Rre31, acts as transducer of hyperosmotic stress
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
the two-component systes of histidine kinase and response regulator, His34-Rre1, acts as transducer of hyperosmotic stress
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
ATP + Spo0A L-histidine
ADP + Spo0A N-phospho-L-histidine
-
-
-
?
ATP + Spo0A L-histidine
ADP + Spo0A N-phospho-L-histidine
-
-
-
?
ATP + VicR L-histidine
ADP + VicR N-phospho-L-histidine
-
-
-
?
ATP + VicR L-histidine
ADP + VicR N-phospho-L-histidine
-
-
-
?
GTP + protein-L-histidine
GDP + protein N-phospho-L-histidine
the enzyme is involved the transition between the vegetative cycle and sporulation, multiple sensor histidine kinases are induced to autophosphorylate in response to sporulation specific signals in the phosphorelay, the BA2291 protein may act as a phosphatase on the sporulation phosphorelay when present at elevated levels, overview
-
-
r
GTP + protein-L-histidine
GDP + protein N-phospho-L-histidine
the enzyme is involved the transition between the vegetative cycle and sporulation, multiple sensor histidine kinases are induced to autophosphorylate in response to sporulation specific signals in the phosphorelay, the BA2291 protein may act as a phosphatase on the sporulation phosphorelay when present at elevated levels, overview
-
-
r
GTP + Spo0F L-histidine
GDP + Spo0F N-phospho-L-histidine
a protein purified from Bacillus subtilis
-
-
r
GTP + Spo0F L-histidine
GDP + Spo0F N-phospho-L-histidine
a protein purified from Bacillus subtilis
-
-
r
additional information
?
-
it is proposed that VirA acts as an environmental sensor of plant-derived inducer molecules and transmits this information to the level of vir gene expression
-
-
?
additional information
?
-
it is proposed that VirA acts as an environmental sensor of plant-derived inducer molecules and transmits this information to the level of vir gene expression
-
-
?
additional information
?
-
membrane-bound sensor of plant signal molecules
-
-
?
additional information
?
-
membrane-bound sensor of plant signal molecules
-
-
?
additional information
?
-
AaHSK1 may interact with AaHOG1 at post-translational levels
-
-
?
additional information
?
-
-
AaHSK1 may interact with AaHOG1 at post-translational levels
-
-
?
additional information
?
-
AaHSK1 may interact with AaHOG1 at post-translational levels
-
-
?
additional information
?
-
AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
-
-
?
additional information
?
-
AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
-
-
?
additional information
?
-
AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
-
-
?
additional information
?
-
AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
-
-
?
additional information
?
-
AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
-
-
?
additional information
?
-
AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
-
-
?
additional information
?
-
AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
-
-
?
additional information
?
-
-
AlHK1p is important for, but not the sole factor responsible for Alternaria longipes resistance to dicarboximide fungicides, e.g. dimethachlon, molecular basis of the fungicide resistance, overview
-
-
?
additional information
?
-
ETR1 acts as an ethylene receptor
-
-
?
additional information
?
-
ETR1 acts as an ethylene receptor
-
-
?
additional information
?
-
ETR1 acts as an ethylene receptor
-
-
?
additional information
?
-
ETR1 acts as an ethylene receptor
-
-
?
additional information
?
-
-
ETR1 acts as an ethylene receptor
-
-
?
additional information
?
-
ETR1 acts as an ethylene receptor
-
-
?
additional information
?
-
-
histidine kinases are part of two-component signal transduction systems that act to integrate environmental stimuli into a cellular response via a phosphotransfer relay mechanism, e.g. involved in stomatal guard cell response to H2O2, regulation of the physiological function, overview
-
-
?
additional information
?
-
CKI1 interacts with proteins AHP2 and AHP3, but CKI1 is incapable of binding to cytokinins
-
-
?
additional information
?
-
CKI1 interacts with proteins AHP2 and AHP3, but CKI1 is incapable of binding to cytokinins
-
-
?
additional information
?
-
the two-component regulatory system, NtrY/NtrX is involved in nitrogen fixation and metabolism. NtrY is likely to represent the transmembrane sensor protein element in a two-component regulatory system
-
-
?
additional information
?
-
genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay
-
-
?
additional information
?
-
-
genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay
-
-
?
additional information
?
-
genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay
-
-
?
additional information
?
-
two-component regulatory system CssR-CssS, is required for the cell to survive the severe secretion stress caused by a combination of high-level production of the alpha-amylase AmyQ and reduced levels of the extracytoplasmic folding factor PrsA. The Css system is required to degrade misfolded exported proteins at the membrane-cell wall interface. CssS represents the first identified sensor for extracytoplasmic protein misfolding in a Gram-positive eubacterium
-
-
?
additional information
?
-
the CitST two-component system regulates the expression of the Mg-citrate transporter in Bacillus subtilis
-
-
?
additional information
?
-
mediates the transfer of phosphate to the Spo0A and Spo0F sporulation regulatory proteins
-
-
?
additional information
?
-
the enzyme is a regulator of chemotaxis
-
-
?
additional information
?
-
-
the enzyme is a regulator of chemotaxis
-
-
?
additional information
?
-
enzyme is responsible for regulation of subtilin biosynthesis
-
-
?
additional information
?
-
enzyme is responsible for regulation of subtilin biosynthesis
-
-
?
additional information
?
-
activation role for ResD, and to a lesser extent ResE, in global regulation of aerobic and anaerobic respiration in Bacillus subtilis
-
-
?
additional information
?
-
the N-terminal Per-ARNT-Sim domain plays a critical role in the catalytic activity of this enzyme, a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking this domain
-
-
?
additional information
?
-
-
the N-terminal Per-ARNT-Sim domain plays a critical role in the catalytic activity of this enzyme, a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking this domain
-
-
?
additional information
?
-
The sensor histidine kinase YycG acts in a two-component system with response regulator/transcription factor YycF in Bacillus subtilis controling the synthesis of autolysins and autolysin inhibitors, that function in cell wall remodelling and cell separation, YycG sensor histidine kinase is a component of and perceives infirmation at the division septum in growing cells constituting a positive feedback loop, that serves to co-ordinate cell division with cell wall homeostasis, overview
-
-
?
additional information
?
-
-
The sensor histidine kinase YycG acts in a two-component system with response regulator/transcription factor YycF in Bacillus subtilis controling the synthesis of autolysins and autolysin inhibitors, that function in cell wall remodelling and cell separation, YycG sensor histidine kinase is a component of and perceives infirmation at the division septum in growing cells constituting a positive feedback loop, that serves to co-ordinate cell division with cell wall homeostasis, overview
-
-
?
additional information
?
-
the N-terminal Per-ARNT-Sim domain plays a critical role in the catalytic activity of this enzyme, a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking this domain
-
-
?
additional information
?
-
bvgS and bvgA control the expression of the virulence-associated genes in Bordetella species by a system similar to the two-component systems used by a variety of bacterial species to respond to environmental stimuli
-
-
?
additional information
?
-
NodV and NodW proteins are members of the family of two-component regulatory systems, NodV responds to an environmental stimulus and, after signal transduction, NodW may be required to positively regulate the transcription of one or several unknown genes involved in the nodulation process
-
-
?
additional information
?
-
the enzyme is a biological oxygen sensors that restricts the expression of specific genes to hypoxic conditions
-
-
?
additional information
?
-
-
the enzyme is a biological oxygen sensors that restricts the expression of specific genes to hypoxic conditions
-
-
?
additional information
?
-
FixL and FixJ proteins are members of the two-component sensor/regulator family
-
-
?
additional information
?
-
LOVHK is able to phosphotransfer to the central regulator of the GSR system in Brucella, specific interaction with its cognate response regulators
-
-
?
additional information
?
-
-
LOVHK is able to phosphotransfer to the central regulator of the GSR system in Brucella, specific interaction with its cognate response regulators
-
-
?
additional information
?
-
LOVHK is able to phosphotransfer to the central regulator of the GSR system in Brucella, specific interaction with its cognate response regulators
-
-
?
additional information
?
-
the two-component regulatory system irlR-irlS is involved in invasion of eukaryotic cells and heavy-metal resistance in Burkholderia pseudomallei
-
-
?
additional information
?
-
the two-component regulatory system irlR-irlS is involved in invasion of eukaryotic cells and heavy-metal resistance in Burkholderia pseudomallei
-
-
?
additional information
?
-
Cm-ETR1 mRNA is very high in the seeds and placenta. Marked increase of Cm-ETR1 mRNA parallels climacteric ethylene production. Cm-ETR1 plays a specific role not only in ripening but also in the early development of melon fruit
-
-
?
additional information
?
-
-
Cm-ETR1 mRNA is very high in the seeds and placenta. Marked increase of Cm-ETR1 mRNA parallels climacteric ethylene production. Cm-ETR1 plays a specific role not only in ripening but also in the early development of melon fruit
-
-
?
additional information
?
-
the VanR B-VanS B two-component regulatory system activates a promoter located immediately downstream from the vanS B gene
-
-
?
additional information
?
-
-
the sensory histidine kinase acts in the two-component system with the response regulator as RR-HK17, EF1633-EF1632, in the regulation of ethanolamine utilization, which can be the sole carbon source for the organism, mechanism, overview
-
-
?
additional information
?
-
BarA/UvrY system activated biofilm formation. UvrY resides downstream from csrA in a signaling pathway for csrB and CsrA stimulates UvrY-dependent activation of csrB expression by BarA-dependent and BarA-independent mechanisms
-
-
?
additional information
?
-
E. coli BarA-UvrY two-component system is required for efficient switching between glycolytic and gluconeogenic carbon sources
-
-
?
additional information
?
-
-
E. coli BarA-UvrY two-component system is required for efficient switching between glycolytic and gluconeogenic carbon sources
-
-
?
additional information
?
-
purified BarA protein is able to autophosphorylate when incubated with [gamma-(32)P]ATP but not with [alpha-(32)P]ATP or [gamma-(32)P]GTP. Phosphorylated BarA, in turn, acts as an efficient phosphoryl group donor to UvrY. BarA and UvrY constitute a new two-component system for gene regulation in Escherichia coli
-
-
?
additional information
?
-
-
purified BarA protein is able to autophosphorylate when incubated with [gamma-(32)P]ATP but not with [alpha-(32)P]ATP or [gamma-(32)P]GTP. Phosphorylated BarA, in turn, acts as an efficient phosphoryl group donor to UvrY. BarA and UvrY constitute a new two-component system for gene regulation in Escherichia coli
-
-
?
additional information
?
-
enzyme is involved in adaptive responses in E. coli
-
-
?
additional information
?
-
-
enzyme is involved in adaptive responses in E. coli
-
-
?
additional information
?
-
CpxA functions as a transmembrane sensory protein
-
-
?
additional information
?
-
EnvZ modulates expression of the ompF and ompC genes through phosphotransfer signal transduction in Escherichia coli
-
-
?
additional information
?
-
enzyme controls the osmoregulated biosynthesis of the porin proteins OmpF and OmpC
-
-
?
additional information
?
-
the enzyme plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions
-
-
?
additional information
?
-
-
the enzyme plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions
-
-
?
additional information
?
-
the enzyme plays an important role in coupling signals received from membrane-bound receptors to changes in the swimming behavior of the cells in order to respond appropriately to environmental signals
-
-
?
additional information
?
-
-
the enzyme plays an important role in coupling signals received from membrane-bound receptors to changes in the swimming behavior of the cells in order to respond appropriately to environmental signals
-
-
?
additional information
?
-
a complex of the proteins CheA (CheAL and CheAS) and CheW constitutes a functional unit that responds to the signaling state of the chemoreceptors. The autophosphorylation rate of CheAL is much greater when CheAL and CheAS are complexed with CheW. Moreover, the presence of mutant chemoreceptors that cause cells to tumble increases this rate. At wild-type levels of expression, the isolated CheAL/CheAS/CheW complex accounts for about 10% of the total number of CheAL, CheAS, and CheW molecules and exists in a 1:1:1 stoichiometry. This complex is also required for CheAL/CheAS and CheW binding to the phosphorylation substrate, CheY
-
-
?
additional information
?
-
the protein is involved in osmoregulation of OmpF and OmpC. EnvZ is considered to be an osmosensor which transmits signals across the membrane to OmpR, a transcriptional activator for ompF and ompC
-
-
?
additional information
?
-
UhpB and perhaps UhpC play both positive and negative roles in the control of uhpT transcription
-
-
?
additional information
?
-
enzyme has an enhancing effect on the transcription of phoA, primary function may not be connected to the phosphate regulon
-
-
?
additional information
?
-
RcsC is the sensor components of the two-component regulatory system which regulates expression of the slime polysaccharide colanic acid. rcs system is essential for expression of high levels of the group I capsular polysaccharide in lon+ E. coli K30
-
-
?
additional information
?
-
colanic acid capsule synthesis in Escherichia coli K-12 is regulated by RcsB and RcsC. RcsC acts as the sensor and RcsB acts as the receiver or effector to stimulate capsule synthesis from cps genes
-
-
?
additional information
?
-
the HydH/G system senses high periplasmic Zn2+ and Pb2+ concentrations and contributes to metal tolerance by activating the expression of zraP
-
-
?
additional information
?
-
-
narL and narX mediate nitrate induction of nitrate reductase synthesis and nitrate repression of fumarate reductase synthesis
-
-
?
additional information
?
-
enzyme is involved in signal transduction
-
-
?
additional information
?
-
either of two functionally redundant sensor proteins, NarX and NarQ, is sufficient for nitrate regulation in Escherichia coli K-12. NarQ and NarX may have subtle functional differences
-
-
?
additional information
?
-
narQ is a nitrate sensor for nitrate-dependent gene regulation in Escherichia coli
-
-
?
additional information
?
-
the two-component sensor-effector system KdpD /KdpE controls expression of the kdpABC operon
-
-
?
additional information
?
-
the two-component sensor-effector system KdpD /KdpE controls expression of the kdpABC operon
-
-
?
additional information
?
-
-
the two-component sensor-effector system KdpD /KdpE controls expression of the kdpABC operon
-
-
?
additional information
?
-
the TorS/TorR two-component system induces the expression of the tor structural operon encoding the trimethylamine N-oxide reductase respiratory system in response to substrate availability. TorS belongs to a sensor subfamily that includes a classical transmitter domain, a receiver, and a C-terminal alternative transmitter domain
-
-
?
additional information
?
-
TorS is a sensor that contains three phosphorylation sites and transphosphorylates TorR via a four-step phosphorelation, His443--Asp723--His850--Asp(TorR)
-
-
?
additional information
?
-
QseBC is a two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli strains EHEC and K-12
-
-
?
additional information
?
-
QseBC is a two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli strains EHEC and K-12
-
-
?
additional information
?
-
-
QseBC is a two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli strains EHEC and K-12
-
-
?
additional information
?
-
TorS mediates the induction of the tor structural genes in response to trimethylamine N-oxide
-
-
?
additional information
?
-
-
TorS mediates the induction of the tor structural genes in response to trimethylamine N-oxide
-
-
?
additional information
?
-
the two-component regulatory system DcuSR of Escherichia coli controls the expression of genes of C4-dicarboxylate metabolism in response to extracellular C4-dicarboxylates such as fumarate or succinate. The phosphoryl group of DcuS is rapidly transferred to the response regulator DcuR. Upon phosphorylation, DcuR binds specifically to dcuB promoter DNA
-
-
?
additional information
?
-
-
the two-component regulatory system DcuSR of Escherichia coli controls the expression of genes of C4-dicarboxylate metabolism in response to extracellular C4-dicarboxylates such as fumarate or succinate. The phosphoryl group of DcuS is rapidly transferred to the response regulator DcuR. Upon phosphorylation, DcuR binds specifically to dcuB promoter DNA
-
-
?
additional information
?
-
the genes encoding the anaerobic fumarate respiratory system are transcriptionally regulated by C4-dicarboxylates. The regulation is effected by a two-component regulatory system, DcuSR, consisting of a sensory histidine kinase DcuS and a response regulator DcuR
-
-
?
additional information
?
-
-
the genes encoding the anaerobic fumarate respiratory system are transcriptionally regulated by C4-dicarboxylates. The regulation is effected by a two-component regulatory system, DcuSR, consisting of a sensory histidine kinase DcuS and a response regulator DcuR
-
-
?
additional information
?
-
periplasmic loop of DcuS serves as a C4-dicarboxylate sensor. The cytosolic region of DcuS contains two domains: a central PAS domain possibly acting as a second sensory domain and a C-terminal transmitter domain
-
-
?
additional information
?
-
expression of cusC is induced by high concentrations of copper ions, the cusRS two-component signal transduction system is required for copper-induced expression of pcoE, a plasmid-borne gene from the E. coli copper resistance operon pco. The genes cusRS are also required for the copper-dependent expression of at least one chromosomal gene, designated cusC, which is allelic to the recently identified virulence gene ibeB in E. coli K1. The cus locus may comprise a copper ion efflux system
-
-
?
additional information
?
-
the antizyme is a bifunctional protein serving as both an inhibitor of polyamine biosynthesis as well as a transcriptional regulator of an as yet unknown set of genes
-
-
?
additional information
?
-
-
the antizyme is a bifunctional protein serving as both an inhibitor of polyamine biosynthesis as well as a transcriptional regulator of an as yet unknown set of genes
-
-
?
additional information
?
-
the two-component systemDpiA/DpiB is involved in regulation of plasmid inheritance
-
-
?
additional information
?
-
-
the two-component systemDpiA/DpiB is involved in regulation of plasmid inheritance
-
-
?
additional information
?
-
-
deletion of PilS results in a non-pilated phenotype
-
-
?
additional information
?
-
DcuS is the C4-dicarboxylate sensor of Escherichia coli catalyzing transmembrane sensing
-
-
?
additional information
?
-
a chemical or other stimulus is detected by the periplasmic sensor domain of a transmembrane histidine kinase sensor, which in turn relays a signal through a phosphotransfer cascade to the cognate cytoplasmic response regulator. Such systems lead ultimately to changes in gene expression or cell motility. Mechanisms of ligand binding and signal transduction through the cell membrane, overview
-
-
?
additional information
?
-
RcsC is the sensor components of the two-component regulatory system which regulates expression of the slime polysaccharide colanic acid. rcs system is essential for expression of high levels of the group I capsular polysaccharide in lon+ E. coli K30
-
-
?
additional information
?
-
the enzyme HP0244 is not only required to regulate flagellar gene expression via its cognate response regulator, HP0703, but also to generate a response to declining medium pH. Although not required for survival at pH 4.5, HP0244 is required for survival at pH 2.5, overview
-
-
?
additional information
?
-
-
the enzyme HP0244 is not only required to regulate flagellar gene expression via its cognate response regulator, HP0703, but also to generate a response to declining medium pH. Although not required for survival at pH 4.5, HP0244 is required for survival at pH 2.5, overview
-
-
?
additional information
?
-
the HydH/G system senses high periplasmic Zn2+ and Pb2+ concentrations and contributes to metal tolerance by activating the expression of zraP
-
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additional information
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enzyme is involved in regulation of the phosphate regulon
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additional information
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citrate, Na+, and oxygen exert their regulatory effects via the CitA/CitB system. In the presence of these signals, the citAB gene products induce their own synthesis. The positive autoregulation occurs via co-transcription of citAB with citS and oadGAB
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additional information
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citrate, Na+, and oxygen exert their regulatory effects via the CitA/CitB system. In the presence of these signals, the citAB gene products induce their own synthesis. The positive autoregulation occurs via co-transcription of citAB with citS and oadGAB
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additional information
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the periplasmic domain of the histidine autokinase CitA functions as a highly specific citrate receptor
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additional information
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the periplasmic domain of the histidine autokinase CitA functions as a highly specific citrate receptor
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additional information
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DNA sequences of plnB reveals that the product closely resembles members of bacterial two-component signal transduction systems. The finding that plnABCD are transcribed from a common promoter suggests that the biological role played by the bacteriocin is somehow related to the regulatory function of the two-component system located on the same operon
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additional information
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DNA sequences of plnB reveals that the product closely resembles members of bacterial two-component signal transduction systems. The finding that plnABCD are transcribed from a common promoter suggests that the biological role played by the bacteriocin is somehow related to the regulatory function of the two-component system located on the same operon
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additional information
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FrzE is a second messenger that relays information between the signaling protein FrzCD and the gliding motor
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additional information
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Myxococcus xanthus undergoes a complex starvation-induced developmental program that results in cells forming multicellular fruiting bodies by aggregating into mounds and then differentiating into spores. This developmental program involves EspA, which plays a key role in the timing of expression of genes necessary for progression of cells through the developmental program, overview
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additional information
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Myxococcus xanthus undergoes a complex starvation-induced developmental program that results in cells forming multicellular fruiting bodies by aggregating into mounds and then differentiating into spores. This developmental program involves EspA, which plays a key role in the timing of expression of genes necessary for progression of cells through the developmental program, overview
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additional information
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moxY is part of the two-component regulatory system controlling methanol dehydrogenase synthesis
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additional information
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PilS/PilR is a two-component transcriptional regulatory system controlling expression of type 4 fimbriae in Pseudomonas aeruginosa. PilS is a sensor protein which when stimulated by the appropriate environmental signals activates PilR through kinase activity. PilR then activates transcription of pilA, probably by interacting with RNA polymerase containing RpoN
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additional information
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PilS/PilR is a two-component transcriptional regulatory system controlling expression of type 4 fimbriae in Pseudomonas aeruginosa. PilS is a sensor protein which when stimulated by the appropriate environmental signals activates PilR through kinase activity. PilR then activates transcription of pilA, probably by interacting with RNA polymerase containing RpoN
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additional information
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the two-component regulatory system PfeR/PfeS is involved in the expression of the ferric enterobactin receptor PfeA
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additional information
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deletion of PilS results in a non-pilated phenotype
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additional information
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signal transduction mechanism in the bacteriophytochrome, overview
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additional information
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signal transduction mechanism in the bacteriophytochrome, overview
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additional information
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A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
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additional information
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A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
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additional information
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A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
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additional information
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a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
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additional information
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a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
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additional information
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a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
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additional information
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significant number of genes are influenced directly or indirectly by the RoxSR two-component system. 173 genes are found showing reduced expression in EU58 (RoxSR mutant strain) in comparison to the wild type, whereas 84 genes are upregulated in the mutant
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additional information
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significant number of genes are influenced directly or indirectly by the RoxSR two-component system. 173 genes are found showing reduced expression in EU58 (RoxSR mutant strain) in comparison to the wild type, whereas 84 genes are upregulated in the mutant
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additional information
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The two-component system is implicated in redox signaling and cytochrome oxidase activity, in expression of the cell density-dependent gene ddcA and in bacterial colonization of plant surfaces. The RoxS/RoxR regulon includes genes involved in sugar and amino acid metabolism and the sulfur starvation response and elements of the respiratory chain (a cbb3 cytochrome oxidase, Fe-S clusters, and cytochrome c-related proteins) or genes participating in the maintenance of the redox balance. The RoxS/RoxR system controls a broad set of functions that have an influence on energy metabolism, such as formaldehyde and formate dehydrogenases.
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additional information
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The two-component system is implicated in redox signaling and cytochrome oxidase activity, in expression of the cell density-dependent gene ddcA and in bacterial colonization of plant surfaces. The RoxS/RoxR regulon includes genes involved in sugar and amino acid metabolism and the sulfur starvation response and elements of the respiratory chain (a cbb3 cytochrome oxidase, Fe-S clusters, and cytochrome c-related proteins) or genes participating in the maintenance of the redox balance. The RoxS/RoxR system controls a broad set of functions that have an influence on energy metabolism, such as formaldehyde and formate dehydrogenases.
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additional information
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significant number of genes are influenced directly or indirectly by the RoxSR two-component system. 173 genes are found showing reduced expression in EU58 (RoxSR mutant strain) in comparison to the wild type, whereas 84 genes are upregulated in the mutant
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additional information
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The two-component system is implicated in redox signaling and cytochrome oxidase activity, in expression of the cell density-dependent gene ddcA and in bacterial colonization of plant surfaces. The RoxS/RoxR regulon includes genes involved in sugar and amino acid metabolism and the sulfur starvation response and elements of the respiratory chain (a cbb3 cytochrome oxidase, Fe-S clusters, and cytochrome c-related proteins) or genes participating in the maintenance of the redox balance. The RoxS/RoxR system controls a broad set of functions that have an influence on energy metabolism, such as formaldehyde and formate dehydrogenases.
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additional information
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two-component regulatory system CopR/CopS is required for copper-inducible expression of the copper resistance operon
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required for the activation of the C4-dicarboxylate transport structural gene dctA in free-living Rhizobium leguminosarum
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the gene regulates transcription of the nifHDK operon and so limits the expression of nitrogen fixation activity to periods of low environmental concentrations of both oxygen and fixed nitrogen
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additional information
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role of the C-terminal domains in the photocycle of a light sensor histidine kinase Ppr having a photoactive yellow protein, PYP, domain as the photosensor domain, photocycles of the PYP domain of Ppr and of the full-length Ppr. The, overview
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the two-component system regulates an osmosensing MAP kinase cascade
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additional information
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the two-component system regulates an osmosensing MAP kinase cascade
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additional information
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ompR-envZ is a two component regulatory system that plays an important role in the regulation of Vi polysaccharide synthesis in Salmonella typhi. One of the environmental signals for this regulation may be osmolarity
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additional information
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UhpB and perhaps UhpC play both positive and negative roles in the control of uhpT transcription
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additional information
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during bacterial chemotaxis, the binding of stimulatory ligands to chemoreceptors at the cell periphery leads to a response at the flagellar motor. Three proteins appear to be required for receptor-mediated control of swimming behavior, the products of the cheA, cheW, and cheY genes
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during bacterial chemotaxis, the binding of stimulatory ligands to chemoreceptors at the cell periphery leads to a response at the flagellar motor. Three proteins appear to be required for receptor-mediated control of swimming behavior, the products of the cheA, cheW, and cheY genes
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enzyme is required for the proper expression of the outer membrane proteins OmpC and OmpF
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the two-component regulatory system phoP/phoQ controls Salmonella typhimurium virulence
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additional information
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the PhoP-PhoQ system exerts a master regulatory function for preventing bacterial overgrowth within fibroblasts
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enzyme is involved in the regulation of expression of phosphoglycerate transport in Salmonella typhimurium. pgtB and pgtC genes are involved in the induction of the pgtP expression by modulating derepressor activity
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PgtB and PgtC polypeptides modulate PgtA activity
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enzyme is involved in regulation of the phosphate regulon
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regulation of nitrogen fixation genes in Rhizobium meliloti is mediated by two proteins, FixL and FixJ, in response to oxygen availability, oxygen sensor
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FixL senses an environmental signal and transduces it to FixJ, a transcriptional activator of nif and fix genes
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genes dctB and dctD form a two-component system which responds to the presence of C4-dicarboxylates to regulate expression of a transport protein encoded by dctA
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in free-living cells, the regulatory dctBD genes are absolutely required for the expression of the dctA gene
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dctB-encoded protein includes a putative periplasmic N-terminal domain that senses the presence of dicarboxylates and a C-terminal cytoplasmic domain that activates the dctD-encoded protein
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the ExoS-ChvI two-component regulatory system regulates succinoglycan production. ChvG is the sensor protein of the ChvG-ChvI two-component regulatory system
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the ExoS-ChvI two-component regulatory system regulates succinoglycan production. ChvG is the sensor protein of the ChvG-ChvI two-component regulatory system
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additional information
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the two-component regulatory system afsQ1/afsQ2 is involved in secondary metabolism
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additional information
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the cutR-cutS operon regulates copper metabolism in Streptomyces
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additional information
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a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase
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additional information
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a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase
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additional information
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a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase
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additional information
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the SenS/SenR system of Streptomyces reticuli regulates the expression of the redox regulator FurS, the catalase-peroxidase CpeB and the heme-binding protein HbpS. SenS/SenR also participates in sensing redox changes, mediated by HbpS. The heme-binding protein HbpS regulates the activity of the Streptomyces reticuli iron-sensing histidine kinase SenS in a redox-dependent manner, presence of SenS/SenR leads to the synthesis of extracellular redox active proteins, overview
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additional information
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the SenS/SenR system of Streptomyces reticuli regulates the expression of the redox regulator FurS, the catalase-peroxidase CpeB and the heme-binding protein HbpS. SenS/SenR also participates in sensing redox changes, mediated by HbpS. The heme-binding protein HbpS regulates the activity of the Streptomyces reticuli iron-sensing histidine kinase SenS in a redox-dependent manner, presence of SenS/SenR leads to the synthesis of extracellular redox active proteins, overview
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the enzyme is involved in chemical sensing
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interaction of Hik2 with Rre1 and RppA, usage of recombinant N-terminally MBP-tagged proteins purified from Escherichia coli expression host
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the enzyme is involved in chemotaxis
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the enzyme is involved in regulation of density-dependent expression of luminescence in Vibrio harveyi
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additional information
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the enzyme is involved in regulation of density-dependent expression of luminescence in Vibrio harveyi
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additional information
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enzyme is involved in positive regulation of synthesis of extracellular enzymes and polysaccharide in Xanthomonas campestris pathovar campestris
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evolution
Brucella spp. genomes encode a LOV-domain-containing protein that is associated to a PAS (Per, Arnt and Sim) domain plus a HK domain (LOVHK), which belongs to the HWE family
evolution
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CheA differs from sensor histidine kinases in several ways: CheA does not contain a transmembrane domain, relying instead on P5 and CheW for interaction with transmembrane components. It has the phosphorylatable His residue on a separate domain (P1) instead of the dimerization domain (P3), and it utilizes a separate docking domain (P2) for CheY. P2 is not necessary for phosphotransfer to the response regulator CheY per se but variants lacking the P2 domain (DELTAP2) exhibit a reduced phosphotransfer rate relative to full-length CheA (CheAFL) and support a lower extent of chemotaxis. The linkers between the CheA domains play important roles in CheA activity
evolution
different structures of FimS kinase domains in strains strain ATCC 33277 and strain W83
evolution
different structures of FimS kinase domains in strains strain ATCC 33277 and strain W83. Although the production of FimR in W83 is modest, the protein still is detectable and can be functional because its amino acid sequence is almost identical to that of strain ATCC 33277, except for the alteration of one residue from serine to threonine, S209T
evolution
glycerol and manganese have a similar biofilm-promoting effect in two related Bacillus species, Bacillus licheniformis and Bacillus cereus, indicating that the biofilm-promoting effect of GM is conserved in Bacillus species
evolution
histidine kinase Shk1 is a member of the histidine kinase class III, whose members are all known to signal through the high-osmolarity glycerol mitogen-activated protein kinase
evolution
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the Arabidopsis thaliana genome encodes eight canonical HKs (AHK1-5, ETR1, ERS1, and CKI1), five canonical AHPs (AHP1-5), and one pseudo-AHP (AHP6) that carries an asparagine instead of the critical histidine residue
evolution
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the Brucella histidine kinase domain belongs to the HWE histidine kinase family. The HWE HK domains are present in LOV-HKs and bacteriophytochromes among other proteins
evolution
the class I enzyme DesK belongs to the HK family HPK7, which includes the nitrogen metabolism regulators NarX/Q and the antibiotic sensor LiaS among other important sensor kinases
evolution
the CusS histidine kinase has overall sequence identity to putative metal-sensing HKs such as SilS (56%), CopS (42%), PcoS (38%) and CinS (35%)
evolution
while the GacS/GacA two-component system is widely distributed throughout the bacterial kingdom, the molecular switch formed by the hybrid LadS, PA1611 and RetS histifine kinases is unique to the Pseudomonas species, though it can function in very different ways in phylogenetically related Pseudomonas species
evolution
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Brucella spp. genomes encode a LOV-domain-containing protein that is associated to a PAS (Per, Arnt and Sim) domain plus a HK domain (LOVHK), which belongs to the HWE family
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evolution
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the class I enzyme DesK belongs to the HK family HPK7, which includes the nitrogen metabolism regulators NarX/Q and the antibiotic sensor LiaS among other important sensor kinases
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evolution
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histidine kinase Shk1 is a member of the histidine kinase class III, whose members are all known to signal through the high-osmolarity glycerol mitogen-activated protein kinase
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evolution
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different structures of FimS kinase domains in strains strain ATCC 33277 and strain W83. Although the production of FimR in W83 is modest, the protein still is detectable and can be functional because its amino acid sequence is almost identical to that of strain ATCC 33277, except for the alteration of one residue from serine to threonine, S209T
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evolution
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different structures of FimS kinase domains in strains strain ATCC 33277 and strain W83
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malfunction
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Arabidopsis mutants lacking HK5 show reduced stomatal closure in response to H2O2, overexpression of HK5 results in constitutively less stomatal closure
malfunction
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genetic modifications of cytokinin-independent1 activity in Arabidopsis cause dysfunction of the two-component signaling pathway and defects in procambial cell maintenance, loss-of-function histidine kinase2 and histidine kinase3 mutants show defects in procambium proliferation and an absence of secondary growth
malfunction
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HP0244 deletion abolishes urease activation and assembly, impairs cytoplasmic and periplasmic pH homeostasis, and depolarizes the cells, with an about 7-log loss of survival at pH 2.5, even in 10 mM urea
malfunction
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a group A streptococci strain selectively deficient in CovS phosphatase activity has a distinct transcriptome relative to that of its parental strain. Inactivation of CovS in the serotype M1 background results in a greater decrease in phosphorylated CovR levels and a greater increase in the transcript levels of CovR-repressed genes than does CovS inactivation in a serotype M3 strain
malfunction
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a group A streptococci strain selectively deficient in CovS phosphatase activity has a distinct transcriptome relative to that of its parental strain. Inactivation of CovS in the serotype M1 background results in a greater decrease in phosphorylated CovR levels and a greater increase in the transcript levels of CovR-repressed genes than does CovS inactivation in a serotype M3 strain
malfunction
binK mutants exhibit a colonization advantage in a global genetic screen, phenotype, overview. Bacterial biofilm aggregates in the host are larger in strains lacking BinK, whereas overexpression of BinK suppresses biofilm formation and squid colonization
malfunction
DeltaHik34 mutant cells are resistant to heat stress within its first hours, they cannot recover after 24 h long high temperature treatment, while the wild-type cell population is able to recover after 24 h of cultivation at 44°C. The damage caused by high temperature depends on many factors, which differ in these experiments: light intensity, CO2 content, the growth stage, or the growth temperature before heat stress. In DELTAHik34 mutant, the content of all pigments starts to decrease after 6 h of heat stress. Heat stress phenotypes, overview
malfunction
disruption of Shk1 results in resistance to phenylpyrrole and dicarboximide fungicides and increases sensitivity to hyperosmotic stress and H2O2-induced oxidative stress. The Shk1 mutant shows a significant reduction in vegetative hyphal growth and is unable to produce sclerotia. The Shk1 mutant shows no change in virulence. All the defects are restored by genetic complementation of the Shk1 deletion mutant with the wild-type Shk1 gene
malfunction
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ectopic CKI1 expression generates non-propagating seeds with dual fertilized endosperms and no embryos. CKI1 loss-of-function mutants exhibit gametophytic defects resulting in semi-sterility. Cell specification is defective in cki1 mutant embryo sacs. Autonomous endosperms arise from ectopic central cells in the PRC2 fis2 (fertilization independent 2) mutant
malfunction
enzyme FimS from W83 is malfunctional. Complementation analysis with chimeric fimS constructs reveals that W83 FimS has a defective kinase domain due to a truncated conserved G3 box motif that provides an ATP-binding pocket. The introduction of the functional fimS from strain ATCC 33277 restores the production, but not polymerization, of endogenous FimA subunits in W83. But even the fimbria-deficient strain W83 retains the ability to polymerize FimA from strain ATCC 33277, indicating the assembly of mature FimA by a primary structure-dependent mechanism. Strain ATCC 33277 FimS-induced W83 FimA is a mature polypeptide and is localized on the cell surface
malfunction
gacS or gacA mutations are epistasic to ladS mutation
malfunction
group B streptococci deficient in RgfC expression exhibit increased virulence, deletion of rgfC in group B streptococci strains lacking a functional RgfA increased systemic infection. Infection with the rgfC mutant increases induction of proinflammatory signaling pathways in vivo. 19 phosphopeptides corresponding to 12 proteins are differentially phosphorylated at aspartate, cysteine, serine, threonine, or tyrosine residues in the rgfC mutant. This includes aspartate phosphorylation of a tyrosine kinase, CpsD, and a transcriptional regulator. Over 200 genes show altered expression compared to the isogenic wild-type strain and included transcriptional regulators, transporters, and genes previously associated with group B streptococci pathogenesis. In the absence of RgfA, nonspecific RgfC signaling affects the expression of virulence factors and GBS pathogenesis. Sialic acid levels are higher in the DELTArgfCAd mutant than in wild-type A909, correlated with an increase in gene expression of the capsular polysaccharide operon. Sialylation of the group B streptococci capsular polysaccharide is critical for group B streptococci bloodstream infections and pathogenesis
malfunction
Hik2 mutants are not viable
malfunction
impairment of the AaHSK1 gene does not reduce radial growth of the resulting two null mutants (HD1 and HD2) in the presence of tert-butyl-hydroxyperoxide, H2O2, KCl or NaCl, compared to the wild-type. Expression of a functional copy of the AaHSK1 gene in the HD1 null mutant fully restores the altered phenotypes. Deletion of AaHSK1 affects AaHOG1 phosphorylation. Fungal mutants impaired in AaHSK1, AaHOG1, AaAP1 (encoding a redox-responsive transcription factor) or AaFUS3 (encoding a MAP kinase) are all hypersensitive to 2-chloro-5-hydroxypyridine or 2,3,5-triiodobenzoic acid. Glucose enhances AaHOG1 phosphorylation and nuclear localization in the AaHSK1 deficient background. Genetic disruption of the AaHSK1 gene yields fungal strains that are insensitive to dicarboximide (iprodione and vinclozolin) and phenylpyrrole (fludioxonil) fungicides. Inactivation of the AaHSK1 or AaHOG1 gene does not alter the production of host-selective ACT toxin by Alternaria alternata
malfunction
in contrast to the wild-type strain, which forms mature pigmented perithecia, only an insignificant number of small unpigmented mutant fruiting bodies are observed in the dcc-1 deletion mutant, thus deletion of dcc-1 leads to sterility. Supplementation with cAMP does not restore the sexual defects (formation of submerged perithecia) of the DELTAdcc-1 mutant
malfunction
in the absence of LOVHK the expression of the virB operon is downregulated. LOVHK plays a role in the intracellular survival of Brucella, since deletion of this gene in Brucella abortus shows an attenuated phenotype in cell-culture infection assays. PhyR expression is decreased in the lovhk mutant
malfunction
loss of function of AHK5 also confers tolerance to high salinity, suggesting that AHK5 acts to integrate multiple stress responses. The AHK5 mutant is more resistant to salt stress, the insensitivity of the ahk5-1 mutant in response to salinity is caused by loss of AHK5 function
malfunction
mutations in the DHp domain affect kinase activity
malfunction
N-terminal truncations of YycG lose negative regulation of their activity, phenotypes, overview. Truncated YycG constructs fail to co-immunoprecipitate with the regulatory proteins YycH and YycI. Deletion or depletion of later stage cell division proteins does not perturb YycG localization
malfunction
removal of the HAMP or the PAS domain from Hik33n-SphSc and substitutions of amino acid residues in the PAS domain influence kinase activity, overview. Subdomain-deleted variants of Hik33n-SphSc show reduced activity compared to the unaltered chimera
malfunction
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residue 293 plays a central role in the altered structural specificity of the DELTA280-293 truncation, activation of VirA by phenols increases in the absence of enzyme aas 285-293. Mutations in the L domain can rescue null mutants in the R domain. Y293F substitution switches VirA from requiring two separate inputs to an OR gate, responding to both signals separately
malfunction
the DELTAkinD mutant (and less significantly the DELTAkinC mutant) has the most defective phenotype, while all other kin kinase mutants are able to respond to the addition of GM by forming robust biofilm
malfunction
the female gametophytic lethal phenotype of cki1-5 (a null mutant) can be partially rescued by IPT8 or ARR1 (a type-B Arabidopsis RR) driven by a CKI1 promoter. A mutant allele, cki1-8, is cki1-8 is a weak mutant allele with residual CKI1 expression, and can be transmitted through female gametophytes with low frequency, viable homozygous cki1-8 mutant plants that grow larger than wild-type plants, show defective megagametogenesis, and rarely set enlarged seeds. The cki1-8 mutation impairs female gametophyte development, phenotype overview. Mutant cki1-8 responds normally to cytokinin, remarkably smaller siliques are formed in cki1-8 plants than in the wild type
malfunction
the isogenic chiS mutant (ChiS-) shows less growth compared to the wild-type strain ChiS+ in the presence of mucin supplemented media. The mutant ChiS- strain also shows highly retarded motility as well as mucin layer penetration in vitro
malfunction
the wild-type strain experiences copper susceptibility at 2.75 mM CuSO4, whereas DELTAcusS mutant cells show a phenotype at lower concentrations. The growth defects observed in the DELTAcusS strain can be partially rescued by expression of intact CusS from a plasmid
malfunction
-
the isogenic chiS mutant (ChiS-) shows less growth compared to the wild-type strain ChiS+ in the presence of mucin supplemented media. The mutant ChiS- strain also shows highly retarded motility as well as mucin layer penetration in vitro
-
malfunction
-
in the absence of LOVHK the expression of the virB operon is downregulated. LOVHK plays a role in the intracellular survival of Brucella, since deletion of this gene in Brucella abortus shows an attenuated phenotype in cell-culture infection assays. PhyR expression is decreased in the lovhk mutant
-
malfunction
-
the DELTAkinD mutant (and less significantly the DELTAkinC mutant) has the most defective phenotype, while all other kin kinase mutants are able to respond to the addition of GM by forming robust biofilm
-
malfunction
-
N-terminal truncations of YycG lose negative regulation of their activity, phenotypes, overview. Truncated YycG constructs fail to co-immunoprecipitate with the regulatory proteins YycH and YycI. Deletion or depletion of later stage cell division proteins does not perturb YycG localization
-
malfunction
-
residue 293 plays a central role in the altered structural specificity of the DELTA280-293 truncation, activation of VirA by phenols increases in the absence of enzyme aas 285-293. Mutations in the L domain can rescue null mutants in the R domain. Y293F substitution switches VirA from requiring two separate inputs to an OR gate, responding to both signals separately
-
malfunction
-
disruption of Shk1 results in resistance to phenylpyrrole and dicarboximide fungicides and increases sensitivity to hyperosmotic stress and H2O2-induced oxidative stress. The Shk1 mutant shows a significant reduction in vegetative hyphal growth and is unable to produce sclerotia. The Shk1 mutant shows no change in virulence. All the defects are restored by genetic complementation of the Shk1 deletion mutant with the wild-type Shk1 gene
-
malfunction
-
mutations in the DHp domain affect kinase activity
-
malfunction
-
binK mutants exhibit a colonization advantage in a global genetic screen, phenotype, overview. Bacterial biofilm aggregates in the host are larger in strains lacking BinK, whereas overexpression of BinK suppresses biofilm formation and squid colonization
-
malfunction
-
ectopic CKI1 expression generates non-propagating seeds with dual fertilized endosperms and no embryos. CKI1 loss-of-function mutants exhibit gametophytic defects resulting in semi-sterility. Cell specification is defective in cki1 mutant embryo sacs. Autonomous endosperms arise from ectopic central cells in the PRC2 fis2 (fertilization independent 2) mutant
-
malfunction
-
the female gametophytic lethal phenotype of cki1-5 (a null mutant) can be partially rescued by IPT8 or ARR1 (a type-B Arabidopsis RR) driven by a CKI1 promoter. A mutant allele, cki1-8, is cki1-8 is a weak mutant allele with residual CKI1 expression, and can be transmitted through female gametophytes with low frequency, viable homozygous cki1-8 mutant plants that grow larger than wild-type plants, show defective megagametogenesis, and rarely set enlarged seeds. The cki1-8 mutation impairs female gametophyte development, phenotype overview. Mutant cki1-8 responds normally to cytokinin, remarkably smaller siliques are formed in cki1-8 plants than in the wild type
-
malfunction
-
loss of function of AHK5 also confers tolerance to high salinity, suggesting that AHK5 acts to integrate multiple stress responses. The AHK5 mutant is more resistant to salt stress, the insensitivity of the ahk5-1 mutant in response to salinity is caused by loss of AHK5 function
-
malfunction
-
enzyme FimS from W83 is malfunctional. Complementation analysis with chimeric fimS constructs reveals that W83 FimS has a defective kinase domain due to a truncated conserved G3 box motif that provides an ATP-binding pocket. The introduction of the functional fimS from strain ATCC 33277 restores the production, but not polymerization, of endogenous FimA subunits in W83. But even the fimbria-deficient strain W83 retains the ability to polymerize FimA from strain ATCC 33277, indicating the assembly of mature FimA by a primary structure-dependent mechanism. Strain ATCC 33277 FimS-induced W83 FimA is a mature polypeptide and is localized on the cell surface
-
malfunction
-
impairment of the AaHSK1 gene does not reduce radial growth of the resulting two null mutants (HD1 and HD2) in the presence of tert-butyl-hydroxyperoxide, H2O2, KCl or NaCl, compared to the wild-type. Expression of a functional copy of the AaHSK1 gene in the HD1 null mutant fully restores the altered phenotypes. Deletion of AaHSK1 affects AaHOG1 phosphorylation. Fungal mutants impaired in AaHSK1, AaHOG1, AaAP1 (encoding a redox-responsive transcription factor) or AaFUS3 (encoding a MAP kinase) are all hypersensitive to 2-chloro-5-hydroxypyridine or 2,3,5-triiodobenzoic acid. Glucose enhances AaHOG1 phosphorylation and nuclear localization in the AaHSK1 deficient background. Genetic disruption of the AaHSK1 gene yields fungal strains that are insensitive to dicarboximide (iprodione and vinclozolin) and phenylpyrrole (fludioxonil) fungicides. Inactivation of the AaHSK1 or AaHOG1 gene does not alter the production of host-selective ACT toxin by Alternaria alternata
-
malfunction
-
in contrast to the wild-type strain, which forms mature pigmented perithecia, only an insignificant number of small unpigmented mutant fruiting bodies are observed in the dcc-1 deletion mutant, thus deletion of dcc-1 leads to sterility. Supplementation with cAMP does not restore the sexual defects (formation of submerged perithecia) of the DELTAdcc-1 mutant
-
metabolism
-
DcuS and CitA are involved in the regulation of carboxylate metabolism
metabolism
biofilm formation depends on the synthesis of an extracellular matrix, which is indirectly regulated by the transcriptional regulator Spo0A. The activity of Spo0A depends on its phosphorylation state. Low and intermediate levels of phosphorylated Spo0A lead to induction of the epsA-O and tapA operons, which results in production of the extracellular matrix and thus biofilm formation, while at high levels, the matrix genes are repressed. The level of phosphorylated Spo0A is controlled by a network of kinases and phosphatases, which respond to environmental and physiological signals. Biofilm formation of Bacillus subtilis in LB medium is triggered by a combination of glycerol and manganese via KinD sensoring. The kinase KinD contains an extracellular domain, so called CACHE domain, for sensing small chemical molecules released from plant host during colonization. The glpK-encoded glycerol kinase and glpF encoded glycerol transport facilitator are critical in utilization of glycerol as a carbon source
metabolism
-
compared to a serotype M3 strain, serotype M1 GAS strains have high levels of phosphorylated CovR, low transcript levels of CovR-repressed genes, and strikingly different responses to environmental cues
metabolism
-
compared to a serotype M3 strain, serotype M1 GAS strains have high levels of phosphorylated CovR, low transcript levels of CovR-repressed genes, and strikingly different responses to environmental cues. Genetic inactivation of covS decreases but does not eliminate CovR phosphorylation
metabolism
five distinct sensor kinases (KinA, KinB, KinC, KinD, and KinE) have the capability of transferring a phosphoryl group into the phosphorelay to control the level of phosphorylated transcriptional regulator Spo0A present at any moment in the cell
metabolism
gene CKI1 is part of the genetic pathway consisting of CKI1, AHPs, and type-B ARRs in the regulation of female gametophyte development and vegetative growth
metabolism
-
in response to starvation, Bacillus subtilis cells differentiate into different subsets, undergoing cannibalism, biofilm formation or sporulation. These processes require a multiple component phosphorelay, wherein the master regulator Spo0A is activated upon phosphorylation by one or a combination of five histidine kinases (KinA-KinE) via two intermediate phosphotransferases, Spo0F and Spo0B. KinC controls the expression of cannibalism genes in a manner independent of surfactin andthe bacterial flotillin-like proteins FloT and FloA
metabolism
proposed signal transduction pathway for the Hik2-based two-component system in cyanobacteria, overview
metabolism
the AaHOG1-mediated pathway confers cellular resistance to salts and oxidative stress and bypasses AaHSK1. Accumulation of the AaHSK1 gene transcript is negatively regulated by AaHOG1, AaAP1 or AaFUS3. AaHOG1 is necessary for fungal pathogenicity, yet AaHSK1 is completely dispensable for pathogenicity. AaHSK1 functions in osmotic tolerance without involving AaHOG1. Relationships between the HOG1 MAP kinase and the histidine kinase in Alternaria alternata, overview
metabolism
the expression level of ohkAsp exerts different effects on the transcriptional level of genes responsible for regulation of doxorubicin/daunorubicin production, efflux system, cofactor supply and developmental genes
metabolism
the functional form of Hik2 is a higher-order oligomer such as a hexamer or octamer. The monomer, tetramer and hexamer forms of Hik2 are autokinase-active. Increased NaCl concentrations convert the active hexamer into an inactive tetramer. The action of NaCl appears to be confined to the Hik2 kinase domain
metabolism
-
the expression level of ohkAsp exerts different effects on the transcriptional level of genes responsible for regulation of doxorubicin/daunorubicin production, efflux system, cofactor supply and developmental genes
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metabolism
-
in response to starvation, Bacillus subtilis cells differentiate into different subsets, undergoing cannibalism, biofilm formation or sporulation. These processes require a multiple component phosphorelay, wherein the master regulator Spo0A is activated upon phosphorylation by one or a combination of five histidine kinases (KinA-KinE) via two intermediate phosphotransferases, Spo0F and Spo0B. KinC controls the expression of cannibalism genes in a manner independent of surfactin andthe bacterial flotillin-like proteins FloT and FloA
-
metabolism
-
biofilm formation depends on the synthesis of an extracellular matrix, which is indirectly regulated by the transcriptional regulator Spo0A. The activity of Spo0A depends on its phosphorylation state. Low and intermediate levels of phosphorylated Spo0A lead to induction of the epsA-O and tapA operons, which results in production of the extracellular matrix and thus biofilm formation, while at high levels, the matrix genes are repressed. The level of phosphorylated Spo0A is controlled by a network of kinases and phosphatases, which respond to environmental and physiological signals. Biofilm formation of Bacillus subtilis in LB medium is triggered by a combination of glycerol and manganese via KinD sensoring. The kinase KinD contains an extracellular domain, so called CACHE domain, for sensing small chemical molecules released from plant host during colonization. The glpK-encoded glycerol kinase and glpF encoded glycerol transport facilitator are critical in utilization of glycerol as a carbon source
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metabolism
-
five distinct sensor kinases (KinA, KinB, KinC, KinD, and KinE) have the capability of transferring a phosphoryl group into the phosphorelay to control the level of phosphorylated transcriptional regulator Spo0A present at any moment in the cell
-
metabolism
-
gene CKI1 is part of the genetic pathway consisting of CKI1, AHPs, and type-B ARRs in the regulation of female gametophyte development and vegetative growth
-
metabolism
-
the AaHOG1-mediated pathway confers cellular resistance to salts and oxidative stress and bypasses AaHSK1. Accumulation of the AaHSK1 gene transcript is negatively regulated by AaHOG1, AaAP1 or AaFUS3. AaHOG1 is necessary for fungal pathogenicity, yet AaHSK1 is completely dispensable for pathogenicity. AaHSK1 functions in osmotic tolerance without involving AaHOG1. Relationships between the HOG1 MAP kinase and the histidine kinase in Alternaria alternata, overview
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physiological function
-
CckA has a central role in establishing the cell cycle periodicity of CtrA activity by controlling both its phosphorylation and stability
physiological function
-
cytokinin-independent1 and Arabidopsis histidine kinase2 and 3 regulate vascular tissue development in Arabidopsis shoots, the cytokinin-independent activity of CKI1 and cytokinin-induced histidine kinase2 and histidine kinase3 are important for vascular bundle formation in Arabidopsis
physiological function
-
FixL utilizes a heme bound to an N-terminal PAS domain to detect the amount of oxygen present in the cytoplasm through direct binding
physiological function
-
functional HK5 histidine kinase is required for H2O2 responses in stomatal guard cells
physiological function
-
HHK1 regulates polar growth, sporulation, and cell wall composition
physiological function
-
histidine kinase Chk1p HK is part of a functionally similar but parallel pathway to the Sho1p-Cek1p pathway that confers resistance to the cell wall inhibitors Congo red and calcofluor white
physiological function
-
histidine kinase KinA promotes the initiation of sporulation when nutrients are limiting
physiological function
-
histidine kinase Ppr functions as a UV-red light sensor
physiological function
-
HP0244 is required for inner membrane assembly of UreA, UreB, and UreE and for urease activity
physiological function
-
KdpD regulates the expression of potassium transporters in response to osmolarity
physiological function
-
NikA is responsible for the responses to fungicides such as iprodione and fludioxonil, NikA functions as sensor upstream of the response regulators SskA and SrrA in response to fungicides
physiological function
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the AgrC receptor histidine kinase detects its autoinducing peptide ligand and generates an intracellular signal resulting in secretion of virulence factors
physiological function
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the histidine kinase SphS is involved in transcriptional activation of the phosphate (Pi)-acquisition system
physiological function
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the histidine kinase-related domain of phytochrome A controls the spectral sensitivity and the subcellular distribution of the photoreceptor
physiological function
the NIK1 gene is involved in ambruticin susceptibility
physiological function
the TorS histidine kinase activates the trimethylamine-N-oxide reductase pathway when sensing trimethylamine-N-oxide in the environment
physiological function
-
the TorS histidine kinase activates the trimethylamine-N-oxide reductase pathway when sensing trimethylamine-N-oxide in the environment
physiological function
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the VirA receiver domain is required for efficient vir gene expression, including the transcriptional induction of virG, VirA's receiver domain acts as a recruitment and/or alignment factor that increases the availability of VirG for phosphate transfer from VirA's kinase region to the VirG receiver domain
physiological function
AaHSK1 is a primary regulator for cellular resistance to sugar osmotic stress and for sensitivity to dicarboximide or phenylpyrrole fungicides. Important role of AaHSK1 in osmotic adaption, specifically to sugar osmoticants. AaHSK1 does not play an essential role in fungal pathogenicity
physiological function
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Arabidopsis thaliana endosperm formation requires the cytokinin independent 1 (CKI1) histidine kinase, an activator of the cytokinin signaling pathway, which specifies central cells and restricts egg cell fate. Seeds of flowering plants contain embryos and nutritive endosperm arising from double fertilization of two dimorphic female gametes. The key to specification of only one female gamete for endosperm formation is the regulated localization of the CKI1 histidine kinase by expression control and protein translocation. Dimorphism of the two adjacent gametes is mechanistically established in the syncytial embryo sac by spatially restricted CKI1 expression, followed by translocation of endoplasmic reticulum-localized CKI1 protein via nuclear migration. CKI1-directed specification of the endosperm precursor central cell results in seeds containing an embryo and an endosperm, mechanism, overview
physiological function
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CheA differs from sensor histidine kinases in several ways: CheA does not contain a transmembrane domain, relying instead on P5 and CheW for interaction with transmembrane components. It has the phosphorylatable His residue on a separate domain (P1) instead of the dimerization domain (P3), and it utilizes a separate docking domain (P2) for CheY. P2 is not necessary for phosphotransfer to the response regulator CheY per se but variants lacking the P2 domain (DELTAP2) exhibit a reduced phosphotransfer rate relative to full-length CheA (CheAFL) and support a lower extent of chemotaxis. The linkers between the CheA domains play important roles in CheA activity
physiological function
CusS is a prototypical periplasmic sensing histidine kinase, the histidine kinase CusS of the CusRS two-component system functions as a Ag(I)/Cu(I)-responsive sensor kinase and is essential for induction of the genes encoding the CusCFBA efflux pump. CusS has an important role in silver resistance and regulation of copper homeostasis
physiological function
cytokinin signaling is mediated by a multiple-step phosphorelay. Key components of the phosphorelay consist of the histidine kinase (HK)-type receptors, histidine phosphotransfer proteins (HP), and response regulators (RRs). Histidine kinase CKI1 acts upstream of histidine phosphotransfer proteins to regulate female gametophyte development and vegetative growth, role of AHP proteins in female gametophyte development, overview
physiological function
DesK is a sensor histidine kinase that allows Bacillus subtilis to respond to cold shock, triggering the adaptation of membrane fluidity via transcriptional control of a fatty acid desaturase. The transmembrane region can sense temperature-modulated fluidity changes of lipid bilayers, transmitting the signal toward the C-terminal cytoplasmic catalytic core of about 220 residues. The cold thermal stimulus is detected by DesK, which then interacts with its cognate response regulator, DesR, constituting a canonical two-component system, TCS
physiological function
DraK is a sensory histidine kinase involved in the differential regulation of antibiotics in Streptomyces coelicolor through the DraR/DraK two-component system
physiological function
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enzyme KinC regulates cannibalism and biofilm formation, and activates the expression of cannibalism genes in response to starvation in a manner dependent on phosphorelay. KinC activity and the membrane localization are independent of both the lipid raft marker proteins FloTA and cytoplasmic potassium concentration. KinC becomes active by forming a homotetramer via the N-terminal PAS domain
physiological function
gene VF_A0360 encodes the biofilm inhibitor kinase binK, an orphan hybrid histidine kinase that negatively regulates the Vibrio fischeri symbiotic biofilm (Syp) in vivo and in vitro. Colonization of Euprymna scolopes bobtail squid by Vibrio fischeri bacteria requires bacterial aggregation in host mucus as the symbiont transitions from a planktonic lifestyle in seawater to a biofilm-associated state in the host. Enzyme BinK acts upstream of SypG, the sigma54-dependent transcriptional regulator of the syp biofilm locus. The BinK effects are dependent on intact signaling in the RscS-Syp biofilm pathway. Enzyme BinK antagonizes the signal from RscS and serves as an integral component in Vibrio fischeri biofilm regulation. The hybrid histidine kinase BinK is a negative regulator of in vivo aggregation and squid colonization and of Syp biofilm phenotypes in culture. BinK is acting through SypG and not SypE
physiological function
Hik2 is one of three essential histidine kinases in the cyanobacterium Synechocystis sp. PCC 6803. The signal input domain of Hik2 responds to environmental Cl- concentration
physiological function
Hik2 is the cytoplasmic homologue of chloroplast sensor kinase (CSK), a protein involved in redox regulation of chloroplast gene expression during changes in light quality in plants and algae. Hik2 is the sensor that acts on Rre1 and RppA transcription factors to regulate photosynthesis genes as part of the mechanism of photosystem stoichiometry adjustment in cyanobacteria. Signaling mechanism of Hik2 and its phosphotransferase activity, overview. Hik2-based signaling pathway integrates acclimatory responses to light and salt stresses in cyanobacteria
physiological function
histidine kinase Hik33 is one of the key regulators helping Synechocystis acclimate to multiple stress conditions, Hik33 may play important roles in allowing cells to acclimate to changing environmental conditions
physiological function
histidine kinase SphS senses phosphate-deficient conditions. SphS phosphorylates its cognate response regulator, SphR, under phosphate-deficient conditions and regulates the expression of the so-called pho regulon, which includes genes for acclimation to phosphate-deficient conditions, namely genes for a periplasmic alkaline phosphatase PhoA and phosphate transporters
physiological function
in bacteria, two-component systems act as signaling systems to respond to environmental stimuli. Two-component systems generally consist of a sensor histidine kinase and a response regulator, which work together through histidyl-aspartyl phospho-relay to result in gene regulation. One of the two-component systems in Escherichia coli, CusS-CusR, is known to induce expression of cusCFBA genes under increased periplasmic Cu(I) and Ag(I) concentrations to help maintain metal ion homeostasis. CusS senses increasing metal ion concentrations and activates CusR. ATP-dependent auto-phosphorylation occurs at a conserved His residue in the kinase core. The phosphoryl group is then transferred from the histidine kinase to a conserved Asp residue on the N-terminal receiver domain of the response regulator, which in turn activates the C-terminal effector domain to mediate an adaptive response. The phosphorylated response regulator activates transcription of genes that respond to the environmental stimulus. Analysis of the molecular role of CusS in Cu(I)/Ag(I) resistance and the mechanism of CusS signal transduction in Escherichia coli, overview. In response to periplasmic Ag(I) and Cu(I), CusS upregulates the genes to express the CusCBA Cu(I)/Ag(I) efflux pump to remove excess metal ions from the cell
physiological function
in response to environmental changes, Pseudomonas aeruginosa is able to switch from a planktonic (free swimming) to a sessile (biofilm) lifestyle. The two-component system GacS/GacA activates the production of two small non-coding RNAs, RsmY and RsmZ, but four histidine kinases, RetS, GacS, LadS and PA1611, are instrumental in this process. RetS hybrid histidine kinase blocks GacS unorthodox histidine kinase autophosphorylation through the formation of a heterodimer. PA1611 hybrid histidine kinase, which is structurally related to GacS, interacts with RetS in Pseudomonas aeruginosa in a very similar manner to GacS. LadS hybrid histidine kinase phenotypically antagonizes the function of RetS by a mechanism that has never been investigated. The four sensors are found in most Pseudomonas species but their characteristics and mode of signaling may differ from one species to another. In Pseudomonas aeruginosa, LadS controls both rsmY and rsmZ gene expression and this regulation occurs through the GacS/GacA two-component system. In contrast to RetS, LadS signals through GacS/GacA without forming heterodimers, either with GacS or with RetS. Enzyme LadS is involved in a genuine phospho relay, which requires both transmitter and receiver LadS domains. LadS signaling ultimately requires the alternative histidine-phosphotransfer domain of GacS. LadS histidine kinase forms, with the GacS/GacA two-component system, a multicomponent signal transduction system with an original phosphorelay cascade, i.e. H1LadS -> D1LadS -> H2GacS -> D2GacA. This highlights an original strategy in which a unique output, i.e. the modulation of sRNA levels, is controlled by a complex multi-sensing network to fine-tune an adapted biofilm and virulence response. H1 and D1 domain involvement of the LadS hybrid histidine kinase in the LadS signaling pathway, and involvement of the H2 domain of the GacS unorthodox histidine kinase in the LadS signaling pathway, overview
physiological function
in response to environmental changes, Pseudomonas aeruginosa is able to switch from a planktonic (free swimming) to a sessile (biofilm) lifestyle. The two-component system GacS/GacA activates the production of two small non-coding RNAs, RsmY and RsmZ, but four histidine kinases, RetS, GacS, LadS and PA1611, are instrumental in this process. RetS hybrid histidine kinase blocks GacS unorthodox histidine kinase autophosphorylation through the formation of a heterodimer. PA1611 hybrid histidine kinase, which is structurally related to GacS, interacts with RetS in Pseudomonas aeruginosa in a very similar manner to GacS. LadS hybrid histidine kinase phenotypically antagonizes the function of RetS. The four sensors are found in most Pseudomonas species but their characteristics and mode of signaling may differ from one species to another. In Pseudomonas aeruginosa, LadS controls both rsmY and rsmZ gene expression and this regulation occurs through the GacS/GacA two-component system. In contrast to RetS, LadS signals through GacS/GacA without forming heterodimers, either with GacS or with RetS. Enzyme LadS is involved in a genuine phospho relay, which requires both transmitter and receiver LadS domains. LadS signaling ultimately requires the alternative histidine-phosphotransfer domain of GacS. LadS histidine kinase forms, with the GacS/GacA two-component system, a multicomponent signal transduction system with an original phosphorelay cascade, i.e. H1LadS -> D1LadS -> H2GacS -> D2GacA. This highlights an original strategy in which a unique output, i.e. the modulation of sRNA levels, is controlled by a complex multi-sensing network to fine-tune an adapted biofilm and virulence response. In vitro transphosphorylation of GacS H2 domain by LadS histidine kinase, involvement of the H2 domain of the GacS unorthodox histidine kinase in the LadS signaling pathway
physiological function
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in response to light, as part of a two-component system, the Brucella blue light-activated histidine kinase (LOV-HK) increases its autophosphorylation, modulating the virulence of this microorganism
physiological function
KinD is a principal histidine kinase for sensing the presence of GM, exclusively by its extracellular CACHE domain. A combination of glycerol and manganese promotes multicellular development by Bacillus subtilis. The strong biofilm-stimulating activity in response to the addition of a combination of glycerol and manganese is indeed due to upregulation of the matrix genes mediated mainly by the histidine kinase KinD
physiological function
LOV histidine kinase positively regulates the general stress response system and affects the virB operon expression in Brucella abortus. The Brucella genome encodes a sensor histidine kinase containing a LOV domain upstream from the kinase, LOVHK, which plays an important role in light-regulated Brucella virulence. The intracellular signaling pathway is initiated by the light sensor LOVHK, which functionally interacts with two response regulators: PhyR and LovR, constituting a functional two-component signal-transduction system. LOVHK contributes to the activation of the general stress response (GSR) system in Brucella via PhyR, the main regulator of the general stress response system, while LovR is proposed to be a phosphate-sink for LOVHK, decreasing its phosphorylation state. LOVHK plays a role in the intracellular survival of Brucella and in defense of stress induced by starvation. LOVHK signaling cascade, overview
physiological function
one of the main components of two-component systems, TCSs, is a sensor histidine kinase, which relays extracellular signals to intracellular pathways. VicK is an important sensor histidine kinase in the tooth decay pathogen Streptomyces mutans
physiological function
role of a sensor histidine kinase ChiS as an regulator in pathogenesis. The enzyme regulates the chitin utilization pathway and the associated two required factors, chitin binding protein and chitinases, like ChiA2. Enzyme ChiS is important for adherence and survival in HT-29 cells. ChiS is an important factor for utilizing mucin as a sole nutrient source. Cell adhesion, motility, and mucin penetration depends on ChiS. ChiS affects suckling mice colonization in mice and contributes in fluid accumulation as well as colonization in rabbit intestine
physiological function
the activity of transcriptional regulator Spo0A depends on its phosphorylation state. The level of phosphorylated Spo0A is controlled by a network of kinases and phosphatases, which respond to environmental and physiological signals. KinD is a principal histidine kinase responsible for sensing the presence of glycerol and manganese, which trigger biofilm formation of Bacillus subtilis in LB medium, exclusively by its extracellular CACHE sensor domain. The biofilm-promoting effect of glycerol and manganese is mediated mainly by the histidine kinase KinD
physiological function
the DraR/DraK two-component system (TCS) of Streptomyces coelicolor is involved in the differential regulation of antibiotic biosynthesis. The extracellular sensory domain of histidine kinase DraK shows a pH-dependent conformational change involved in signal transduction process of DraR/DraK TCS. At low pH, the extracellular sensory domain is more structured than that at high pH. In particular, the glutamate at position 83 is an important residue for the pH-dependent conformational change
physiological function
the DraR/DraK two-component system is involved in the differential regulation of antibiotic biosynthesis in a medium-dependent manner, the DraR/DraK two-component system plays an important role in the pH regulation of Streptomyces coelicolor growth medium. The enzyme and the DraR/DraK two-component system are essential for the recovery of the pH of Streptomyces coelicolor growth medium after acid shock, overview
physiological function
the enzyme Hik34 plays an important role in changes in transcriptome, proteome, lipidome, and photosynthesis in response to short term heat stress. Hik34 affects the expression of sets of genes under salt and osmotic stress, under normal conditions and heat stress and under oxidative stress
physiological function
The enzyme YycG is part of the two-component signal transduction system YycFG or WalRK. The YycG (WalK) sensor histidine kinase coordinates cell wall remodeling with cell division in Gram-positive bacteria by controlling the transcription of genes for autolysins and their inhibitors. The essential enzyme YycG senses cell division and is enzymatically activated by associating with the divisome at the division septum. The cytoplasmic PAS domain of this multidomain trans-membrane kinase is a determining factor translocating the kinase to the division septum. YycG activity in non-dividing cells is suppressed by its interaction with YycH and YycI and its activation is coordinated to cell division in dividing cells by specific interactions that occur within the divisome. This regulation is accomplished through its transmembrane and extra-membrane domains interacting with the membrane associated YycH and YycI proteins that do not localize to the divisome. Signaling by YycG involves later stage cell division proteins, overview
physiological function
the FimA-related gene cluster (the fim gene cluster) is positively regulated by the FimS-FimR two-component system. The assembly of mature FimA by a primary structure-dependent mechanism. FimSR is the unique and universal regulatory system that activates the fim gene cluster in a fimA genotype-independent manner
physiological function
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the globin-coupled histidine kinase, AfGcHK, is a part of the two-component signal transduction system. Activation of its sensor domain significantly increases its autophosphorylation activity, which targets the His183 residue of its functional domain. The phosphate group of phosphorylated AfGcHK is then transferred to the cognate response regulator
physiological function
the hybrid histidine kinase Arabidopsis histidine kinase 5 (AHK5) mediates stomatal responses to exogenous and endogenous signals in Arabidopsis thaliana, AHK5 integrates abiotic and biotic stimuli in stomatal guard cells through regulation of H2O2 homeostasis. Role for AHK5 in the regulation of survival following challenge by a hemi-biotrophic bacterium and a necrotrophic fungus, as well as in the growth response to salt stress. AHK5 positively regulates salt sensitivity and contributes to resistance to the bacterium Pseudomonas syringae pv. tomato DC3000 and the fungal pathogen Botrytis cinerea, detailed overview. Function of AHK5 in regulating the production of hormones and redox homeostasis. Enzyme AHK5 functions as a negative regulator of root growth inhibition mediated by abscisic acid/ethylene. AHK5 positively regulates salt-induced root growth inhibition
physiological function
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the integral membrane protein AgrC is a histidine kinase whose sensor domains interact with an autoinducing peptide, resulting in a series of downstream responses
physiological function
the two-component system comprising the sensor histidine kinase RgfC and the response regulator RgfA mediate GBS binding to extracellular matrix components, such as fibrinogen. The sensor histidine kinase RgfC is involved in gene regulation in group B streptococci and affects group B streptococcal virulence factor expression independent of its response regulator RgfA. Enzyme RgfC regulates expression of capsular polysaccharide and serine protease genes in GBS A909. RgfC functions as a nonspecific or orphan kinase in group B streptococci strains
physiological function
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Ti plasmid-encoded two-component signaling system, designated VirA and VirG, where VirA serves as the histidine autokinase antenna that phosphorylates VirG as the active transcriptional regulator. Histidine kinase VirA processes multiple small molecule host signals (phenol and sugar) and is essential for pathogenesis of Rhizobium radiobacter. A single residue can switch enzyme VirA from a functional AND logic gate to an OR gate where each of two signals activate independently. Host range preferences among natural strains of Rhizobium radiobacter correlate with these gate logic strategies. VirA, which exists in the inner membrane as a homodimer, is composed of multiple domains assigned as periplasmic (P), linker (L), kinase (K), and receiver (R). Sugar perception requires the P domain, whereas phenols require the L domain, localizing detection of these small molecules to opposite sides of the inner membrane. Importance of the integration node, specifically residue 293, as critical for signaling. In most natural isolates, including the frequently used A6 and C58 strains, the wild-type residue for 293 is tyrosine, but in strains Ag162, AB2/73, and KU12, the residue at 293 is phenylalanine. Strains A6, C58, and KU12 are wide-host-range pathogens, whereas strains Ag162 and AB2/73 show limited host ranges
physiological function
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two-component gene regulatory systems (TCSs) are a major mechanism by which bacteria respond to environmental stimuli and are critical to infectivity. The control of virulence regulator/sensor kinase (CovRS) TCS is central to the virulence of the major human pathogen group A Streptococcus (GAS). In the system, the histidine kinase CovS primarily serves to phosphorylate CovR, thereby resulting in the repression of virulence factor-encoding genes. Both CovS kinase and phosphatase activities influence the CovR phosphorylation status. Serotype M1 GAS strains have high rates of spontaneous mutations in covS during invasive GAS infection, thus providing a link between TCS molecular function and the epidemiology of deadly bacterial infections
physiological function
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two-component gene regulatory systems (TCSs) are a major mechanism by which bacteria respond to environmental stimuli and are critical to infectivity. The control of virulence regulator/sensor kinase (CovRS) TCS is central to the virulence of the major human pathogen group A Streptococcus (GAS). In the system, the histidine kinase CovS primarily serves to phosphorylate CovR, thereby resulting in the repression of virulence factor-encoding genes. Both CovS kinase and phosphatase activities influence the CovR phosphorylation status. Serotype M1 GAS strains have high rates of spontaneous mutations in covS during invasive GAS infection, thus providing a link between TCS molecular function and the epidemiology of deadly bacterial infections
physiological function
two-component histidine kinases (HKs) regulate responses to environmental stimuli in bacteria and eukaryotes, including yeasts, plants, slime moulds and filamentous fungi. Fungal histidine kinases are involved in osmotic and oxidative stress responses, hyphal development, fungicide sensitivity and virulence. The two-component histidine kinase Shk1 controls stress response, sclerotial formation and fungicide resistance in Sclerotinia sclerotiorum. The expression of SsHOG1 (the last kinase of the Hog pathway) and glycerol accumulation are regulated by the Shk1 gene, but PAK (p21-activated kinase) is not
physiological function
two-component signal transduction systems (TCSs) in bacteria perceive environmental stress and transmit the information via phosphorelay to adjust multiple cellular functions for adaptation. The EvgS/EvgA system is a TCS that confers acid resistance to Escherichia coli cells. Activation of the EvgS sensor initiates a cascade of transcription factors, EvgA, YdeO, and GadE, which induce the expression of a large group of acid resistance genes
physiological function
two-component signaling pathways are based on phosphoryl group transfer between histidine kinase and response regulator proteins and regulate environmental responses. The DCC-1 protein in Neurospora crasse protein participates in the regulation of processes such as conidiation, perithecial development, and, to a certain degree, carotenogenesis. DCC-1 exerts its effect by promoting cyclic AMP production, including GNA-3 and CR-1, thereby placing this protein within the context of a signaling pathway that operates during conidiation and sexual development. The DCC-1 histidine kinase is required for proper perithecial development, it has a significant role as a negative regulator of sporulation during vegetative growth
physiological function
CheA is a central component of the chemotaxis signal transduction pathway that allows prokaryotic cells to control their movements in response to environmental cues
physiological function
a CPR0195 null mutant makes 1000fold fewer spores than its wild-type parent and produces no detectable enterotoxin. CPR0195 functions early during sporulation, i.e., prior to production of sporulation-associated sigma factors. The CPR0195 kinase domain can autophosphorylate and phosphorylate Spo0A
physiological function
a GacS mutant devoid of the periplasmic detector domain is severely defective in biofilm formation accompanied by concomitant changes in the expression of small RNAs RsmY/Z that control activation of GacA-regulated genes. Point mutations in a putative ligand binding pocket lined by positively-charged residues originating primarily from the major loop impair biofilm formation
physiological function
a helix linking the transmembrane region with the cytoplasmic catalytic domain is involved in DesK pH sensing. This helix contains several glutamate, lysine, and arginine residues At neutral pH, the linker forms an alpha helix that is stabilized by hydrogen bonds in the i, i + 4 register and favors the kinase state. At low pH, protonation of glutamate residues breaks salt bridges, which results in helix destabilization and interruption of signaling. This mechanism inhibits unsaturated fatty acid synthesis and rigidifies the membrane when Bacillus subtilis grows in acidic conditions
physiological function
an allosteric switching mechanism may involve two autophosphorylation and two phosphotransfer reactions. The CpxR-mediated allosteric control of the autophosphorylation reaction ensures that the large-scale domain movements proceed in a coordinated way along the cycle, thus optimizing the overall catalytic efficiency
physiological function
free-standing PilZ protein PA2799 interacts directly with the histidine kinase SagS. PA2799 binds directly to the phosphoreceiver domain of SagS, and the SagS-HapZ interaction is further enhanced at elevated c-di-GMP concentration. Binding of HapZ to SagS inhibits the phosphotransfer between SagS and the downstream protein HptB in a c-di-GMP-dependent manner. HapZ impacts surface attachment and biofilm formation most likely by regulating the expression of a large number of genes
physiological function
isoform NikA is required for wild-type-like growth on Czapek-Dox medium and a normal resistance to certain oxidative stressors. A NikA mutant grows well in the presence of 1 microg/ml fludioxonil, whereas the wild-type strain is severely impaired in growth. In the presence of fludioxonil, the NikA mutant forms fluffy and often white colonies. Resting conidia of the NikA mutant retain their viability during storage at 4°C
physiological function
MHZ1 is autophosphorylated at a conserved histidine residue and can transfer the phosphoryl signal to the response regulator RR21 via the phosphotransfer proteins AHP1/2. This phosphorelay pathway is required for root ethylene responses. Ethylene receptor ERS2, via its GAF domain, physically interacts with MHZ1 and inhibits its kinase activity. MHZ1 acts at the level of ethylene perception and works together with the EIN2-mediated pathway to regulate root growth. MHZ1 overexpression enhances ethylene response in roots
physiological function
NME1 depletion impacts migration and differentiation but not proliferation in neuroblastoma cells. Candidate targets of NME1 histidine kinase activity include ENO1, GAPDH, and PKM
physiological function
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outer-membrane lipoprotein RcsF interacts with the periplasmic domain of the innermembrane-localized histidine kinase RcsC (RcsCperi). RcsCperi, when secreted to the periplasm by fusion to maltose-binding protein, titrates RcsF's activating effect. Deletions in the periplasmic domain of RcsC abolish the activation effect of RcsF
physiological function
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repression of HK1 impairs cell specification in the central endosperm transfer cell region and the development of transfer cell morphology, and consecutively defects differentiation of adjacent endosperm tissues. Concomittantly, disturbed cell plate formation and fusion are observed at the initiation of endosperm cellularization, loss of transfer cell identity, compromised cell wall biogenesis and reduced transport capacities in aberrant cells and elucidated two-component signaling and hormone pathways that are mediated by HK1. Non-canonical auxin signaling elements are predicted as direct targets of HvHK1 as the main regulatory links governing cellularization of endosperm transfer cells
physiological function
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sporangia of an HhkA deletion mutant contain many distorted or ectopically germinated spores and scarcely open to release the spores under sporangium dehiscence-inducing conditions. HhkA regulates a signal transduction pathway involved in sporangium formation, spore dormancy, and sporangium dehiscence. Genes regulated by HhkA overlap mostly with global transcriptional activator TcrA-regulated genes. The interaction between HhkA and TcrA is very weak and probably transient
physiological function
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TcsC is required for wild-type-like growth on Czapek-Dox medium and a normal resistance to certain oxidative stressors. An increased resistance to the cell wall disturbing agents Congo red and Calcofluor white is found for the TcsC mutant
physiological function
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role of a sensor histidine kinase ChiS as an regulator in pathogenesis. The enzyme regulates the chitin utilization pathway and the associated two required factors, chitin binding protein and chitinases, like ChiA2. Enzyme ChiS is important for adherence and survival in HT-29 cells. ChiS is an important factor for utilizing mucin as a sole nutrient source. Cell adhesion, motility, and mucin penetration depends on ChiS. ChiS affects suckling mice colonization in mice and contributes in fluid accumulation as well as colonization in rabbit intestine
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physiological function
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LOV histidine kinase positively regulates the general stress response system and affects the virB operon expression in Brucella abortus. The Brucella genome encodes a sensor histidine kinase containing a LOV domain upstream from the kinase, LOVHK, which plays an important role in light-regulated Brucella virulence. The intracellular signaling pathway is initiated by the light sensor LOVHK, which functionally interacts with two response regulators: PhyR and LovR, constituting a functional two-component signal-transduction system. LOVHK contributes to the activation of the general stress response (GSR) system in Brucella via PhyR, the main regulator of the general stress response system, while LovR is proposed to be a phosphate-sink for LOVHK, decreasing its phosphorylation state. LOVHK plays a role in the intracellular survival of Brucella and in defense of stress induced by starvation. LOVHK signaling cascade, overview
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physiological function
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TcsC is required for wild-type-like growth on Czapek-Dox medium and a normal resistance to certain oxidative stressors. An increased resistance to the cell wall disturbing agents Congo red and Calcofluor white is found for the TcsC mutant
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physiological function
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enzyme KinC regulates cannibalism and biofilm formation, and activates the expression of cannibalism genes in response to starvation in a manner dependent on phosphorelay. KinC activity and the membrane localization are independent of both the lipid raft marker proteins FloTA and cytoplasmic potassium concentration. KinC becomes active by forming a homotetramer via the N-terminal PAS domain
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physiological function
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KinD is a principal histidine kinase for sensing the presence of GM, exclusively by its extracellular CACHE domain. A combination of glycerol and manganese promotes multicellular development by Bacillus subtilis. The strong biofilm-stimulating activity in response to the addition of a combination of glycerol and manganese is indeed due to upregulation of the matrix genes mediated mainly by the histidine kinase KinD
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physiological function
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the activity of transcriptional regulator Spo0A depends on its phosphorylation state. The level of phosphorylated Spo0A is controlled by a network of kinases and phosphatases, which respond to environmental and physiological signals. KinD is a principal histidine kinase responsible for sensing the presence of glycerol and manganese, which trigger biofilm formation of Bacillus subtilis in LB medium, exclusively by its extracellular CACHE sensor domain. The biofilm-promoting effect of glycerol and manganese is mediated mainly by the histidine kinase KinD
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physiological function
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DesK is a sensor histidine kinase that allows Bacillus subtilis to respond to cold shock, triggering the adaptation of membrane fluidity via transcriptional control of a fatty acid desaturase. The transmembrane region can sense temperature-modulated fluidity changes of lipid bilayers, transmitting the signal toward the C-terminal cytoplasmic catalytic core of about 220 residues. The cold thermal stimulus is detected by DesK, which then interacts with its cognate response regulator, DesR, constituting a canonical two-component system, TCS
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physiological function
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a helix linking the transmembrane region with the cytoplasmic catalytic domain is involved in DesK pH sensing. This helix contains several glutamate, lysine, and arginine residues At neutral pH, the linker forms an alpha helix that is stabilized by hydrogen bonds in the i, i + 4 register and favors the kinase state. At low pH, protonation of glutamate residues breaks salt bridges, which results in helix destabilization and interruption of signaling. This mechanism inhibits unsaturated fatty acid synthesis and rigidifies the membrane when Bacillus subtilis grows in acidic conditions
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physiological function
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The enzyme YycG is part of the two-component signal transduction system YycFG or WalRK. The YycG (WalK) sensor histidine kinase coordinates cell wall remodeling with cell division in Gram-positive bacteria by controlling the transcription of genes for autolysins and their inhibitors. The essential enzyme YycG senses cell division and is enzymatically activated by associating with the divisome at the division septum. The cytoplasmic PAS domain of this multidomain trans-membrane kinase is a determining factor translocating the kinase to the division septum. YycG activity in non-dividing cells is suppressed by its interaction with YycH and YycI and its activation is coordinated to cell division in dividing cells by specific interactions that occur within the divisome. This regulation is accomplished through its transmembrane and extra-membrane domains interacting with the membrane associated YycH and YycI proteins that do not localize to the divisome. Signaling by YycG involves later stage cell division proteins, overview
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physiological function
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Ti plasmid-encoded two-component signaling system, designated VirA and VirG, where VirA serves as the histidine autokinase antenna that phosphorylates VirG as the active transcriptional regulator. Histidine kinase VirA processes multiple small molecule host signals (phenol and sugar) and is essential for pathogenesis of Rhizobium radiobacter. A single residue can switch enzyme VirA from a functional AND logic gate to an OR gate where each of two signals activate independently. Host range preferences among natural strains of Rhizobium radiobacter correlate with these gate logic strategies. VirA, which exists in the inner membrane as a homodimer, is composed of multiple domains assigned as periplasmic (P), linker (L), kinase (K), and receiver (R). Sugar perception requires the P domain, whereas phenols require the L domain, localizing detection of these small molecules to opposite sides of the inner membrane. Importance of the integration node, specifically residue 293, as critical for signaling. In most natural isolates, including the frequently used A6 and C58 strains, the wild-type residue for 293 is tyrosine, but in strains Ag162, AB2/73, and KU12, the residue at 293 is phenylalanine. Strains A6, C58, and KU12 are wide-host-range pathogens, whereas strains Ag162 and AB2/73 show limited host ranges
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physiological function
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the DraR/DraK two-component system (TCS) of Streptomyces coelicolor is involved in the differential regulation of antibiotic biosynthesis. The extracellular sensory domain of histidine kinase DraK shows a pH-dependent conformational change involved in signal transduction process of DraR/DraK TCS. At low pH, the extracellular sensory domain is more structured than that at high pH. In particular, the glutamate at position 83 is an important residue for the pH-dependent conformational change
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physiological function
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two-component histidine kinases (HKs) regulate responses to environmental stimuli in bacteria and eukaryotes, including yeasts, plants, slime moulds and filamentous fungi. Fungal histidine kinases are involved in osmotic and oxidative stress responses, hyphal development, fungicide sensitivity and virulence. The two-component histidine kinase Shk1 controls stress response, sclerotial formation and fungicide resistance in Sclerotinia sclerotiorum. The expression of SsHOG1 (the last kinase of the Hog pathway) and glycerol accumulation are regulated by the Shk1 gene, but PAK (p21-activated kinase) is not
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physiological function
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DraK is a sensory histidine kinase involved in the differential regulation of antibiotics in Streptomyces coelicolor through the DraR/DraK two-component system
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physiological function
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one of the main components of two-component systems, TCSs, is a sensor histidine kinase, which relays extracellular signals to intracellular pathways. VicK is an important sensor histidine kinase in the tooth decay pathogen Streptomyces mutans
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physiological function
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gene VF_A0360 encodes the biofilm inhibitor kinase binK, an orphan hybrid histidine kinase that negatively regulates the Vibrio fischeri symbiotic biofilm (Syp) in vivo and in vitro. Colonization of Euprymna scolopes bobtail squid by Vibrio fischeri bacteria requires bacterial aggregation in host mucus as the symbiont transitions from a planktonic lifestyle in seawater to a biofilm-associated state in the host. Enzyme BinK acts upstream of SypG, the sigma54-dependent transcriptional regulator of the syp biofilm locus. The BinK effects are dependent on intact signaling in the RscS-Syp biofilm pathway. Enzyme BinK antagonizes the signal from RscS and serves as an integral component in Vibrio fischeri biofilm regulation. The hybrid histidine kinase BinK is a negative regulator of in vivo aggregation and squid colonization and of Syp biofilm phenotypes in culture. BinK is acting through SypG and not SypE
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physiological function
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isoform NikA is required for wild-type-like growth on Czapek-Dox medium and a normal resistance to certain oxidative stressors. A NikA mutant grows well in the presence of 1 microg/ml fludioxonil, whereas the wild-type strain is severely impaired in growth. In the presence of fludioxonil, the NikA mutant forms fluffy and often white colonies. Resting conidia of the NikA mutant retain their viability during storage at 4°C
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physiological function
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Arabidopsis thaliana endosperm formation requires the cytokinin independent 1 (CKI1) histidine kinase, an activator of the cytokinin signaling pathway, which specifies central cells and restricts egg cell fate. Seeds of flowering plants contain embryos and nutritive endosperm arising from double fertilization of two dimorphic female gametes. The key to specification of only one female gamete for endosperm formation is the regulated localization of the CKI1 histidine kinase by expression control and protein translocation. Dimorphism of the two adjacent gametes is mechanistically established in the syncytial embryo sac by spatially restricted CKI1 expression, followed by translocation of endoplasmic reticulum-localized CKI1 protein via nuclear migration. CKI1-directed specification of the endosperm precursor central cell results in seeds containing an embryo and an endosperm, mechanism, overview
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physiological function
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cytokinin signaling is mediated by a multiple-step phosphorelay. Key components of the phosphorelay consist of the histidine kinase (HK)-type receptors, histidine phosphotransfer proteins (HP), and response regulators (RRs). Histidine kinase CKI1 acts upstream of histidine phosphotransfer proteins to regulate female gametophyte development and vegetative growth, role of AHP proteins in female gametophyte development, overview
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physiological function
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the hybrid histidine kinase Arabidopsis histidine kinase 5 (AHK5) mediates stomatal responses to exogenous and endogenous signals in Arabidopsis thaliana, AHK5 integrates abiotic and biotic stimuli in stomatal guard cells through regulation of H2O2 homeostasis. Role for AHK5 in the regulation of survival following challenge by a hemi-biotrophic bacterium and a necrotrophic fungus, as well as in the growth response to salt stress. AHK5 positively regulates salt sensitivity and contributes to resistance to the bacterium Pseudomonas syringae pv. tomato DC3000 and the fungal pathogen Botrytis cinerea, detailed overview. Function of AHK5 in regulating the production of hormones and redox homeostasis. Enzyme AHK5 functions as a negative regulator of root growth inhibition mediated by abscisic acid/ethylene. AHK5 positively regulates salt-induced root growth inhibition
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physiological function
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a CPR0195 null mutant makes 1000fold fewer spores than its wild-type parent and produces no detectable enterotoxin. CPR0195 functions early during sporulation, i.e., prior to production of sporulation-associated sigma factors. The CPR0195 kinase domain can autophosphorylate and phosphorylate Spo0A
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physiological function
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a GacS mutant devoid of the periplasmic detector domain is severely defective in biofilm formation accompanied by concomitant changes in the expression of small RNAs RsmY/Z that control activation of GacA-regulated genes. Point mutations in a putative ligand binding pocket lined by positively-charged residues originating primarily from the major loop impair biofilm formation
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physiological function
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NikA is responsible for the responses to fungicides such as iprodione and fludioxonil, NikA functions as sensor upstream of the response regulators SskA and SrrA in response to fungicides
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physiological function
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the DraR/DraK two-component system is involved in the differential regulation of antibiotic biosynthesis in a medium-dependent manner, the DraR/DraK two-component system plays an important role in the pH regulation of Streptomyces coelicolor growth medium. The enzyme and the DraR/DraK two-component system are essential for the recovery of the pH of Streptomyces coelicolor growth medium after acid shock, overview
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physiological function
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the TorS histidine kinase activates the trimethylamine-N-oxide reductase pathway when sensing trimethylamine-N-oxide in the environment
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physiological function
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the FimA-related gene cluster (the fim gene cluster) is positively regulated by the FimS-FimR two-component system. The assembly of mature FimA by a primary structure-dependent mechanism. FimSR is the unique and universal regulatory system that activates the fim gene cluster in a fimA genotype-independent manner
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physiological function
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AaHSK1 is a primary regulator for cellular resistance to sugar osmotic stress and for sensitivity to dicarboximide or phenylpyrrole fungicides. Important role of AaHSK1 in osmotic adaption, specifically to sugar osmoticants. AaHSK1 does not play an essential role in fungal pathogenicity
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physiological function
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two-component signaling pathways are based on phosphoryl group transfer between histidine kinase and response regulator proteins and regulate environmental responses. The DCC-1 protein in Neurospora crasse protein participates in the regulation of processes such as conidiation, perithecial development, and, to a certain degree, carotenogenesis. DCC-1 exerts its effect by promoting cyclic AMP production, including GNA-3 and CR-1, thereby placing this protein within the context of a signaling pathway that operates during conidiation and sexual development. The DCC-1 histidine kinase is required for proper perithecial development, it has a significant role as a negative regulator of sporulation during vegetative growth
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physiological function
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histidine kinase Chk1p HK is part of a functionally similar but parallel pathway to the Sho1p-Cek1p pathway that confers resistance to the cell wall inhibitors Congo red and calcofluor white
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additional information
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basic architecture of VirA/VirG histidine kinase: the membrane-embedded VirA histidine kinase contains four modular domains, and the signal inputs activate the VirG response regulator. The sugar-binding protein ChvE interacts with the periplasmic domain, and phenols interact with the linker domain. The linker is predicted to adopt a GAF fold with the alpha1 helix. The conserved His474 is located in the dimerization domain of the kinase
additional information
conserved proline-222, which is adjacent to the phosphoryl acceptor histidine, contributes to helical bending, which is essential for the autokinase and phosphatase activities. The proline is essential for phosphatase activity. The C-terminal ends of the VicK dimer harbor two monomeric catalytic domains. The enzyme architecture with a signal transducer and sensor domain suggests a model where DHp helical bending and a CA swing movement are likely coordinated for autokinase activation, structure-function analysis, overview
additional information
effect of the nonconserved flanking sequence on the signaling lifetime of LovK, the effects of structure outside the LOV core on its signaling lifetime do not combine in a simple, additive way. Kinetics of recovery from the adduct state depend not only on the buffer environment but also on the structural context in which the LOV domain is contained. Full-length LovK (residues 1-368) has a long recovery, with a half-life of 2 h, the isolated LOV core (residues 25-138) recovers more quickly, with a half-life of 37 min. LovK (25-163), which contains the LOV core and the nonconserved linker sequence at its C-terminus, has a recovery half-life of 28 min. A construct containing the LOV core and the nonconserved N-terminal flanking sequence, LovK(1-138), has a half-life of only 2 min, but this N-terminal region has not a general rate enhancement effect. LovK(1-163), a construct with fully intact N- and C-termini (but missing the kinase domain), is slower to recover than either LovK(25-138), LovK(1-138), or LovK(25-163)
additional information
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effect of the nonconserved flanking sequence on the signaling lifetime of LovK, the effects of structure outside the LOV core on its signaling lifetime do not combine in a simple, additive way. Kinetics of recovery from the adduct state depend not only on the buffer environment but also on the structural context in which the LOV domain is contained. Full-length LovK (residues 1-368) has a long recovery, with a half-life of 2 h, the isolated LOV core (residues 25-138) recovers more quickly, with a half-life of 37 min. LovK (25-163), which contains the LOV core and the nonconserved linker sequence at its C-terminus, has a recovery half-life of 28 min. A construct containing the LOV core and the nonconserved N-terminal flanking sequence, LovK(1-138), has a half-life of only 2 min, but this N-terminal region has not a general rate enhancement effect. LovK(1-163), a construct with fully intact N- and C-termini (but missing the kinase domain), is slower to recover than either LovK(25-138), LovK(1-138), or LovK(25-163)
additional information
EvgS is a hybrid histidine kinase composed of a histidine kinase domain, receiver domain, and Hpt transmitter domain. The phosphate at the initial histidine residue in the histidine kinase domain is subsequently transferred to an aspartate residue in the receiver domain and is relayed to the second histidine residue in the Hpt domain before being transferred to the aspartate residue in EvgA
additional information
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EvgS is a hybrid histidine kinase composed of a histidine kinase domain, receiver domain, and Hpt transmitter domain. The phosphate at the initial histidine residue in the histidine kinase domain is subsequently transferred to an aspartate residue in the receiver domain and is relayed to the second histidine residue in the Hpt domain before being transferred to the aspartate residue in EvgA
additional information
Hik2 contains a GAF (cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA) domain in the signal input region
additional information
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Hik2 contains a GAF (cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA) domain in the signal input region
additional information
KinD is located upstream of Spo0A and AbrB in the pathway. CACHE is present in many bacterial sensory histidine kinases and is capable of sensing small molecules, often in the presence of cofactors, such as metal ions
additional information
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KinD is located upstream of Spo0A and AbrB in the pathway. CACHE is present in many bacterial sensory histidine kinases and is capable of sensing small molecules, often in the presence of cofactors, such as metal ions
additional information
LOV domains are blue-light sensory modules which bind a flavin molecule as cofactor
additional information
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LOV domains are blue-light sensory modules which bind a flavin molecule as cofactor
additional information
mechanism for the pH-dependent conformational change of the extracellular sensor domain of DraK protein involving residues E83, E105, and E107 with very high pKa values, overview
additional information
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mechanism for the pH-dependent conformational change of the extracellular sensor domain of DraK protein involving residues E83, E105, and E107 with very high pKa values, overview
additional information
protein-protein docking analysis of the catalytic domain with the dimerization DHp domain of DesK, the C-terminal part of the ATP lid interacts with helix alpha1 of the DHp, through hydrogen bonds between His335 and Asp289 as well as Gly199 with Lys333, overview
additional information
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protein-protein docking analysis of the catalytic domain with the dimerization DHp domain of DesK, the C-terminal part of the ATP lid interacts with helix alpha1 of the DHp, through hydrogen bonds between His335 and Asp289 as well as Gly199 with Lys333, overview
additional information
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structure-function analysis histidine kinase AHK5 bound to its cognate phosphotransfer protein AHP1, overview. AHP1 binds AHK5RD via a prominent hydrogen bond docking ridge and a hydrophobic patch. AHK5RD binds to AHP1-3 with similar, micromolar affinity, consistent with the transient nature of this signaling complex. Architecture of the AHK5RD-AHP1 Interface, overview
additional information
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the coordination and oxidation state of the sensor domain heme iron profoundly affect the enzyme's catalytic activity because they modulate its ATP binding affinity and thus change its kcat/Km(ATP) value. Effects of the response regulator and different divalent metal cations on the autophosphorylation reaction, overview
additional information
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the HK domain is a monomer in solution and presents autokinase activity
additional information
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the N-terminal transmembrane domain is dispensable but the PAS domain is needed for the kinase activity
additional information
the periplasmic sensor domain of CusS directly interacts with Ag(I) ions and undergoes a conformational change upon metal binding. Metal binding also enhances the tendency of the domain to dimerize. For NMR structure analysis, the enzyme is prepared with Ag+, Ni2+, Zn2+, and Cu+ ions via dialysis
additional information
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the periplasmic sensor domain of CusS directly interacts with Ag(I) ions and undergoes a conformational change upon metal binding. Metal binding also enhances the tendency of the domain to dimerize. For NMR structure analysis, the enzyme is prepared with Ag+, Ni2+, Zn2+, and Cu+ ions via dialysis
additional information
the VicK kinase activates itself by helical bending of the DHp domain and coordinated swinging around of the catalytic and ATP binding domain to engage with the target histidine. Modelling of the active state structure of the catalytic ATP-binding domain and positioning of inactive domain. Structure-function analysis of the enzyme domains, detailed overview. Transient formation of the active site
additional information
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LOV domains are blue-light sensory modules which bind a flavin molecule as cofactor
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additional information
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the N-terminal transmembrane domain is dispensable but the PAS domain is needed for the kinase activity
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additional information
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protein-protein docking analysis of the catalytic domain with the dimerization DHp domain of DesK, the C-terminal part of the ATP lid interacts with helix alpha1 of the DHp, through hydrogen bonds between His335 and Asp289 as well as Gly199 with Lys333, overview
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additional information
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basic architecture of VirA/VirG histidine kinase: the membrane-embedded VirA histidine kinase contains four modular domains, and the signal inputs activate the VirG response regulator. The sugar-binding protein ChvE interacts with the periplasmic domain, and phenols interact with the linker domain. The linker is predicted to adopt a GAF fold with the alpha1 helix. The conserved His474 is located in the dimerization domain of the kinase
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additional information
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the VicK kinase activates itself by helical bending of the DHp domain and coordinated swinging around of the catalytic and ATP binding domain to engage with the target histidine. Modelling of the active state structure of the catalytic ATP-binding domain and positioning of inactive domain. Structure-function analysis of the enzyme domains, detailed overview. Transient formation of the active site
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additional information
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conserved proline-222, which is adjacent to the phosphoryl acceptor histidine, contributes to helical bending, which is essential for the autokinase and phosphatase activities. The proline is essential for phosphatase activity. The C-terminal ends of the VicK dimer harbor two monomeric catalytic domains. The enzyme architecture with a signal transducer and sensor domain suggests a model where DHp helical bending and a CA swing movement are likely coordinated for autokinase activation, structure-function analysis, overview
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additional information
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mechanism for the pH-dependent conformational change of the extracellular sensor domain of DraK protein involving residues E83, E105, and E107 with very high pKa values, overview
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tetramer
and monomer and oligomer, 4 * 48500, calculated from sequence, 4 * 50000, SDS-PAGE.The functional form of Hik2 is a higher-order oligomer such as a hexamer or octamer
?
x * 99000, SDS-PAGE
?
x * 48846, calculation from nucleotide sequence
?
x * 44600, calculation from nucleotide sequence
?
x * 47774, calculation from nucleotide sequence
?
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x * 54000, SDS-PAGE of MtrB
?
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x * 67275, calculation from nucleotide sequence
?
x * 102452, calculation from nucleotide sequence
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x * 49772, calculation from nucleotide sequence
?
x * 38409, calculation from nucleotide sequence
?
x * 50597, calculation from nucleotide sequence
?
x * 46389, calculation from nucleotide sequence
dimer
2 * 79000
dimer
2 * 44000, SDS-PAGE
dimer
-
2 * 44000, SDS-PAGE
-
dimer
wild-type KinA PAS-A, NMR, SDS-PAGE and gel filtration
dimer
-
wild-type KinA PAS-A, NMR, SDS-PAGE and gel filtration
-
dimer
-
the Brucella HK domain presents two different dimeric assemblies in the asymmetric unit: one similar to canonical parallel homodimers (C) and the other, an antiparallel non-canonical (NC) dimer, each with distinct relative subdomain orientations and dimerization interfaces. The C dimer is the functionally relevant species and can be stabilized and is active in solution. The HK domain is a monomer in solution and presents autokinase activity
dimer
the isolated TorS sensor domain dimerizes in solution
dimer
periplasmic sensor domain of CusS directly interacts with Ag(I) ions and undergoes a conformational change upon metal binding. Metal binding also enhances the tendency of the domain to dimerize
dimer
the overall structure of Ag(I)-CusS(39-187) is a mixed alpha/beta fold with a PAS-like topology. The central five-stranded anti-parallel beta-sheet is flanked by alpha-helices on either side. The structure begins with a long N-terminal alpha-helix and ends with a short C-terminal alpha-helix that both lie on the same side of the sheet, The structure of the periplasmic sensor domain of the histidine kinase CusS shows unusual metal ion coordination at the dimeric interface, enzyme CusS forms a homodimer with four Ag(I) binding sites per dimeric complex. Metal-induced dimerization results in increases in kinase activity in the cytoplasmic domains of CusS. There are four Ag(I)-CusS(39-187) molecules in the asymmetric unit that interact to form two homodimers
dimer
-
x-ray crystallography
dimer
x-ray crystallography
dimer
-
the signal transduction histidine kinase domain, H-NOXA revealing a Per-Arnt-Sim fold, monomers dimerize in a parallel arrangement juxtaposing their N-terminal helices and preceding residues, overview
dimer
dimeric PaBphP-PCD structure with PAS, GAF, and PHY domains, interdomain and histidine kinase domain, domain structure, overview
dimer
-
AgrC forms ligand-independent dimers that undergo trans-autophosphorylation upon interaction with autoinducing peptide
dimer
the extracellular domain of enzyme YycG exhibits two dimerization modes, dimerization configurations, cross-linking experiments, overview. Both YycH and YycI are required to inhibit the dimerization of YycG
dimer
-
the extracellular domain of enzyme YycG exhibits two dimerization modes, dimerization configurations, cross-linking experiments, overview. Both YycH and YycI are required to inhibit the dimerization of YycG
-
dimer
the dimeric VicK protein has a rod-shaped structure with the domains linearly connected like beads on a string
dimer
-
the dimeric VicK protein has a rod-shaped structure with the domains linearly connected like beads on a string
-
dimer
the holoenzyme exists as a stable dimer in solution. The overall structure of VicK is a long-rod dimer that anchors four connected domains: HAMP, Per-ARNT-SIM (PAS), DHp, and catalytic and ATP binding domain (CA). The HAMP, a signal transducer, and the PAS domain, major sensor, adopt canonical folds with dyad symmetry. In contrast, the dimer of the DHp and CA domains is asymmetric because of different helical bends in the DHp domain and spatial positions of the CA domains. A conserved proline, which is adjacent to the phosphoryl acceptor histidine, contributes to helical bending, which is essential for the autokinase and phosphatase activities. Following the transmembrane domain, the HAMP signal transducer domain and PAS sensor domain are directly connected to the catalytic domain through a DHp domain, a dimerization and histidine phosphorylation domain. Structure of the HAMP domain (aa 36-86), located at the uppermost position within the N-terminal region of the VicK structure, overview
dimer
-
the holoenzyme exists as a stable dimer in solution. The overall structure of VicK is a long-rod dimer that anchors four connected domains: HAMP, Per-ARNT-SIM (PAS), DHp, and catalytic and ATP binding domain (CA). The HAMP, a signal transducer, and the PAS domain, major sensor, adopt canonical folds with dyad symmetry. In contrast, the dimer of the DHp and CA domains is asymmetric because of different helical bends in the DHp domain and spatial positions of the CA domains. A conserved proline, which is adjacent to the phosphoryl acceptor histidine, contributes to helical bending, which is essential for the autokinase and phosphatase activities. Following the transmembrane domain, the HAMP signal transducer domain and PAS sensor domain are directly connected to the catalytic domain through a DHp domain, a dimerization and histidine phosphorylation domain. Structure of the HAMP domain (aa 36-86), located at the uppermost position within the N-terminal region of the VicK structure, overview
-
dimer
the Cph1 protein forms dimers through the C-terminal region
dimer
-
the isolated TorS sensor domain dimerizes in solution
dimer
-
the isolated TorS sensor domain dimerizes in solution
-
homodimer
-
-
homodimer
x-ray crystallography
homodimer
-
YbdK-transmembrane domain forms homodimers in dodecyl-phosphocholine micelles, cross-linking assay and analytical ultracentrifugation analysis
homodimer
histidine kinases are composed of an N-terminal sensory (or input) domain, which senses external stimuli, and a conserved kinase domain, which contains an N-terminal dimerization and histidine phosphotransfer domain and a catalytic and ATP binding (CA) domain
homodimer
-
histidine kinases are composed of an N-terminal sensory (or input) domain, which senses external stimuli, and a conserved kinase domain, which contains an N-terminal dimerization and histidine phosphotransfer domain and a catalytic and ATP binding (CA) domain
-
homotetramer
-
KinC becomes active by forming a homotetramer via the N-terminal PAS domain
homotetramer
-
KinC becomes active by forming a homotetramer via the N-terminal PAS domain
-
monomer
1 * 110000, SDS-PAGE
monomer
and tetramer and oligomer, 1 * 48500, calculated from sequence, 1 * 50000, SDS-PAGE.The functional form of Hik2 is a higher-order oligomer such as a hexamer or octamer
oligomer
intact YycG HK can form higher-order oligomers at the cell membrane via combinations of the H- and L-dimeric interacting surfaces
oligomer
-
intact YycG HK can form higher-order oligomers at the cell membrane via combinations of the H- and L-dimeric interacting surfaces
-
oligomer
and tetramer and monomer, x * 48500, calculated from sequence, x * 50000, SDS-PAGE.The functional form of Hik2 is a higher-order oligomer such as a hexamer or octamer
additional information
-
basic architecture of VirA/VirG histidine kinase: the membrane-embedded VirA histidine kinase contains four modular domains, and the signal inputs activate the VirG response regulator. The sugar-binding protein ChvE interacts with the periplasmic domain, and phenols interact with the linker domain. The linker is predicted to adopt a GAF fold with the alpha1 helix. The conserved His474 is located in the dimerization domain of the kinase
additional information
-
basic architecture of VirA/VirG histidine kinase: the membrane-embedded VirA histidine kinase contains four modular domains, and the signal inputs activate the VirG response regulator. The sugar-binding protein ChvE interacts with the periplasmic domain, and phenols interact with the linker domain. The linker is predicted to adopt a GAF fold with the alpha1 helix. The conserved His474 is located in the dimerization domain of the kinase
-
additional information
the enzyme AaHSK1 has several conserved domains and motifs, such as a HAMP (histidine kinase, adenylate cyclase, methyl binding protein, and phosphatase) domain and a dimerization/phosphoacceptor domain. AaHSK1 contains four repeat domains within HAMP
additional information
-
the enzyme AaHSK1 has several conserved domains and motifs, such as a HAMP (histidine kinase, adenylate cyclase, methyl binding protein, and phosphatase) domain and a dimerization/phosphoacceptor domain. AaHSK1 contains four repeat domains within HAMP
additional information
-
the enzyme AaHSK1 has several conserved domains and motifs, such as a HAMP (histidine kinase, adenylate cyclase, methyl binding protein, and phosphatase) domain and a dimerization/phosphoacceptor domain. AaHSK1 contains four repeat domains within HAMP
-
additional information
high affinity binding is observed between AHK1 monomers resulting in the formation of the dimer present at physiological conditions. A high affinity interaction is also observed between AHK1 and AHP2 transfer protein
additional information
determination of the importance of several residues at the dimer interface for KinA enzymatic activity in vitro and in vivo, KinA architecture and domain structure, and PAS-A domain organization and secondary structure, overview
additional information
-
determination of the importance of several residues at the dimer interface for KinA enzymatic activity in vitro and in vivo, KinA architecture and domain structure, and PAS-A domain organization and secondary structure, overview
additional information
analysis of the structure of enzyme catalytic and ATP-binding domain using the crystal structure, overview
additional information
-
analysis of the structure of enzyme catalytic and ATP-binding domain using the crystal structure, overview
additional information
-
the N-terminal transmembrane domain is dispensable but the PAS domain is needed for the kinase activity
additional information
-
the N-terminal transmembrane domain is dispensable but the PAS domain is needed for the kinase activity
-
additional information
-
analysis of the structure of enzyme catalytic and ATP-binding domain using the crystal structure, overview
-
additional information
-
determination of the importance of several residues at the dimer interface for KinA enzymatic activity in vitro and in vivo, KinA architecture and domain structure, and PAS-A domain organization and secondary structure, overview
-
additional information
-
Brucella LOV-HK comprises an N-terminal blue-light sensor (LOV) domain, followed by a central PAS domain and a C-terminal HK domain. Crystal structure analysis, overview
additional information
LovK trypsin peptide mapping
additional information
-
LovK trypsin peptide mapping
additional information
-
the N-terminus of HK17 forms a GAF domain, structure of the RR-HK17 two-component system
additional information
-
the periplasmic region of histidine kinase EnvZ(Ala38-Arg162) forms a dimer in solution
additional information
NMR structure analysis, localization and structural model, detailed overview
additional information
CusS is predicted to be a canonical histidine kinase with a periplasmic sensor domain connected by transmembrane helices to the catalytic cytoplasmic domains
additional information
-
CusS is predicted to be a canonical histidine kinase with a periplasmic sensor domain connected by transmembrane helices to the catalytic cytoplasmic domains
additional information
EvgS is a hybrid histidine kinase composed of a histidine kinase domain, receiver domain, and Hpt transmitter domain. EvgS has a large periplasmic sensor region consisting of two tandem bacterial periplasmic solute-binding protein (PBPb) domains at its N-terminus. The periplasmic sensor region of EvgS is necessary for EvgS activation, and Leu152, located within the first PBPb domain, is involved in the activation. Alkali metals are perceived at the periplasmic sensor region, whereas the cytoplasmic linker domain, connecting the transmembrane region and the histidine kinase domain, is required for low-pH perception
additional information
-
EvgS is a hybrid histidine kinase composed of a histidine kinase domain, receiver domain, and Hpt transmitter domain. EvgS has a large periplasmic sensor region consisting of two tandem bacterial periplasmic solute-binding protein (PBPb) domains at its N-terminus. The periplasmic sensor region of EvgS is necessary for EvgS activation, and Leu152, located within the first PBPb domain, is involved in the activation. Alkali metals are perceived at the periplasmic sensor region, whereas the cytoplasmic linker domain, connecting the transmembrane region and the histidine kinase domain, is required for low-pH perception
additional information
DcuS shows a mixed alpha/beta-structure containing two subdomains of similar folds, each consisting of a five-stranded antiparallel beta-sheet flanked by helices on either side, structure analysis, residues 42-181 comprise the sensory domain of the enzyme, dimerization of DcuS-42181, overview
additional information
-
the N-terminal domain in an STHK from Nostoc punctiforme is homologous to the central region in soluble guanylyl cyclase, the main receptor for nitric oxide, structure-function analysis and dimerization mechanism, overview
additional information
modeling of the full-length bacteriophytochrome structure, including its output histidine kinase domain, structure-function relationship, overview
additional information
-
modeling of the full-length bacteriophytochrome structure, including its output histidine kinase domain, structure-function relationship, overview
additional information
-
Ppr is composed of three domains, a PYP domain, a bacteriophytochrome Bph domain, and a histidine kinase domain, in the order from the N- to the C-terminal of Ppr
additional information
-
Both YycH and YycI are required to inhibit the dimerization of YycG. Genes yycH and yycI are members of the yyc operon. The actions of YycH and YycI on YycG likely occur at the transmembrane helices, in which an octameric complex was formed by an YycG homodimer flanked by YycH-YycI heterodimers
additional information
Both YycH and YycI are required to inhibit the dimerization of YycG. Genes yycH and yycI are members of the yyc operon. The actions of YycH and YycI on YycG likely occur at the transmembrane helices, in which an octameric complex was formed by an YycG homodimer flanked by YycH-YycI heterodimers
additional information
-
Both YycH and YycI are required to inhibit the dimerization of YycG. Genes yycH and yycI are members of the yyc operon. The actions of YycH and YycI on YycG likely occur at the transmembrane helices, in which an octameric complex was formed by an YycG homodimer flanked by YycH-YycI heterodimers
-
additional information
enzyme VicK is composed of several domains (HAMP, PAS, DHp, and catalytic and ATP binding domain [CA]) in addition to a short transmembrane domain. Domain structure-function relationship and analysis, overview. The overall structure of VicK comprises a dimer in the shape of a long slim rod
additional information
-
enzyme VicK is composed of several domains (HAMP, PAS, DHp, and catalytic and ATP binding domain [CA]) in addition to a short transmembrane domain. Domain structure-function relationship and analysis, overview. The overall structure of VicK comprises a dimer in the shape of a long slim rod
-
additional information
enzyme DraK consists of an extracellular domain flanked by two transmembrane helices (Leu5-Val27 and Leu126-Ile145), a sensory domain (Glu28-Thr125), a HAMP (histidine kinases, adenylyl cyclases, methyl-accepting chemotaxis proteins and phosphatases) domain (Asn149-Thr201) and a kinase domain (Ala202-Pro410) composed of His KA and CA domains
additional information
-
enzyme DraK consists of an extracellular domain flanked by two transmembrane helices (Leu5-Val27 and Leu126-Ile145), a sensory domain (Glu28-Thr125), a HAMP (histidine kinases, adenylyl cyclases, methyl-accepting chemotaxis proteins and phosphatases) domain (Asn149-Thr201) and a kinase domain (Ala202-Pro410) composed of His KA and CA domains
additional information
mechanism for the pH-dependent conformational change of the the extracellular sensor domain protein of DraK, overview. The structure contains a mixed alpha-beta fold, adopting a fold similar to the ubiquitous sensor domain of histidine kinase
additional information
-
mechanism for the pH-dependent conformational change of the the extracellular sensor domain protein of DraK, overview. The structure contains a mixed alpha-beta fold, adopting a fold similar to the ubiquitous sensor domain of histidine kinase
additional information
monomer-dimer equilibrium of the shortened extracellular sensing domain of DraK in solution, with MWs of 9.7 kDa for the monomeric and 19.4 kDa for the dimeric form
additional information
-
monomer-dimer equilibrium of the shortened extracellular sensing domain of DraK in solution, with MWs of 9.7 kDa for the monomeric and 19.4 kDa for the dimeric form
additional information
-
monomer-dimer equilibrium of the shortened extracellular sensing domain of DraK in solution, with MWs of 9.7 kDa for the monomeric and 19.4 kDa for the dimeric form
-
additional information
-
mechanism for the pH-dependent conformational change of the the extracellular sensor domain protein of DraK, overview. The structure contains a mixed alpha-beta fold, adopting a fold similar to the ubiquitous sensor domain of histidine kinase
-
additional information
-
enzyme DraK consists of an extracellular domain flanked by two transmembrane helices (Leu5-Val27 and Leu126-Ile145), a sensory domain (Glu28-Thr125), a HAMP (histidine kinases, adenylyl cyclases, methyl-accepting chemotaxis proteins and phosphatases) domain (Asn149-Thr201) and a kinase domain (Ala202-Pro410) composed of His KA and CA domains
-
additional information
-
analysis of the enzyme subdomains of the N-terminal region
additional information
analysis of the enzyme subdomains of the N-terminal region
additional information
-
Hik33 has several subdomains in its N-terminal region, two of which are transmembrane (TM) helices (TM1 and TM2), and it is located on plasma and/or thylakoid membranes. The N-terminal region also includes a periplasmic loop region between the TM helices, a HAMP domain, and a PAS domain. Analysis of the enzyme subdomains of the N-terminal region
additional information
Hik33 has several subdomains in its N-terminal region, two of which are transmembrane (TM) helices (TM1 and TM2), and it is located on plasma and/or thylakoid membranes. The N-terminal region also includes a periplasmic loop region between the TM helices, a HAMP domain, and a PAS domain. Analysis of the enzyme subdomains of the N-terminal region
additional information
-
DctB shows a mixed alpha/beta-structure containing two subdomains of similar folds, each consisting of a five-stranded antiparallel beta-sheet flanked by helices on either side, structure analysis, residues 28-286 comprise the sensory domain of the enzyme, overview
additional information
Vibrio cholerae serotype O1 MO45
-
DctB shows a mixed alpha/beta-structure containing two subdomains of similar folds, each consisting of a five-stranded antiparallel beta-sheet flanked by helices on either side, structure analysis, residues 28-286 comprise the sensory domain of the enzyme, overview
-
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Y293F
-
site-directed mutagenesis, Y293F substitution in full-length VirA changes the phenol perception, mutation VirA(LKR)D280-284,Y293F does not alter phenol specificity nearly to the extent as mutant Y293T, it does increase the activity of virtually all active phenols roughly 30fold above that of VirA(LKR)D280-284. Acetosyringone sensitivity increases in VirAY293F with and without glucose
Y293T
-
site-directed mutagenesis, Y293T substitution in full-length VirA changes the phenol perception, mutation VirA(LKR)D280-284,Y293T alters phenol specificity of the enzyme
Y293F
-
site-directed mutagenesis, Y293F substitution in full-length VirA changes the phenol perception, mutation VirA(LKR)D280-284,Y293F does not alter phenol specificity nearly to the extent as mutant Y293T, it does increase the activity of virtually all active phenols roughly 30fold above that of VirA(LKR)D280-284. Acetosyringone sensitivity increases in VirAY293F with and without glucose
-
Y293T
-
site-directed mutagenesis, Y293T substitution in full-length VirA changes the phenol perception, mutation VirA(LKR)D280-284,Y293T alters phenol specificity of the enzyme
-
D1050A
mutation changes conformation of the beta3-alpha3 loop in solution and shifts residue F1102 to the inactive orientation
D1050E
mutation changes conformation of the beta3-alpha3 loop in solution and shifts residue F1102 to the inactive orientation
H405A
-
negative mutation of CKI1
A413R
-
the mutation impairs KinA activity, folding or stability
Ala413L
-
the mutation impairs KinA activity, folding or stability
E342A
site-directed mutagenesis of the catalytic domain residue
E343A
site-directed mutagenesis of the catalytic domain residue
F432C
-
the substitution has less effect on Sda binding
F436S
-
the mutation increases the efficiency of sporulation in cells overexpressing KinA inhibitor Sda by about 10fold while actually reducing the efficiency of sporulation in cells that lack sda
G192C/G334C
site-directed mutagenesis, the Cys-engineered mutant is used for interdomain disulfide covalent bonding studies
H430C
-
the substitution has less effect on Sda binding
H5K
mutation in extracellular tail, mutant is sensitive to pH
I108A
the point mutation does not affect KinA autophosphorylation activity, but interfers with KinA PAS-A dimerization
I95A
the point mutation slightly reduces the KinA autophosphorylation activity and interfers with KinA PAS-A dimerization
I95E
the point mutation reduces the KinA autophosphorylation activity and interfers with KinA PAS-A dimerization
K32E/E36K
mutations in linker region, mutant shows higher activity at higher pH and maintains pH regulation
P410L
-
the mutation increases the efficiency of sporulation in cells overexpressing KinA inhibitor Sda by about 10fold while actually reducing the efficiency of sporulation in cells that lack sda
P410L/F436S
-
the mutant has a low affinity for inhibitor Sda
Q193C/G334C
site-directed mutagenesis, the Cys-engineered mutant is used for interdomain disulfide covalent bonding studies
R34E/ E36K/ R37E
mutations in linker region, mutant is inactive and insensitive to pH
S196C/G334C
site-directed mutagenesis, the Cys-engineered mutant is used for interdomain disulfide covalent bonding studies
Y29A
the point mutation is an activating mutation in full-length KinA, but interfers with KinA PAS-A dimerization shifting the PAS-A monomer/dimer equilibrium significantly toward the monomeric form
E342A
-
site-directed mutagenesis of the catalytic domain residue
-
E343A
-
site-directed mutagenesis of the catalytic domain residue
-
G192C/G334C
-
site-directed mutagenesis, the Cys-engineered mutant is used for interdomain disulfide covalent bonding studies
-
H188V
-
site-directed mutagenesis of the catalytic domain residue
-
H5K
-
mutation in extracellular tail, mutant is sensitive to pH
-
I108A
-
the point mutation does not affect KinA autophosphorylation activity, but interfers with KinA PAS-A dimerization
-
I95A
-
the point mutation slightly reduces the KinA autophosphorylation activity and interfers with KinA PAS-A dimerization
-
I95E
-
the point mutation reduces the KinA autophosphorylation activity and interfers with KinA PAS-A dimerization
-
K32E/E36K
-
mutations in linker region, mutant shows higher activity at higher pH and maintains pH regulation
-
Q193C/G334C
-
site-directed mutagenesis, the Cys-engineered mutant is used for interdomain disulfide covalent bonding studies
-
R34E/ E36K/ R37E
-
mutations in linker region, mutant is inactive and insensitive to pH
-
Y29A
-
the point mutation is an activating mutation in full-length KinA, but interfers with KinA PAS-A dimerization shifting the PAS-A monomer/dimer equilibrium significantly toward the monomeric form
-
H1172Q
mutation abolishes BvgS activity in vivo and eliminates detectable phosphorylation of BvgA in vitro. Activity of BvgS H1172Q can be restored by providing the wild-type C-terminal domain in trans
A287C/L333C
-
site-directed mutagenesis, the mutant cross-linked dimer shows altered autophosphorylation activity compared to the wild-type enzyme
I286C
-
site-directed mutagenesis of the long HK domain version, the mutation is located in the alpha1 helix N-terminal to the histidine phosphoacceptor, the mutant cross-linked dimer shows altered autophosphorylation activity compared to the wild-type enzyme
I286C/N388A
-
site-directed mutagenesis of the short HK domain version, the N388A mutation impairs the phosphorylation capacity, the mutant is unable to bind ATP
V282C
-
site-directed mutagenesis, the mutation is located in the alpha1 helix N-terminal to the histidine phosphoacceptor, the mutant cross-linked dimer shows altered autophosphorylation activity compared to the wild-type enzyme
C70A
site-directed mutagenesis
D286C
-
t1/2 at room temperature is 16 min, compared to 12 min for wild-type enzyme. 71% of the wild-type phosphatase activity
E257C
-
t1/2 at room temperature is 30 min, compared to 12 min for wild-type enzyme. 31% of the wild-type phosphatase activity
E261C
-
t1/2 at room temperature is 15 min, compared to 12 min for wild-type enzyme. 77% of the wild-type phosphatase activity
E268C
-
t1/2 at room temperature is 23 min, compared to 12 min for wild-type enzyme. 45% of the wild-type phosphatase activity
E275C
-
t1/2 at room temperature is 28 min, compared to 12 min for wild-type enzyme. 34% of the wild-type phosphatase activity
E276C
-
t1/2 at room temperature is 68 min, compared to 12 min for wild-type enzyme. 5% of the wild-type phosphatase activity
E282C
-
t1/2 at room temperature is 15 min, compared to 12 min for wild-type enzyme. 77% of the wild-type phosphatase activity
F43I
site-directed mutagenesis, the mutation results in a slightly reduced growth defect compared to the construct in which all interface binding site residues are mutated
G240C
-
t1/2 at room temperature is 10 min, compared to 12 min for wild-type enzyme. 123% of the wild-type phosphatase activity
G264C
-
t1/2 at room temperature is 12 min, compared to 12 min for wild-type enzyme. As active as wild-type enzyme
H153F
mutation in periplasmic arm, mutant does not show any detectable activity above background at pH 7 or pH 5.6
H176A
site-directed mutagenesis, the mutation results in the same growth defects as the construct in which all interface binding site residues are mutated
H226A
mutant can be induced at low pH
H226L
mutant cannot be induced at low pH
H226N
mutant cannot be induced at low pH
H226Q
mutant cannot be induced at low pH
H226Q/S600I
level of activity at pH 7 is very similar to that of EvgS S600I and mutant is inducible at pH 5.6
H226T
mutant cannot be induced at low pH
H226V
mutant cannot be induced at low pH
H226W
mutant cannot be induced at low pH
H243K
-
inactive mutant protein
H243N
-
inactive mutant protein
H243S
-
inactive mutant protein
H243V
-
inactive mutant protein
H243X
the His residue at position 243 of the EnvZ protein is changed by means of site-directed mutagenesis. The mutant EnvZ protein is defective in its in vitro ability not only as to EnvZ-autophosphorylation but also OmpR-phosphorylation and OmpR-dephosphorylation. This particular mutant EnvZ protein seems to exhibit null functions as to the in vivo osmoregulatory phenotype
H243Y
-
inactive mutant protein
H248A
-
mutation abrogates autophosphorylation by disrupting the phosphorylation site in the DHp domain
H248A/N356K
-
mutation abrogates autophosphorylation
H398L
-
the mutant retains itscapability to bind ATP and is competent to catalyze the transphosphorylation of an AtoS G-box (G565A) mutant protein which otherwise fails to autophosphorylate due to its inability to bind ATP
H42A
site-directed mutagenesis, the mutation results in the same growth defects as the construct in which all interface binding site residues are mutated
H63A
noninducible mutant, no protein is detected
H63Q/H106Q/H124Q
mutations in potential His triad, mutant shows the same level of induction as the wild-type EvgS
K152A
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows moderate activation by KCl-supplemented M9 medium, pH 5.5
K152E
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows strong activation by KCl-supplemented M9 medium, pH 5.5
K152F
naturally occuring mutation and site-directed mutagenesis, in the mutant, EvgS activation is observed only by complementation with pBADevgS, mutation L152F leads to the desensitization of EvgS in strain KMY1. The mutant shows no activation by KCl-supplemented M9 medium, pH 5.5. The L152F mutation is found in only two Escherichia coli strains, MC4100 and DH1
K152I
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows strong activation by KCl-supplemented M9 medium, pH 5.5
K152R
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows moderate activation by KCl-supplemented M9 medium, pH 5.5
K152Y
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows no activation by KCl-supplemented M9 medium, pH 5.5
K272C
-
t1/2 at room temperature is 55 min, compared to 12 min for wild-type enzyme. 10% of the wild-type phosphatase activity
L152F/S600I
level of activity at pH 7 is very similar to that of EvgS S600I and mutant is inducible at pH 5.6
L236C
-
t1/2 at room temperature is 25 min, compared to 12 min for wild-type enzyme. 40% of the wild-type phosphatase activity
L254C
-
inactive mutant enzyme, t1/2 at room temperature is 90 min, compared to 12 min for wild-type enzyme
N248A
site-directed mutagenesis, the mutation activates the enzyme
N248D
site-directed mutagenesis, the mutation activates the enzyme
N248G
site-directed mutagenesis, the mutation activates the enzyme
N271C
-
t1/2 at room temperature is 36 min, compared to 12 min for wild-type enzyme. 23% of the wild-type phosphatase activity
N278C
-
t1/2 at room temperature is 45 min, compared to 12 min for wild-type enzyme. 15% of the wild-type phosphatase activity
N356K
-
mutation abrogates autophosphorylation by disrupting the ATP-binding site in the CA domain
P522A/S600I
level of activity at pH 7 is very similar to that of EvgS S600I and mutant is inducible at pH 5.6
Q262C
-
t1/2 at room temperature is 11 min, compared to 12 min for wild-type enzyme. 111% of the wild-type phosphatase activity
Q283C
-
t1/2 at room temperature is 13 min, compared to 12 min for wild-type enzyme. 91% of the wild-type phosphatase activity
R246C
-
t1/2 at room temperature is 62 min, compared to 12 min for wild-type enzyme. 7% of the wild-type phosphatase activity
S242C
-
t1/2 at room temperature is 39 min, compared to 12 min for wild-type enzyme. 20% of the wild-type phosphatase activity
S260C
-
t1/2 at room temperature is 13 min, compared to 12 min for wild-type enzyme. 91% of the wild-type phosphatase activity
S269C
-
t1/2 at room temperature is 20 min, compared to 12 min for wild-type enzyme. 54% of the wild-type phosphatase activity
S600I
mutation in cytoplasmic PAS domain, renders EvgS constitutively active at pH 7
T235C
-
t1/2 at room temperature is 14 min, compared to 12 min for wild-type enzyme. 84% of the wild-type phosphatase activity
T247R
-
inactive mutant protein
T250C
-
t1/2 at room temperature is 23 min, compared to 12 min for wild-type enzyme. 45% of the wild-type phosphatase activity
T256C
-
t1/2 at room temperature is 27 min, compared to 12 min for wild-type enzyme. 36% of the wild-type phosphatase activity
Y265C
-
t1/2 at room temperature is 20 min, compared to 12 min for wild-type enzyme. 54% of the wild-type phosphatase activity
H44A
-
the mutation may increase the side chain pKa of acidic amino acids in the input domain, whose protonation contributes to the activation of ArsS
H94A
-
H94 in the input domain of ArsS is crucial for acid perception
D56N
phosphorylation of CitB is inhibited by a D56N exchange. In the presence of ATP, CitB-D56N forms a stable complex with MalE-CitAC
H350L
autokinase activity of CitA is abolished by an H350L exchange
D657N
-
substitution in the first receiver domain, is unable to complement the deltarodK strain SA1708, delayed timing of aggregation, rare sporulation outside fruiting bodies, but normal fruiting body morphology on CF agar, loose aggregates of fruiting bodies in submerged culutre
D657N/D782N
-
delayed timing of aggregation, frequent sporulation outside fruiting bodies, and loose mounds of fruiting body morphology on CF agar, no aggregation of fruiting bodies in submerged culutre, no autophosphorylation
D657N/D782N/D909N
-
delayed timing of aggregation, frequent sporulation outside fruiting bodies, and irregular fruiting body morphology on CF agar, no aggregation of fruiting bodies in submerged culutre, autophosphorylates
D657N/D909N
-
delayed timing of aggregation, frequent sporulation outside fruiting bodies, and irregular and small fruiting body morphology on CF agar, no aggregation of fruiting bodies in submerged culutre, autophosphorylates
D696A
site-directed mutagenesis, the mutation of the receiver domain residue leads to release of phosphate to the medium, overview
D782N
-
substitution in the second receiver domain, is unable to complement the deltarodK strain SA1708, delayed timing of aggregation, frequent sporulation outside fruiting bodies, and irregular and small fruiting body morphology on CF agar, no aggregation of fruiting bodies in submerged culutre
D782N/D909N
-
delayed timing of aggregation, frequent sporulation outside fruiting bodies, and loose mounds of fruiting body morphology on CF agar, no aggregation of fruiting bodies in submerged culutre, autophosphorylates
D909N
-
substitution in the third receiver domain, is unable to complement the deltarodK strain SA1708, delayed timing of aggregation, frequent sporulation outside fruiting bodies, but normal fruiting body morphology on CF agar, no aggregation of fruiting bodies in submerged culutre
H360A
-
is unable to complement the deltarodK strain SA1708, delayed timing of aggregation, frequent sporulation outside fruiting bodies, and irregular fruiting body morphology on CF agar, no aggregation of fruiting bodies in submerged culutre
H407A
site-directed mutagenesis, the mutation of the autophosphorylation site residue H407 inhibits autophosphorylation of the enzyme
A143G
-
the mutant still has some divalent cation-mediated repression and therefore likely has some ability to bind cations
D110A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
D60C
contrary to wild-type, mutant strain displays Co(II)-inducible resistance to antibiotic meropenem
E115A
-
the mutant still has some divalent cation-mediated repression and therefore likely has some ability to bind cations
E133A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
E77A
-
the mutant still has some divalent cation-mediated repression and therefore likely has some ability to bind cations
G139A
-
the mutant still has some divalent cation-mediated repression and therefore likely has some ability to bind cations
H124A
no change in overall periplasmic domain fold, mutant shows an altered biofilm morphology compared to the wild-type strain
H133A
no change in overall periplasmic domain fold, mutant abolishes biofilm formation
H55A
mutant loses its intrinsic resistance to Zn(II) and meropenem due to the destruction of Zn(II) binding site
H97A
mutant abolishes biofilm formation
L137A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
L158A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
L38C/H55A
mutation L38C restores the lost responsiveness of mutation H55A to Zn(II) stimulus
Q188L
site-directed mutagenesis, crystal structure determination and analysis
R94A
mutant strain shows biofilm morphology similar to wild-type
R94A/H97A
no change in overall periplasmic domain fold
S145A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
W150A
variant is misfolded
D60C
-
contrary to wild-type, mutant strain displays Co(II)-inducible resistance to antibiotic meropenem
-
H124A
-
no change in overall periplasmic domain fold, mutant shows an altered biofilm morphology compared to the wild-type strain
-
H133A
-
no change in overall periplasmic domain fold, mutant abolishes biofilm formation
-
H55A
-
mutant loses its intrinsic resistance to Zn(II) and meropenem due to the destruction of Zn(II) binding site
-
H97A
-
mutant abolishes biofilm formation
-
L38C/H55A
-
mutation L38C restores the lost responsiveness of mutation H55A to Zn(II) stimulus
-
R94A
-
mutant strain shows biofilm morphology similar to wild-type
-
W150A
-
variant is misfolded
-
H146R
the mutation does not affect the ability to sense copper
H146R/H147R/H149R
the mutant shows minimal copper inducibility compared to wild type CinS
H147R
the mutation has an almost 10fold reduced copper-dependent induction of cinAQ compared to the wild type
H147R/H149R
the mutant shows minimal copper inducibility compared to wild type CinS
H149R
the mutation does not affect the ability to sense copper
H37R
the mutation has an almost 10fold reduced copper-dependent induction of cinAQ compared to the wild type
H146R/H147R/H149R
-
the mutant shows minimal copper inducibility compared to wild type CinS
-
H147R
-
the mutation has an almost 10fold reduced copper-dependent induction of cinAQ compared to the wild type
-
H147R/H149R
-
the mutant shows minimal copper inducibility compared to wild type CinS
-
H149R
-
the mutation does not affect the ability to sense copper
-
H37R
-
the mutation has an almost 10fold reduced copper-dependent induction of cinAQ compared to the wild type
-
A143G
-
the mutant still has some divalent cation-mediated repression and therefore likely have some ability to bind cations
D110A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
E115A
-
the mutant still has some divalent cation-mediated repression and therefore likely have some ability to bind cations
E133A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
E77A
-
the mutant still has some divalent cation-mediated repression and therefore likely have some ability to bind cations
G139A
-
the mutant still has some divalent cation-mediated repression and therefore likely have some ability to bind cations
L137A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
L158A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
S145A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
G394A/G396A
-
completely inactive
H271Y
introducing the mutation into wild-type activates the WalKR regulon. Zn2+ is tetrahedrally-coordinated by four amino acids including H271. The H271Y mutation abrogates metal binding, increasing WalK kinase activity and WalR phosphorylation. The mutant strain shows increased lysostaphin and vancomycin sensitivity
L128C
site-directed mutagenesis
N44C/G142C
site-directed mutagenesis, the monomeric band intensities of the double mutant are dramatically decreased
N44C/G143C
site-directed mutagenesis, the monomeric band intensities of the double mutant are dramatically decreased
N44C/R146C
site-directed mutagenesis, introducing cysteine substitution at Arg146 of YycG N44C mutant does not show any high molecular weight bands, but it shows only the dimeric band of YycG N44C
S81C
site-directed mutagenesis
L128C
-
site-directed mutagenesis
-
N44C/G142C
-
site-directed mutagenesis, the monomeric band intensities of the double mutant are dramatically decreased
-
N44C/G143C
-
site-directed mutagenesis, the monomeric band intensities of the double mutant are dramatically decreased
-
S81C
-
site-directed mutagenesis
-
D326A/N337A
site-directed mutagenesis, the mutant is inactive in autophosphorylation
D326A/Q330A
site-directed mutagenesis, the mutant shows highly reduced autophosphorylation activity compared to the wild-type enzyme
F383A/R385A
site-directed mutagenesis, the mutant shows highly reduced autophosphorylation activity compared to the wild-type enzyme
N334A/N337A
site-directed mutagenesis, the mutant is nearly as active as the wild-type enzyme in autophosphorylation
P222A
site-directed mutagenesis, the mutation eliminates the phosphatase activity of the enzyme
P222G
site-directed mutagenesis, the mutant shows phosphatase activity similar to the wild-type enzyme
Q297A/I298A
site-directed mutagenesis, the mutant is nearly as active as the wild-type enzyme in autophosphorylation
R294A
site-directed mutagenesis, the mutant is nearly as active as the wild-type enzyme in autophosphorylation
T221A
site-directed mutagenesis, the mutation eliminates the phosphatase activity but does not affect the autokinase activity of the enzyme
D326A/Q330A
-
site-directed mutagenesis, the mutant shows highly reduced autophosphorylation activity compared to the wild-type enzyme
-
N334A/N337A
-
site-directed mutagenesis, the mutant is nearly as active as the wild-type enzyme in autophosphorylation
-
Q297A/I298A
-
site-directed mutagenesis, the mutant is nearly as active as the wild-type enzyme in autophosphorylation
-
R294A
-
site-directed mutagenesis, the mutant is nearly as active as the wild-type enzyme in autophosphorylation
-
T221A
-
site-directed mutagenesis, the mutation eliminates the phosphatase activity but does not affect the autokinase activity of the enzyme
-
D326A/N337A
site-directed mutagenesis, the mutation abolishes VicK autokinase activity
D326A/Q330A
site-directed mutagenesis, the mutation highly suppresses VicK autokinase activity
F383A/R385A
site-directed mutagenesis, the mutation highly suppresses VicK autokinase activity
I403S
site-directed mutagenesis, the mutation does not significantly affect VicK autokinase activity
I403W
site-directed mutagenesis, the mutation does not significantly affect VicK autokinase activity but dramatically increases autokinase activity in HK853
K341A/Y342A
site-directed mutagenesis, the mutation negatively affects autokinase activity
N334A/N337A
site-directed mutagenesis, the mutation only slightly affects the autokinase activity of the enzyme compared to the wild-type
P222A
site-directed mutagenesis, the mutant abolishes enzyme VicK's phosphatase activity
P222G
site-directed mutagenesis, the mutant retains full autokinase activity when compared to wild-type, but the mutation abolishes the VicK phosphatase activity
Q297A/I298A
site-directed mutagenesis, the mutation only slightly affects the autokinase activity of the enzyme compared to the wild-type
R294A
site-directed mutagenesis, the mutation only slightly affects the autokinase activity of the enzyme compared to the wild-type
T221A
site-directed mutagenesis, the mutant retains full autokinase activity but the enzyme VicK's phosphatase activity is abolished
T221A/P222A/P222G/V212A/V215A/S213A/S216A
site-directed mutagenesis, the mutation only slightly reduces autokinase activity, while it abolishes the VicK phosphatase activity
V212A/V215A/S213A/S216A
site-directed mutagenesis, the mutation only slightly reduces autokinase activity, while it abolishes the VicK phosphatase activity
N334A/N337A
-
site-directed mutagenesis, the mutation only slightly affects the autokinase activity of the enzyme compared to the wild-type
-
Q297A/I298A
-
site-directed mutagenesis, the mutation only slightly affects the autokinase activity of the enzyme compared to the wild-type
-
R294A
-
site-directed mutagenesis, the mutation only slightly affects the autokinase activity of the enzyme compared to the wild-type
-
T221A
-
site-directed mutagenesis, the mutant retains full autokinase activity but the enzyme VicK's phosphatase activity is abolished
-
E281A
-
site-directed mutagenesis
G457V
-
site-directed mutagenesis
H280V
-
site-directed mutagenesis
I332V
-
site-directed mutagenesis
T284A
-
site-directed mutagenesis
E105A
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E105L
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E105Q
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E107A
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E107L
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E107Q
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E83A
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E83L
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E83L/E105L/E107A
site-directed mutagenesis, the mutant is pH-independent and mimics the low pH structure
E83Q
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E107A
-
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
-
E107Q
-
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
-
E83A
-
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
-
E83Q
-
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
-
D156A
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
D300A
site-directed mutagenesis, the mutation might change the dimeric configuration of the PAS domain, thereby enhancing the negative effect on kinase activity. The D300A-mutated PAS domain of Hik33 also forms dimer in the assay. The Hik33n-SphSc mutant shows reduced expression under non-stressed and salt-stressed conditions compared to unaltered Hik33n-SphSc
D389A
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
D412N
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
E416Q
site-directed mutagenesis, the Hik33n-SphSc mutant shows normal expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
G123A
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
G405A
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
G405S
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and no expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
N309A
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
P114A
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
Q141A
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
Q22A
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2nHik7c construct is inactive in alkaline phosphatase activity
Q411E
site-directed mutagenesis, the Hik33n-SphSc mutant shows normal expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
R129K
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
R377A
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
R400S/R404A
site-directed mutagenesis, the Hik33n-SphSc mutant shows normal expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
R404A
site-directed mutagenesis, the Hik33n-SphSc mutant shows normal expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
R415E
site-directed mutagenesis, the mutation might change the dimeric configuration of the PAS domain, thereby enhancing the negative effect on kinase activity. The Hik33n-SphSc mutant shows reduced expression under non-stressed and salt-stressed conditions compared to unaltered Hik33n-SphSc
T409V
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and no expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
T414V
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and no expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
V395A
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
W134F
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
W318A
site-directed mutagenesis, the mutation might change the dimeric configuration of the PAS domain, thereby enhancing the negative effect on kinase activity. The W318A-mutated PAS domain of Hik33 also forms dimer in the assay. The Hik33n-SphSc mutant shows reduced expression under non-stressed and salt-stressed conditions compared to unaltered Hik33n-SphSc
D449A
-
site-directed mutagenesis, the mutation in the ATP-binding pocket prevents nucleotide binding
H405Y
-
site-directed mutagenesis, the mutation abrogates the kinase activity
H45K
-
site-directed mutagenesis, a CheAFL variant that lacks the substrate His
H45K/H405Y
-
site-directed mutagenesis, the mutant shows reduced kinase activity compared to the wild-type
H45K/S492C
-
site-directed mutagenesis
S492C
-
site-directed mutagenesis
H222A
-
lacks phosphorylation activities
RD51A
-
lacks phosphorylation activities
H222A
-
lacks phosphorylation activities
-
RD51A
-
lacks phosphorylation activities
-
S147L
a BA2291 mutant, which mimics the behavior of the overexpressed wild-type protein.The S147L mutation does not affect the interaction of the kinase with Spo0F or the rate of phosphoryl group transfer to it
S147L
-
a BA2291 mutant, which mimics the behavior of the overexpressed wild-type protein.The S147L mutation does not affect the interaction of the kinase with Spo0F or the rate of phosphoryl group transfer to it
-
H188V
the mutant retains the phosphatase activity of the wild type protein, the mutation triggers formation of an N-terminal 2-helical coiled-coil and extensive dimerization and histidine phosphotransfer domain-ATP-binding domain association
H188V
site-directed mutagenesis of the catalytic domain residue
C69A
-
mutant in LOV-HK knockout background does not return the replication rate to the wild-type level
C69A
-
LOV-HK mutant, binds flavin mononucleotide but cannot form the cysteinyl adduct, does not activate the kinase in response to illumination
D131A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
D131A
-
the purified mutant enzyme shows no fluorescence change well into the mM range of Mg2+, suggesting that this mutation renders the protein incapable of binding Mg2+
D131A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
D131A
-
the purified mutant enzyme shows no fluorescence change well into the mM range of Mg2+, suggesting that this mutation renders the protein incapable of binding Mg2+
R382A/R385A
site-directed mutagenesis, the mutant is inactive in autophosphorylation
R382A/R385A
site-directed mutagenesis, the mutant shows highly reduced autophosphorylation activity compared to the wild-type enzyme
R382A/R385A
site-directed mutagenesis, the mutation abolishes VicK autokinase activity
R382A/R385A
site-directed mutagenesis, the mutation highly suppresses VicK autokinase activity
additional information
-
removal of the first 280 amino acids of VirA, referred to as VirA(LKR), and further removal of the charged residues VirA(LKR)D280-284, preserves basic wild-type induction in response to acetosyringone. Further truncation to VirA(LKR)D280-293 eliminates induction by acetosyringone while increasing the induction of 2,6-dimethoxyphenol, which lacks the para substituent of acetosyringone. Construction of the truncated construct VirA(LKR)D280-284, amino acid residues 285-293 are randomly mutagenized, and the resulting colonies are probed for altered specificity in a sequential phenol specificity screen
additional information
-
removal of the first 280 amino acids of VirA, referred to as VirA(LKR), and further removal of the charged residues VirA(LKR)D280-284, preserves basic wild-type induction in response to acetosyringone. Further truncation to VirA(LKR)D280-293 eliminates induction by acetosyringone while increasing the induction of 2,6-dimethoxyphenol, which lacks the para substituent of acetosyringone. Construction of the truncated construct VirA(LKR)D280-284, amino acid residues 285-293 are randomly mutagenized, and the resulting colonies are probed for altered specificity in a sequential phenol specificity screen
-
additional information
construction of enzyme-deficient mutant strain rscS*DELTAbinK sypG::Tnerm, competition assays of wild-type and mutant strains in vitro and in vivo, overview. DELTAbinK has no effect in the pSypG sypE+ background
additional information
-
construction of enzyme-deficient mutant strain rscS*DELTAbinK sypG::Tnerm, competition assays of wild-type and mutant strains in vitro and in vivo, overview. DELTAbinK has no effect in the pSypG sypE+ background
additional information
-
construction of enzyme-deficient mutant strain rscS*DELTAbinK sypG::Tnerm, competition assays of wild-type and mutant strains in vitro and in vivo, overview. DELTAbinK has no effect in the pSypG sypE+ background
-
additional information
generation of an enzyme deletion mutant strain by gene disruption of AaHSK1 using a hygromycin phosphotransferase gene (HYG) cassette
additional information
-
generation of an enzyme deletion mutant strain by gene disruption of AaHSK1 using a hygromycin phosphotransferase gene (HYG) cassette
additional information
-
generation of an enzyme deletion mutant strain by gene disruption of AaHSK1 using a hygromycin phosphotransferase gene (HYG) cassette
-
additional information
-
construction of ahk5 T-DNA insertion mutants, Arabidopsis mutants lacking AHK5 show reduced stomatal closure in response to H2O2, which is reversed by complementation with the wild type gene. Overexpression of AHK5 results in constitutively less stomatal closure. Abiotic stimuli that generate endogenous H2O2, such as darkness, nitric oxide and the phytohormone ethylene, also show reduced stomatal closure in the ahk5 mutants. However, ABA causes closure, dark adaptation induces H2O2 production and H2O2 induces NO synthesis in mutants, phenotype, overview
additional information
-
generation of CKI1 loss-of-function mutants. Transformation of egg cell to central cell by ectopic CKI1 retains female gametophyte organization
additional information
generation of the ahk5-1 mutant containing a T-DNA insertion in the receiver domain of the AHK5 histidine kinase. The AHK5 mutant is more resistant to salt stress. Two complemented lines, PAHK5-AHK5/ahk5-1-1 and PAHK5-AHK5/ahk5-1-4, are generated by complementation of the ahk5-1 mutant with full-length AHK5 including 3205 bases upstream of the ATG start codon
additional information
-
generation of the ahk5-1 mutant containing a T-DNA insertion in the receiver domain of the AHK5 histidine kinase. The AHK5 mutant is more resistant to salt stress. Two complemented lines, PAHK5-AHK5/ahk5-1-1 and PAHK5-AHK5/ahk5-1-4, are generated by complementation of the ahk5-1 mutant with full-length AHK5 including 3205 bases upstream of the ATG start codon
additional information
the T-DNA insertion is transmitted through female gametophytes at an extremely low frequency in CKI1/cki1-8 plants, while cki1-6 mutation, which carries a T-DNA at a more distal location in the CKI1 promoter than cki1-8 mutatin does not appear to be capable of being transmitted through female gametophytes. The cki1-8 mutation impairs female gametophyte development, cki1-8 mutant phenotype during reproductive development and vegetative growth. Mutant phenotypes, overview
additional information
-
generation of CKI1 loss-of-function mutants. Transformation of egg cell to central cell by ectopic CKI1 retains female gametophyte organization
-
additional information
-
the T-DNA insertion is transmitted through female gametophytes at an extremely low frequency in CKI1/cki1-8 plants, while cki1-6 mutation, which carries a T-DNA at a more distal location in the CKI1 promoter than cki1-8 mutatin does not appear to be capable of being transmitted through female gametophytes. The cki1-8 mutation impairs female gametophyte development, cki1-8 mutant phenotype during reproductive development and vegetative growth. Mutant phenotypes, overview
-
additional information
-
generation of the ahk5-1 mutant containing a T-DNA insertion in the receiver domain of the AHK5 histidine kinase. The AHK5 mutant is more resistant to salt stress. Two complemented lines, PAHK5-AHK5/ahk5-1-1 and PAHK5-AHK5/ahk5-1-4, are generated by complementation of the ahk5-1 mutant with full-length AHK5 including 3205 bases upstream of the ATG start codon
-
additional information
the BA2291 gene is capable of complementing Bacillus subtilis sporulation kinase-deficient mutants when present in the cell in single copy, and its deletion in Bacillus anthracis strongly reduces the ability of the organism to sporulate. BA2291 overexpression in Bacillus subtilis completely prevents sporulation, also in a wild type strain
additional information
-
the BA2291 gene is capable of complementing Bacillus subtilis sporulation kinase-deficient mutants when present in the cell in single copy, and its deletion in Bacillus anthracis strongly reduces the ability of the organism to sporulate. BA2291 overexpression in Bacillus subtilis completely prevents sporulation, also in a wild type strain
additional information
-
the BA2291 gene is capable of complementing Bacillus subtilis sporulation kinase-deficient mutants when present in the cell in single copy, and its deletion in Bacillus anthracis strongly reduces the ability of the organism to sporulate. BA2291 overexpression in Bacillus subtilis completely prevents sporulation, also in a wild type strain
-
additional information
a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking the N-terminal Per-ARNT-Sim domain, which plays a critical role in the catalytic activity of this enzyme
additional information
-
a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking the N-terminal Per-ARNT-Sim domain, which plays a critical role in the catalytic activity of this enzyme
additional information
YycG depletion does not interfere with FtsZ localization, YycG is less active as a kinase of YycF in the absence of a division septum
additional information
-
YycG depletion does not interfere with FtsZ localization, YycG is less active as a kinase of YycF in the absence of a division septum
additional information
deletion in the abrB gene suppresses the DELTAkinD mutation
additional information
-
deletion in the abrB gene suppresses the DELTAkinD mutation
additional information
generation of a KinD-DegS hybrid kinase using overlapping PCR, overview. DegS is a sensory histidine kinase that is able to phosphorylate DegU, a DNA-binding response regulator. The DegS-DegU system controls many genes (both positively and negatively) including the fla/che operon that encodes dozens of genes involved in motility and chemotaxis
additional information
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generation of a KinD-DegS hybrid kinase using overlapping PCR, overview. DegS is a sensory histidine kinase that is able to phosphorylate DegU, a DNA-binding response regulator. The DegS-DegU system controls many genes (both positively and negatively) including the fla/che operon that encodes dozens of genes involved in motility and chemotaxis
additional information
generation of several truncation mutant of enzyme YycG. All truncated YycG constructs including the shortest one that featured only the cytoplasmic PAS and the two catalytic HisKA and HATPase domains retain the ability to localize to the septum. N-terminal truncations of YycG lose negative regulation of their activity, truncated YycG constructs fail to co-immunoprecipitate with the regulatory proteins YycH and YycI
additional information
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generation of several truncation mutant of enzyme YycG. All truncated YycG constructs including the shortest one that featured only the cytoplasmic PAS and the two catalytic HisKA and HATPase domains retain the ability to localize to the septum. N-terminal truncations of YycG lose negative regulation of their activity, truncated YycG constructs fail to co-immunoprecipitate with the regulatory proteins YycH and YycI
additional information
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in vivo quantitative domain-based stepwise deletion analyses to determine the minimum functional domain of KinC, overview
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a truncated version of DesK, which lacks the transmembrane domain, is not pH-dependent
additional information
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a truncated version of DesK, which lacks the transmembrane domain, is not pH-dependent
additional information
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in vivo quantitative domain-based stepwise deletion analyses to determine the minimum functional domain of KinC, overview
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additional information
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deletion in the abrB gene suppresses the DELTAkinD mutation
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additional information
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generation of a KinD-DegS hybrid kinase using overlapping PCR, overview. DegS is a sensory histidine kinase that is able to phosphorylate DegU, a DNA-binding response regulator. The DegS-DegU system controls many genes (both positively and negatively) including the fla/che operon that encodes dozens of genes involved in motility and chemotaxis
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additional information
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a truncated version of DesK, which lacks the transmembrane domain, is not pH-dependent
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additional information
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a significant decrease occurs of the autophosphorylation rate of a KinA protein lacking the N-terminal Per-ARNT-Sim domain, which plays a critical role in the catalytic activity of this enzyme
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additional information
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generation of several truncation mutant of enzyme YycG. All truncated YycG constructs including the shortest one that featured only the cytoplasmic PAS and the two catalytic HisKA and HATPase domains retain the ability to localize to the septum. N-terminal truncations of YycG lose negative regulation of their activity, truncated YycG constructs fail to co-immunoprecipitate with the regulatory proteins YycH and YycI
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additional information
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bos1-null mutants, osmosensitivity and resistance to fungicides, very rarely form conidiophores and those few conidiophores fail to produce conidia, this defect can be partially restored with 1000 mM sorbitol. Mutants are not hypersensitive to various oxidative stresses but are more resistant to menadione, have significantly reduced ability to infect host plants. Appressorium morphogenesis is not altered, however, in planta growth is severely reduced
additional information
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bos1-null mutants, osmosensitivity and resistance to fungicides, very rarely form conidiophores and those few conidiophores fail to produce conidia, this defect can be partially restored with 1000 mM sorbitol. Mutants are not hypersensitive to various oxidative stresses but are more resistant to menadione, have significantly reduced ability to infect host plants. Appressorium morphogenesis is not altered, however, in planta growth is severely reduced
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additional information
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deletion of the pdhS in the presence of a rescue copy expressed from pRH232, pRH232 is replaced in the deltapdhS strain only in the presence of another wild-type copy of pdhS through pRH404
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insertion-knockout mutant strain by introduction of a kanamycin-resistant cassette into the gene, replication is less than the wild-type strain as early as 4 hours after infection with J774A.1 murine macrophages
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construction of a LOVHK knockout mutant
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construction of a LOVHK knockout mutant
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construction of a LOVHK knockout mutant
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additional information
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deletion of the pdhS in the presence of a rescue copy expressed from pRH232, pRH232 is replaced in the deltapdhS strain only in the presence of another wild-type copy of pdhS through pRH404
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additional information
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generation of two different versions of the HK domain: one long (L, the HK domain plus a 23-kDa tag, 49 kDa) and other short (S, 26 kDa). The short version has the N388A mutation which impairs the phosphorylation capacity. Both versions have the I286C mutation
additional information
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the disruption of a PAS-like motif in the sensor domain affects the stability of CckA accumulation at the poles accompanied by a partial loss in CckA function. Shortening of an extended linker between beta-sheets within the CckA catalysis-assisting ATP-binding domain leads to a dramatic cell-to-cell variability in CpdR levels and CtrA cell cycle periodicity
additional information
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in the deltamtrAB mutant, the expression of carrier genes is abolished (betP) or markedly reduced, MtrB mutants in which either the large periplasmic loop or the HAMP domain is deleted, are regulated similar to wild-type MtrB
additional information
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ethanolamine utilization and growth on it is abolished in the response regulator RR17 mutant strain lacking a functional partner of histidine kinase in the RR-HK17 two-component system, phenotype, overview
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cheA mutations leading to defects in chemotaxis are mapped and characterized
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the histidine phosphorylation sites of each TorS transmitter domain and the aspartate phosphorylation site of the TorS receiver are individually changed by site-directed mutagenesis. All three phosphorylation sites proved essential for in vivo induction of the tor structural operon and for in vitro transphosphorylation of the cognate TorR response regulator. The His to Gln change in the classical transmitter domain abolished TorS autophosphorylation, whereas TorS undergoes significant autophosphorylation when the phosphorylation site of its receiver or alternative transmitter is changed
additional information
construction of several phoR genes, with various deletions in the 5' regions, which are regulated by the trp-lac hybrid promoter. The PhoR1084 and PhoR1159 proteins that lack the 83 and 158 N-terminal amino acids, respectively, retain the positive function for the expression of phoA that codes for alkaline phosphatase, but lack the negative function. The PhoR1263 protein that lacks the 262 N-terminal amino acids is deficient in both functions
additional information
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mutations within the linker HAMP domain block the osmosensing function of EnvZ
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construction of a DELTAcusS enzyme nockout mutant in an Escherichia coli strain in which the chromosomal copy of the gene for the multicopper oxidase CueO has been deleted (DELTAcueO). CueO converts Cu(I) to Cu(II) and therefore the use of the strain with the cueO deletion allows the observation of a growth phenotype even under aerobic conditions. The chromosomal copy of cusS is deleted from this background strain to allow characterization of CusS variants expressed from a plasmid. Partial functional complementation ofthe mutant strain with lasmid-expressed wild-type enzyme. The mutations do not significantly affect the relative expression levels of CusS
additional information
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construction of a DELTAcusS enzyme nockout mutant in an Escherichia coli strain in which the chromosomal copy of the gene for the multicopper oxidase CueO has been deleted (DELTAcueO). CueO converts Cu(I) to Cu(II) and therefore the use of the strain with the cueO deletion allows the observation of a growth phenotype even under aerobic conditions. The chromosomal copy of cusS is deleted from this background strain to allow characterization of CusS variants expressed from a plasmid. Partial functional complementation ofthe mutant strain with lasmid-expressed wild-type enzyme. The mutations do not significantly affect the relative expression levels of CusS
additional information
construction of a functional chimeric protein, equivalent to the full cytosolic part of EnvZ, encompassing the entire catalytic part of the Escherichia coli EnvZ histidine kinase, fused to the HAMP domain of the Archaeoglobus fulgidus Af1503 receptor, generation of a second chimeric mutant version with additional A291F exchange
additional information
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construction of a functional chimeric protein, equivalent to the full cytosolic part of EnvZ, encompassing the entire catalytic part of the Escherichia coli EnvZ histidine kinase, fused to the HAMP domain of the Archaeoglobus fulgidus Af1503 receptor, generation of a second chimeric mutant version with additional A291F exchange
additional information
construction of EvgS-PhoQ chimeras and activation of these chimera sensors, overview. The EvgS sensor domain is fused to the cytoplasmic region of PhoQ to examine whether it still responded to the signals. In chimera PvgS-A, the region from the N terminus to the transmembrane region of EvgS (residues 1 to 558 of EvgS) is fused to the cytoplasmic region of PhoQ (residues 215 to 486 of PhoQ) comprising the HAMP, HisKA, and HATPase_c domains, and in chimera PvgS-B, the region from the N terminus to the linker domain of EvgS (residues 1 to 710 of EvgS) is fused to the HisKA and HATPase_c domains of PhoQ (residues 267 to 486 of PhoQ)
additional information
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construction of EvgS-PhoQ chimeras and activation of these chimera sensors, overview. The EvgS sensor domain is fused to the cytoplasmic region of PhoQ to examine whether it still responded to the signals. In chimera PvgS-A, the region from the N terminus to the transmembrane region of EvgS (residues 1 to 558 of EvgS) is fused to the cytoplasmic region of PhoQ (residues 215 to 486 of PhoQ) comprising the HAMP, HisKA, and HATPase_c domains, and in chimera PvgS-B, the region from the N terminus to the linker domain of EvgS (residues 1 to 710 of EvgS) is fused to the HisKA and HATPase_c domains of PhoQ (residues 267 to 486 of PhoQ)
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engineering of covalent dimers of the cytoplasmic domains of CpxA which provide a robust experimental system for investigating cooperativity in histidine kinase autophosphorylation
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His226 is required for induction and is structurally colocated with Pro522 at the top of the predicted transmembrane helix. The constitutive mutations in the PAS domain can be further activated by low external pH. Expression of the cytoplasmic part of the protein alone also gives constitutive activation, which is lost if the constitutive PAS mutations are present. The cytoplasmic part shows pH-dependent dimer formation in vitro
additional information
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His226 is required for induction and is structurally colocated with Pro522 at the top of the predicted transmembrane helix. The constitutive mutations in the PAS domain can be further activated by low external pH. Expression of the cytoplasmic part of the protein alone also gives constitutive activation, which is lost if the constitutive PAS mutations are present. The cytoplasmic part shows pH-dependent dimer formation in vitro
additional information
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growth of HP0244 mutant strain is similar to the growth of the wild-type strain, null mutations in either HP0165 or HP1364 histidine kinases are impaired in their ability to grow at pH 5.0, acid-responsive gene transcription is altered in the HP0165 and HP1364 null mutant strains compared to the parental wild-type strain, growth of complemented mutant strains is similar to that of the wild-type strain
additional information
an acid survival study using an HP0703 mutant and an electrophoretic mobility shift assay with in vitro-phosphorylated HP0703 showe, that HP0703 does not contribute to acid survival and does not bind to the promoter regions of several genes in the HP0244 pH-dependent regulon, suggesting that there is a pathway outside the HP0703 regulon which transduces the acid-responsive signal sensed by HP0244
additional information
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an acid survival study using an HP0703 mutant and an electrophoretic mobility shift assay with in vitro-phosphorylated HP0703 showe, that HP0703 does not contribute to acid survival and does not bind to the promoter regions of several genes in the HP0244 pH-dependent regulon, suggesting that there is a pathway outside the HP0703 regulon which transduces the acid-responsive signal sensed by HP0244
additional information
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delayed timing of aggregation, frequent sporulation outside fruiting bodies, and irregular fruiting body morphology on CF agar, no aggregation of fruiting bodies in submerged culutre
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construction of several mutants by in-frame deletions, espA mutants, encoding an orphan hybrid histidine kinase, alter the timing of the organism's developmental program, greatly accelerating developmental progression, phenotype, overview
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construction of several mutants by in-frame deletions, espA mutants, encoding an orphan hybrid histidine kinase, alter the timing of the organism's developmental program, greatly accelerating developmental progression, phenotype, overview
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deletion of 7 N-terminal enzyme residues affects dimer organization
additional information
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enzyme FimS from W83 is malfunctional and has a defective kinase domain due to a truncated conserved G3 box motif that provides an ATP-binding pocket. The introduction of the functional fimS from strain ATCC 33277 restores the production, but not polymerization, of endogenous FimA subunits in W83. Substantial expression of strain ATCC 33277-type FimA fimbriae in the strain W83 derivative requires the introduction and expression of the functional strain ATCC 33277 fimS
additional information
enzyme FimS from W83 is malfunctional and has a defective kinase domain due to a truncated conserved G3 box motif that provides an ATP-binding pocket. The introduction of the functional fimS from strain ATCC 33277 restores the production, but not polymerization, of endogenous FimA subunits in W83. Substantial expression of strain ATCC 33277-type FimA fimbriae in the strain W83 derivative requires the introduction and expression of the functional strain ATCC 33277 fimS
additional information
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enzyme FimS from W83 is malfunctional and has a defective kinase domain due to a truncated conserved G3 box motif that provides an ATP-binding pocket. The introduction of the functional fimS from strain ATCC 33277 restores the production, but not polymerization, of endogenous FimA subunits in W83. Substantial expression of strain ATCC 33277-type FimA fimbriae in the strain W83 derivative requires the introduction and expression of the functional strain ATCC 33277 fimS
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additional information
construction of diverse point, truncation, and deletion mutants of enzyme GacS, and generation of diverse two-hybrid constructs of enzyme GacS domains
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construction of diverse point, truncation, and deletion mutants of enzyme GacS, and generation of diverse two-hybrid constructs of enzyme GacS domains
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construction of diverse point, truncation, and deletion mutants of enzyme GacS, and generation of diverse two-hybrid constructs of enzyme GacS domains
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construction of diverse point, truncation, and deletion mutants of enzyme LadS, and generation of diverse two-hybrid constructs of enzyme LadS domains
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construction of diverse point, truncation, and deletion mutants of enzyme LadS, and generation of diverse two-hybrid constructs of enzyme LadS domains
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construction of diverse point, truncation, and deletion mutants of enzyme LadS, and generation of diverse two-hybrid constructs of enzyme LadS domains
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generation of a Shk1 deletion mutant, all the defects are restored by genetic complementation of the Shk1 deletion mutant with the wild-type Shk1 gene
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generation of a Shk1 deletion mutant, all the defects are restored by genetic complementation of the Shk1 deletion mutant with the wild-type Shk1 gene
additional information
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generation of a Shk1 deletion mutant, all the defects are restored by genetic complementation of the Shk1 deletion mutant with the wild-type Shk1 gene
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additional information
a point mutation in SaeS of strain Newman is responsible for increased expression of Eap upon exposure to sublethal Perform and SDS concentrations, leading to increased extracellular adherence protein-dependent cellular invasiveness
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a point mutation in SaeS of strain Newman is responsible for increased expression of Eap upon exposure to sublethal Perform and SDS concentrations, leading to increased extracellular adherence protein-dependent cellular invasiveness
additional information
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construction of a truncated AgrCTM5-6C enzyme version, a hydrophobic polypeptide of 297 amino acids, that has two transmembrane helices connected by a small polar loop that is exposed to the periplasm
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cross-linking of the recombinant the SeMet-substituted YycG enzyme
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cross-linking of the recombinant the SeMet-substituted YycG enzyme
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a point mutation in SaeS of strain Newman is responsible for increased expression of Eap upon exposure to sublethal Perform and SDS concentrations, leading to increased extracellular adherence protein-dependent cellular invasiveness
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additional information
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cross-linking of the recombinant the SeMet-substituted YycG enzyme
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additional information
deletion of the first G loop (del392-395, RAQG) negatively affects autokinase activity
additional information
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deletion of the first G loop (del392-395, RAQG) negatively affects autokinase activity
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additional information
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genetic inactivation of covS decreases but does not eliminate CovR phosphorylation
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generation of and draK gene deletion mutants, the gene disruption plasmids pKC-3063A and pKC-3062B are delivered into Streptomyces coelicolor A3(2) cells by conjugation with Escherichia coli ET12567(pUZ8002), and intergeneric conjugation between Escherichia coli and Streptomyces is performed, altered pH profile after acidic pH shock cultivation of the draR and draK gene deletion mutants, overview
additional information
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generation of and draK gene deletion mutants, the gene disruption plasmids pKC-3063A and pKC-3062B are delivered into Streptomyces coelicolor A3(2) cells by conjugation with Escherichia coli ET12567(pUZ8002), and intergeneric conjugation between Escherichia coli and Streptomyces is performed, altered pH profile after acidic pH shock cultivation of the draR and draK gene deletion mutants, overview
additional information
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generation of and draK gene deletion mutants, the gene disruption plasmids pKC-3063A and pKC-3062B are delivered into Streptomyces coelicolor A3(2) cells by conjugation with Escherichia coli ET12567(pUZ8002), and intergeneric conjugation between Escherichia coli and Streptomyces is performed, altered pH profile after acidic pH shock cultivation of the draR and draK gene deletion mutants, overview
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additional information
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construction of a senS disruption and a truncated mutant
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construction of a senS disruption and a truncated mutant
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inactivation of each putative hik gene, no significant alterations in gene expression in most of the mutants. DeltaHik33 and deltaHik19 exhibit reduced ability to activate luciferase at low temperature. Deltahik27, deltahik34, and deltahik20 show enhanced expression of some genes, whereas others are repressed. In deltaHik34 cells, levels of transcripts of heat-shock genes are elevated. In deltaHik33-, deltaHik34-, deltaHik16-, and deltaHik41-mutant cells gene expression is significantly affected by elevated levels of NaCl
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mutation of hik41 does not affect the expression of the genes located downstream of this gene, 22 H2O2-inducible genes are either totally or almost totally unresponsive to H2O2 in deltaHik33 mutant cells, whereas mutation of Hik34, Hik16 or Hik41 abolishes the H2O2 induction of only two genes, Hik16 and Hik41 regulate the H2O2-inducible expression of the same two genes
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construction of a fused sensor, Hik2n-Hik7c, which has the signal input domain of Hik2 and the kinase domain of the phosphate-deficiency sensor Hik7. The coding region of the hik7 gene is replaced with the fused sensor to evaluate the signalling activity in vivo as the activity of alkaline phosphatase (AP), which is regulated by Hik7. Cells expressing Hik2n-Hik7c have weak AP activities under standard growth conditions. Saline stress by NaCl induces AP activity in a dose-dependent manner. Hik2n-Hik7c responds to Cl- concentration. Amino acid substitutions in the signal input domain of Hik2 all result in loss of this responsiveness, i.e. mutants Q22A, P114A, G123A, R129K, W134F, Q141A and D156A completely lose AP activity
additional information
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construction of a fused sensor, Hik2n-Hik7c, which has the signal input domain of Hik2 and the kinase domain of the phosphate-deficiency sensor Hik7. The coding region of the hik7 gene is replaced with the fused sensor to evaluate the signalling activity in vivo as the activity of alkaline phosphatase (AP), which is regulated by Hik7. Cells expressing Hik2n-Hik7c have weak AP activities under standard growth conditions. Saline stress by NaCl induces AP activity in a dose-dependent manner. Hik2n-Hik7c responds to Cl- concentration. Amino acid substitutions in the signal input domain of Hik2 all result in loss of this responsiveness, i.e. mutants Q22A, P114A, G123A, R129K, W134F, Q141A and D156A completely lose AP activity
additional information
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generation of a series of chimeric proteins that include the N-terminal region of Hik33 (M1-A422) and the C-terminal region (Q197-P430) of SphS, a histidine kinase that senses phosphate-deficient conditions. The chimeric protein Hik33n-SphSc regulates expression of the phoA gene under stress conditions. Under standard growth conditions, cells that harbor the gene for Hik33n-SphSc express phoA, whereas the expression of phoA is repressed under salt stress and under cold stress
additional information
generation of a series of chimeric proteins that include the N-terminal region of Hik33 (M1-A422) and the C-terminal region (Q197-P430) of SphS, a histidine kinase that senses phosphate-deficient conditions. The chimeric protein Hik33n-SphSc regulates expression of the phoA gene under stress conditions. Under standard growth conditions, cells that harbor the gene for Hik33n-SphSc express phoA, whereas the expression of phoA is repressed under salt stress and under cold stress
additional information
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generation of a series of chimeric proteins that include the N-terminal region of stress regulator histidine kinase Hik33 (M1-A422) and the C-terminal region (Q197-P430) of SphS. The chimeric protein Hik33n-SphSc regulates expression of the phoA gene under stress conditions. Under standard growth conditions, cells that harbor the gene for Hik33n-SphSc express phoA, whereas the expression of phoA is repressed under salt stress and under cold stress
additional information
generation of a series of chimeric proteins that include the N-terminal region of stress regulator histidine kinase Hik33 (M1-A422) and the C-terminal region (Q197-P430) of SphS. The chimeric protein Hik33n-SphSc regulates expression of the phoA gene under stress conditions. Under standard growth conditions, cells that harbor the gene for Hik33n-SphSc express phoA, whereas the expression of phoA is repressed under salt stress and under cold stress
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delta408ThkA, includes the PAS-sensor, the DHp and CA domains, and delta 517ThkA without the PAS-sensor domain, both are fully active in the autophosphorylation reaction
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delta408ThkA, includes the PAS-sensor, the DHp and CA domains, and delta 517ThkA without the PAS-sensor domain, both are fully active in the autophosphorylation reaction
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disulfide cross-linking of mutant enzymes, overview
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truncated His-RaxH, lacking the N-terminal transmembrane region, shows similar autophosphorylation activities than His-tagged full-length RaxH, but is unable to induce phosphorylation of His-RaxR
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truncated His-RaxH, lacking the N-terminal transmembrane region, shows similar autophosphorylation activities than His-tagged full-length RaxH, but is unable to induce phosphorylation of His-RaxR
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AaHSK1 DNA and amino acid sequence determination and analysis, cloning from strain EV-MIL31
cloned from a root cDNA library
cloned from a Salmonella typhi Ty2 cosmid bank and characterized by DNA sequence analysis
cloning of gene AlHK1 from 19 different isolates, DNA and amino acid sequence determination and analysis, sequence comparisons
cloning of the extracellular sensory domain of DraK, consisting of 88 residues (Glu28-Arg115) from genomic DNA, and overexpression as N-terminally His6-tagged protein in Escherichia coli strain BL21(DE3)
cloning of the RR-HK17 TCS system from strain V583
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cytoplasmic expression of TorSS as a fusion protein, containing a hexahistidine tag on the N-terminus separated by a separated by a thrombin protease recognition sequence, in Escherichia coli BL21(DE3) cells
cytoplasmic portion of BvgS ('BvgS) is overexpressed
downstream of a histidine tag into vector pET15b, His-tagged full-length RaxH and RaxR overexpressed in Escherichia coli BL21 cells in the presence of sorbitol and glycine betaine to produce soluble His-RaxH
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ectopic CKI1 expression in all nuclei of the female gametophyte, under the pAKV promoter using the pOp/LhG4 transactivation system, generates non-propagating seeds with dual fertilized endosperms and no embryos, phenotypes, detailed overview
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EL368-LOV-HK and EL346-LOV-HK expressed in Escherichia coli
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Escherichia coli BL21(DE3) cells transformed with different pASK-IBA7-mtrB strep derivatives
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expressed in Escherichia coli
expressed in Escherichia coli BL21 (DE3) CodonPlus RIL-X
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLysS cells
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expressed in Escherichia coli C41(DE3) cells
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expressed in Escherichia coli DH5alpha cells
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expressed in Escherichia coli Rosetta2 DE3 cells
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expressed in Escherichia coli strains BL21(DE3), C41 (DE3), and C43 (DE3)
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expressed in Escherichia coli Tuner cells
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expressed in Saccharomyces cerevisiae
expression in Bacillus subtilis
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expression in Clostridium beijerinckii
expression in Escherichia coli
expression of Hik1 can confer fungicide-sensitivity to Saccharomyces cerevisiae. This requires both the histidine kinase and the response response regulator domain of Hik1
expression of His-tagged 1-121 and truncated DELTA7 H-NOXA domains in Escherichia coli strain BL21(DE3)
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expression of His10-tagged full-length wild-type Ppr in Escherichia coli strain BL21(DE3), overexpression of the PYP domain of Ppr in Escherichia coli, co-expression of the full-length enzyme with tyrosine ammonia-lyase and p-coumaric acid ligase
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expression of residues 10-117 of KinA, fused to an N-terminal His6Gbeta1-tag and a TEV protease site in the tag-protein linker, in Escherichia coli strain BL21(DE3), expresssion of the selenomethionine variant in Escherichia coli strain B834
expression of selenomethionine-labeled DctB residues 28-286 in Escherichia coli strain BL21(DE3)
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expression of selenomethionine-labeled DcuS residues 42-181 in Escherichia coli strain BL21(DE3) as GST-tagged protein
expression of the periplasmic domain of histidine kinase EnvZ(Ala38-Arg162) in Escherichia coli
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expression of these proteins from a multicopy plasmid vector in Escherichia coli
Expression of wild-type and RoxRS mutant strain EU58 (mutant of two-component system) in Escherichia coli
expresssion of GST-tagged wild-type and mutant enzymes, quantitative expression analysis, overview
gene agrC, recombinant overexpression of His-tagged and GFP-tagged truncated enzyme from pET-28a-AgrCTM5-6C or pET-28-AgrCTM5-6C-GFP vector in Escherichia coli strain C43(DE3)
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gene ahk5, transient expression of GST-tagged full-length AHK5 in Arabidopsis thaliana protoplasts and Nicotiana benthamiana leaf cells the fusion protein in the cytoplasm, independent of whether the GFP tag is fused to the N-terminus or C-terminus of AHK5, expression profile of AHK5 in different tissues and cell types by semi-quantitative RT-PCR
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gene BA2291, genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay. Expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene BAB2_0652, recombinant expression f the enzyme in a two-hybrid system with PdhS in frame with the lambdacl gene, coexpression with gene pdhS, recombinant expression of His-tagged lovhk and hk domains in Escherichia coli strain BL21(DE3) pLysS from pET24a plasmid, coexpression of phyR and lovR. Antibiotic resistance complementation assays with the enzyme in Escherichia coli, overview. Realtime quantitative RT-PCR expression analysis
gene CC_0285, recombinant expression of His-tagged wild-type enzyme, enzyme fragments, and mutant C70A enzyme in Escherichia coli strain Rosetta(DE3)pLysS
gene covS, dNA and amino acid sequence determination and analysis
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gene cusS, recombinant expression of the enzyme's periplasmic domain from pTXB3CusSs plasmid, encoding CusS amino acids 39-187 with a chitin binding domain (CBD) affinity tag, in Escherichia coli strain BL21(DE3)
gene desK, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain M15/pREP4
gene fimS, DNA and amino acid sequence determination and analysis, the transcriptional start site of fimS is disrupted in strain W83
gene hik33, the chimeric gene for Hik33n-SphSc, integrated into the chromosomes, is expressed in Synechocystis from the original promoter of the sphS gene, and the copy number of each chimeric gene is exactly one per chromosome, subcloning in Escherichia coli strain JM109. Quantitative expression analysis of unaltered Hik33n-SphSc chimera and mutants under non-stressed conditions and salt-stressed conditions, overview
gene kinD, recombinant expression of the chimeric KinD-DegS hybrid kinase under control of the kinD native promoter in Escherichia coli strain DH5alpha, construct transfection to Bacillus subtilis strain NCIB3610 by SPP1 phage transduction
gene PGN_0904 or fimS, DNA and amino acid sequence determination and analysis, recombinant expression in the enzyme-deficient Porphyromonas gingivalis strain W38, complementation of the fimS variant in trans, strain ATCC 33277 FimS-induced W83 FimA is a mature polypeptide and is localized on the cell surface
gene SCO3062, recombinant expression of N-terminally GST-tagged extracellular sensing domain (residues 28E-124R), and cytoplasmic domain (residues 146R-424R) of DraK in Escherichia coli strain BL21. Because the extracellular sensing domain of DraK is sensitive to proteolysis during purification, the C-terminal truncated short form (residues 28E-115R) is also constructed without the unstable C-terminal sequence (residues 116S-124R) after determination of the cleavage site (residues 115R-116S) in the extracellular sensing domain
gene senS, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain XL-1 Blue
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gene slr1147, recombinant expression of C-terminally poly-His-tagged full-length enzyme in Escherichia coli strain BL21(DE3)
gene sphS, the chimeric gene for Hik33n-SphSc, integrated into the chromosomes, is expressed in Synechocystis from the original promoter of the sphS gene, and the copy number of each chimeric gene is exactly one per chromosome, subcloning in Escherichia coli strain JM109. Quantitative expression analysis of unaltered Hik33n-SphSc chimera and mutants under non-stressed conditions and salt-stressed conditions, overview
gene SS1G_12694, DNa and amino acid sequence determination and analysis, quantitative real-time PCR expression analysis
gene VF_A0360, genotyping, overview, cloning of plasmid pTn7BinK
gene yycG, recombinant expression of trncated enzyme mutants. Expression of a soluble cytoplasmic YycG construct in a bacterial two-hybrid expression system using the full-length YycG or a truncated YycGDELTA211-611 that lacks all cytoplasmic domains, and cell division proteins FtsZ, FtsA, FtsW, DivIB, DivIC, FtsL, Pbp2B, EzrA, ZapA, SepF and MinJ as C-terminal fusions to the individual domains (T18 and T25) of the two-domain Bordatella pertussis adenylate cyclase protein. YycG makes specific interactions with FtsL, DivIB, Pbp2B and interactions with FtsW and EzrA appear also possible
gene yycG, recombinant expression of wild-type and mutant His-tagged enzymes in Escherichia coli strain BL21(DE3), the SeMet-substituted YycG is produced in Escherichia coli methionine auxotrophic strain B834(DE3)
genes phkA, tcsB, nikA, fphA, hk-8-2, and hk-8-5, expression of GFP-tagged enzyme in Aspergillus nidulans strain ABPU1 under the control of an HK promoter, subcloning in Escherichia coli strain JM109, analysis of the temporally and spatially different expression during the cell cycle, overview
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heterologous expression of the plnABCD operon in a Lactobacillus sake strain
into pQE30 and overexpressed in Escherichia coli M15
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into vector pGEM-T, then cloned genes disrupted in HP0244, HP1364, and HP0165 sequences. The resulting plasmids, which are unable to replicate in Helicobacter pylori, introduced into Helicobacter pylori J99
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kanamycin cartridges are inserted into the cloned fixL gene and recombined into the host genome
LOV-HK expressed in Escherichia coli
low-copy plasmid pRH324 expressing Brucella abortus pdhS fused to cfp into Sinorhizobium meliloti or Caulobacter crescentus
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mutant enzymes cloned and expressed in Escherichia coli strain BL21(DE3)
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no heterologous expression of NRII in Escherichia coli
overexpression in Escherichia coli, histidine kinase Hik34
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overexpression of a 36-kDa truncated EnvZ protein, Glu106 to Gly450, that forms inclusion bodies in the cell
overexpression of nonreceptor-type HK gene cytokinin independent1 (CKI1) activates cytokinin signaling, quantitative RT-PCR expression analysis
pBOS1delta linearized and used to transform protoplasts of the UWS111 wild-type strain
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phoP-phoQ operon cloned and expressed in Escherichia coli
profiling of a HP0244 deletion mutant grown at pH 7.4, contribution of HP0244 to sigma(54) activation via HP0703 to coordinate flagellar biosynthesis by a pH-independent regulon that includes 14 flagellar genes. Microarray analysis of cells grown at pH 4.5 without urea reveals an additional 22 genes, including 4 acid acclimation genes, e.g. ureA, ureB, ureI, and amiE, that are positively regulated by HP0244, overview
recombinant expression of C-terminally His-tagged forms of enzyme domains GacSD1, GacSH1D1, GacSH2, and GacSH2H->Q in Escherichia coli strain BTH101, expression of N-terminally FLAG or Strep tagged enzyme fragment constructs
recombinant expression of C-terminally His-tagged forms of enzyme domains LadSH1D1, LadSH1D1D->A, and LadSD1 in Escherichia coli strain BTH101, expression of N-terminally FLAG or Strep tagged enzyme fragment constructs
recombinant expression of His-tagged enzyme KinC in Escherichia coli strain BL21(DE3)
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recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli. The expression of CusS from a plasmid does not result in the same growth phenotype on copper-containing media as the strain that expresses chromosomal CusS
recombinant expression of wild-type and mutant enzyme domains in Escherichia coli strain BL21(DE3)
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recombinant expression of wild-type and mutant enzymes in Escherichia coli
subcloning of the entire vir regulon
the sensing GAF domain of DosT is expressed in Escherichia coli BL21gold DE3 cells
wild-type and mutants introduced into deltarodK strain SA1708, His6-tagged wild-type and mutants expressed in Escherichia coli
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cytoplasmic expression of TorSS as a fusion protein, containing a hexahistidine tag on the N-terminus separated by a separated by a thrombin protease recognition sequence, in Escherichia coli BL21(DE3) cells
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cytoplasmic expression of TorSS as a fusion protein, containing a hexahistidine tag on the N-terminus separated by a separated by a thrombin protease recognition sequence, in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
LOV-HK expressed in Escherichia coli
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LOV-HK expressed in Escherichia coli
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