2.7.1.189: autoinducer-2 kinase
This is an abbreviated version!
For detailed information about autoinducer-2 kinase, go to the full flat file.
Word Map on EC 2.7.1.189
-
2.7.1.189
-
quorum
-
cell-cell
-
interspecies
-
repressor
-
chemotaxis
-
amp
-
prevailing
-
typhimurium
-
envision
-
quorum-sensing
-
fight
-
drug development
- 2.7.1.189
-
quorum
-
cell-cell
-
interspecies
- repressor
-
chemotaxis
- amp
-
prevailing
- typhimurium
-
envision
-
quorum-sensing
-
fight
- drug development
Reaction
Synonyms
AI-2 kinase, AI-2 processing kinase, Lsr kinase, lsrK, LsrK kinase
ECTree
Advanced search results
General Information
General Information on EC 2.7.1.189 - autoinducer-2 kinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
malfunction
metabolism
physiological function
additional information
-
deletion of lsrR and lsrK does not affect growth or motility. Genomic deletion of gene lsrK. Genes lsrK and lsrR knockouts behave identically concerning the quantity and architecture of biofilms by affecting genes including flu and wza, small riboregulators respond to the QS regulators lsrR and lsrK
malfunction
-
in the DELTAlsrK deletion mutant, expression of the lsr-lacZ fusion is not induced by the presence of luxS or by exogenously supplied AI-2 in contrast to the wild-type. The enzyme activity and ATPase activity in the presence of culture fluids prepared from a luxS null strain is consistently lower than the background level
malfunction
-
no induction of the lsr promoter occurs in the lsrK mutant strain, since the lsr promoter is activated by phosphorylated autoinducer-2. Intracellular accumulation of phosphorylated autoinducer-2 is not observed in a lsrK mutant
malfunction
-
unlike the wild-type, the lsrK mutant does not activate transcription of the lsr operon in response to AI-2. The lsrK mutant fails to activate lsr expression because it cannot produce phospho-AI-2, which is the lsr operon inducer. Specifically, in an lsrK mutant, any AI-2 internalized by a secondary transporter does not get phosphorylated, and cannot be sequestered. In an lsrR/lsrK double mutant extracellular AI-2 accumulates to wild-type levels
malfunction
inhibition of LsrK impairs the quorum-sensing cascade and consequently reduces bacterial pathogenicity
malfunction
inhibition of LsrK leads to quorum sensing inactivation and interfere with the pathogenesis
malfunction
-
inhibition of LsrK leads to quorum sensing inactivation and interfere with the pathogenesis
-
malfunction
-
inhibition of LsrK impairs the quorum-sensing cascade and consequently reduces bacterial pathogenicity
-
malfunction
-
inhibition of LsrK leads to quorum sensing inactivation and interfere with the pathogenesis
-
malfunction
-
inhibition of LsrK impairs the quorum-sensing cascade and consequently reduces bacterial pathogenicity
-
malfunction
-
in the DELTAlsrK deletion mutant, expression of the lsr-lacZ fusion is not induced by the presence of luxS or by exogenously supplied AI-2 in contrast to the wild-type. The enzyme activity and ATPase activity in the presence of culture fluids prepared from a luxS null strain is consistently lower than the background level
-
-
autoinducer 2, AI-2, is imported by the Lsr and is phosphorylated by the LsrK kinase, and AI-2-phosphate is the inducer of the lsr operon. LsrK is necessary for the phosphorylation of AI-2, AI-2 is not phosphorylated by phosphoenolpyruvate phosphotransferase system, which is involved in the AI-2 internalization. Lsr-mediated transport and processing of AI-2 in Escherichia coli, overview
metabolism
-
Lsr-mediated transport and processing of autoinducer 2, AI-2, overview
metabolism
-
model-based design, construction, and characterization of controller cells to modulate the external AI-2 environment, the cells are designed via the compartmentalization of different aspects of AI-2 processing: uptake (lsrACDB), phosphorylation (lsrK), and degradation (lsrFG), mathematical model overview
metabolism
-
the enzyme is involved in quorum sensing, one type of bacterial cell-to-cell communication, which co-ordinates bacterial behaviors within a population. The communication is mediated by a plethora of diffusible signaling molecules, called autoinducers. AI-2 signaling is carried out by the Lsr proteins
metabolism
-
the enzyme is involved in quorum sensing, overview
metabolism
-
the regulatory network for the uptake of Escherichia coli autoinducer 2 (AI-2) is comprised of a transporter complex, LsrABCD, its repressor, LsrR, and the cognate signal kinase, LsrK. This network is an integral part of the AI-2 quorum-sensing system, extended model for AI-2 signaling, overview
metabolism
linkages between quorum sensing (QS) activity and sugar metabolism, model for LsrK/HPr interplay between QS and PTS, overview
metabolism
molecular communication among bacteria occurs via quorum sensing (QS). Modulating molecular communication among bacteria can alter phenotype, including attachment to epithelia, biofilm formation, and even toxin production. Intercepting and modulating communication networks provide a means to attenuate virulence without directly interacting with the bacteria of interest
metabolism
-
the enzyme is involved in quorum sensing, overview
-
metabolism
Escherichia coli W3110 / ATCC 27325
-
the enzyme is involved in quorum sensing, overview
-
metabolism
-
the enzyme is involved in quorum sensing, overview
-
metabolism
-
Lsr-mediated transport and processing of autoinducer 2, AI-2, overview
-
-
autoinducer-2, AI-2, is activated by the bacterial kinase LsrK and modulate AI-2 specific gene transcription through the transcriptional regulator LsrR. Activities of phosphorylated autoinducer 2 analogues in quorum sensing reduction, overview. In vivo, the critical step that makes AI-2 functional in derepressing the lsr operon is phosphorylation by the kinase LsrK. Active autinducer 2 and its analogues quench the quorum sensing response in multiple bacterial species simultaneously, overview
physiological function
-
autoinducer-2, AI-2, is activated by the bacterial kinase LsrK and modulate AI-2 specific gene transcription through the transcriptional regulator LsrR. Activities of phosphorylated autoinducer 2 analogues in quorum sensing reduction, overview. In vivo, the critical step that makes AI-2 functional in derepressing the lsr operon is phosphorylation by the kinase LsrK. Active autinducer 2 and its analogues quench the quorum sensing response in multiple bacterial species simultaneously, overview
physiological function
-
autoinducer-2, AI-2, is activated by the bacterial kinase LsrK and modulate AI-2 specific gene transcription through the transcriptional regulator LsrR. Activities of phosphorylated autoinducer 2 analogues in quorum sensing reduction, overview. In vivo, the critical step that makes AI-2 functional in derepressing the lsr operon is phosphorylation by the kinase LsrK. Active autinducer 2 and its analogues quench the quorum sensing response in multiple bacterial species simultaneously, overview
physiological function
-
enteric bacteria respond to the presence of competitor bacteria by sequestering and destroying autoinducer-2, through phosphorylation by the enzyme LsrK and cleavage of 4-hydroxy-2,3-pentanedione 5-phosphate producing 2-phosphoglycolic acid via enzyme LsrG, thereby eliminating the competitors' intercellular communication capabilities. The phosphorylated form of AI-2 is the intracellular signal responsible for lsr activation
physiological function
-
enzyme LsrK activity, namely, AI-2 phosphorylation, is required to sequester the signal in the cytoplasm, independently of the mechanism of AI-2 internalization
physiological function
-
genes lsrK and crp are required for optimal biofilm formation by Aggregatibacter actinomycetemcomitans. Another kinase is capable of phosphorylating AI-2 in Aggregatibacter actinomycetemcomitans in the absence of LsrK or enzyme LsrK is not essential for regulating the lsrACDBFG and lsrRK operons in AAggregatibacter actinomycetemcomitans
physiological function
-
in enteric bacteria, the kinase LsrK catalyzes the phosphorylation of the C5-hydroxyl group in the linear form of 4,5-dihydroxypentane-2,3-dione, the precursor of the type II bacterial quorum sensing molecule (AI-2), the enzyme is required for phosphorylation is required for autoinducer-2 sequestration in the cytoplasm and subsequent derepression of AI-2 related genes necessary for quorum development and autoinducer-2 quorum sensing activation, catalytic mechanism, overview. Phosphorylated AI-2 (phospho-DPD) binds and inactivates the transcriptional repressor protein LsrR thereby inducing the expression of the lsr operon and potentially other LsrR-regulated, QS-related genes
physiological function
-
LsrK is required for the regulation of the lsr operon and the AI-2 uptake process. LsrK is a kinase that phosphorylates AI-2 upon entry into the cell, phosphorylation of AI-2 results in its sequestration in the cytoplasm
physiological function
-
repressor LsrR and kinase LsrK directly regulate autoinducer 2, AI-2, uptake. Small riboregulators respond to the QS regulators lsrR and lsrK. 117 and 32 genes are induced and repressed, respectively, by lsrK
physiological function
-
the enzyme is repsonsible for the regulation of uptake and processing of the quorum-sensing autoinducer AI-2 in Escherichia coli, overview. Enzyme LsrK and the Lsr transporter are required for AI-2 internalization and processing in Escherichia coli
physiological function
-
the enzyme is responsible for the phosphorylation of autoinducer 2, and thereby attenuating cell-cell communication among bacterial populations. The bacterial signal molecule autoinducer-2 is secreted as a quorum sensing signal. The enzyme LsrK increases the net uptake rate by limiting secretion of AI-2 back into the extracellular environment. LsrK-mediated phosphorylation of AI-2 blocks export back to the extracellular milieu so that accumulated AI-2P binds the regulatory protein LsrR
physiological function
-
when enzyme-treated autoinducer-2 is added ex vivo to Escherichia coli populations, the native quorum sensing response is significantly reduced, overview. The addition of enzyme LsrK and ATP to growing co-cultures of Escherichia coli and Salmonella typhimurium exhibits significantly reduced native cross-talk that ordinarily exists among and between species in an ecosystem
physiological function
communication mediated by the quorum sensing (QS) requires bacterial autoinducer-2, AI-2 ((S)-4,5-dihydroxypentane-2,3-dione). AI-2 mediated QS activity is diminished by phosphorylation via the AI-2 processing kinase, LsrK
physiological function
LsrK is a kinase playing a key role in the processing of autoinducer-2 (AI-2), a quorum-sensing mediator in gut enteric bacteria
physiological function
LsrK is a kinase responsible for the phosphorylation of autoinducer-2, a signaling molecule involved in quorum sensing, the method of bacterial communication
physiological function
quorum sensing (QS), a bacterial process that regulates population-scale behavior, is mediated by small signaling molecules, called autoinducers (AIs), that are secreted and perceived, modulating a collective phenotype. Because the autoinducer AI-2 is secreted by a wide variety of bacterial species, its perception cues bacterial behavior. This response is mediated by the lsr (LuxS-regulated) operon that includes the AI-2 transporter LsrACDB and the kinase LsrK. The AI-2-mediated QS system is partially regulated by substrate availability and cell metabolism. LuxS synthesizes AI-2 as a by-product of the activated methyl cycle, after which AI-2 accumulates extracellularly. AI-2 is imported by LsrACDB and phosphorylated by the kinase LsrK, sequestering it within the cell. LsrK is tightly bound to the PTS protein HPr, and HPr directly influences LsrK activity
physiological function
-
autoinducer-2, AI-2, is activated by the bacterial kinase LsrK and modulate AI-2 specific gene transcription through the transcriptional regulator LsrR. Activities of phosphorylated autoinducer 2 analogues in quorum sensing reduction, overview. In vivo, the critical step that makes AI-2 functional in derepressing the lsr operon is phosphorylation by the kinase LsrK. Active autinducer 2 and its analogues quench the quorum sensing response in multiple bacterial species simultaneously, overview
-
physiological function
-
LsrK is a kinase responsible for the phosphorylation of autoinducer-2, a signaling molecule involved in quorum sensing, the method of bacterial communication
-
physiological function
-
LsrK is a kinase playing a key role in the processing of autoinducer-2 (AI-2), a quorum-sensing mediator in gut enteric bacteria
-
physiological function
-
LsrK is a kinase responsible for the phosphorylation of autoinducer-2, a signaling molecule involved in quorum sensing, the method of bacterial communication
-
physiological function
-
LsrK is a kinase playing a key role in the processing of autoinducer-2 (AI-2), a quorum-sensing mediator in gut enteric bacteria
-
physiological function
Escherichia coli W3110 / ATCC 27325
-
autoinducer-2, AI-2, is activated by the bacterial kinase LsrK and modulate AI-2 specific gene transcription through the transcriptional regulator LsrR. Activities of phosphorylated autoinducer 2 analogues in quorum sensing reduction, overview. In vivo, the critical step that makes AI-2 functional in derepressing the lsr operon is phosphorylation by the kinase LsrK. Active autinducer 2 and its analogues quench the quorum sensing response in multiple bacterial species simultaneously, overview
-
physiological function
-
enteric bacteria respond to the presence of competitor bacteria by sequestering and destroying autoinducer-2, through phosphorylation by the enzyme LsrK and cleavage of 4-hydroxy-2,3-pentanedione 5-phosphate producing 2-phosphoglycolic acid via enzyme LsrG, thereby eliminating the competitors' intercellular communication capabilities. The phosphorylated form of AI-2 is the intracellular signal responsible for lsr activation
-
physiological function
-
autoinducer-2, AI-2, is activated by the bacterial kinase LsrK and modulate AI-2 specific gene transcription through the transcriptional regulator LsrR. Activities of phosphorylated autoinducer 2 analogues in quorum sensing reduction, overview. In vivo, the critical step that makes AI-2 functional in derepressing the lsr operon is phosphorylation by the kinase LsrK. Active autinducer 2 and its analogues quench the quorum sensing response in multiple bacterial species simultaneously, overview
-
physiological function
-
LsrK is required for the regulation of the lsr operon and the AI-2 uptake process. LsrK is a kinase that phosphorylates AI-2 upon entry into the cell, phosphorylation of AI-2 results in its sequestration in the cytoplasm
-
physiological function
-
autoinducer-2, AI-2, is activated by the bacterial kinase LsrK and modulate AI-2 specific gene transcription through the transcriptional regulator LsrR. Activities of phosphorylated autoinducer 2 analogues in quorum sensing reduction, overview. In vivo, the critical step that makes AI-2 functional in derepressing the lsr operon is phosphorylation by the kinase LsrK. Active autinducer 2 and its analogues quench the quorum sensing response in multiple bacterial species simultaneously, overview
-
-
analysis of structure-activity relationship, overview
additional information
-
LsrK-mediated degradation of autoinducer-2 attenuates the quorum sensing response among Salmonella typhimurium and Vibrio harveyi even though the autoinducer-2 signal transduction mechanisms and the phenotypic responses are species-specific
additional information
three-dimensional homology structure modeling of LsrK, overview. LsrK kinase has two domains: N-terminal domain of residues 13-260 (domain I) and C-terminal domain of residues 271-468 (domain II). These two domains form a prominent cleft at their interface including both the ATP and the substrate binding sites. This putative binding site constituted both the ATP binding site and the substrate binding site. The substrate binding site is located deep in the cleft, whereas the ATP binding site is located near the entrance of the pocket. (S)-4,5-Dihydroxypentane-2,3-dione (DPD) docking results show that the C5 position of DPD, where the phosphorylation occurs, orients toward ATP by forming interactions with Thr21
additional information
-
three-dimensional homology structure modeling of LsrK, overview. LsrK kinase has two domains: N-terminal domain of residues 13-260 (domain I) and C-terminal domain of residues 271-468 (domain II). These two domains form a prominent cleft at their interface including both the ATP and the substrate binding sites. This putative binding site constituted both the ATP binding site and the substrate binding site. The substrate binding site is located deep in the cleft, whereas the ATP binding site is located near the entrance of the pocket. (S)-4,5-Dihydroxypentane-2,3-dione (DPD) docking results show that the C5 position of DPD, where the phosphorylation occurs, orients toward ATP by forming interactions with Thr21
-
additional information
-
three-dimensional homology structure modeling of LsrK, overview. LsrK kinase has two domains: N-terminal domain of residues 13-260 (domain I) and C-terminal domain of residues 271-468 (domain II). These two domains form a prominent cleft at their interface including both the ATP and the substrate binding sites. This putative binding site constituted both the ATP binding site and the substrate binding site. The substrate binding site is located deep in the cleft, whereas the ATP binding site is located near the entrance of the pocket. (S)-4,5-Dihydroxypentane-2,3-dione (DPD) docking results show that the C5 position of DPD, where the phosphorylation occurs, orients toward ATP by forming interactions with Thr21
-