BRENDA - Enzyme Database show
show all sequences of 2.7.8.43

Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides

Herrera, C.M.; Hankins, J.V.; Trent, M.S.; Mol. Microbiol. 76, 1444-1460 (2010)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
PmrA
te enzyme EptA is activated in a PmrA-dependent manner, overview
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
LpxT
role for LpxT in the reduction of enzyme EptA activity, the transcriptional regulation of lpxT gene is PmrA-independent. PmrA-dependent inhibition of LpxT is required for phosphoethanolamine decoration of lipid A
Escherichia coli
LpxT
role for LpxT in the reduction of enzyme EptA activity. Loss of Salmonella lpxT greatly increases modification of lipid A through enzyme EptA. LpxT catalyses the phosphorylation of lipid A at the 1-position
Salmonella enterica
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
periplasm
-
Escherichia coli
-
-
periplasm
-
Salmonella enterica
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe3+
required, the peptA (eptA promoter) is induced sevenfold in the presence of Fe3+
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P30845
W3110, gene eptA or pmrC
-
Salmonella enterica
P36555
serovar typhimurium, gene eptA or pmrC
-
Salmonella enterica LT2
P36555
serovar typhimurium, gene eptA or pmrC
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
enzyme EptA catalyses the periplasmic addition of the positively charged substituent phosphoethanolamine to lipid A controlled by the PmrA transcriptional regulator and conferring resistance to cationic antimicrobial peptides, including polymyxin
723212
Salmonella enterica
?
-
-
-
-
additional information
enzyme EptA or PmrC catalyses the periplasmic addition of the positively charged substituent phosphoethanolamine to lipid A controlled by the PmrA transcriptional regulator and conferring resistance to cationic antimicrobial peptides, including polymyxin
723212
Escherichia coli
?
-
-
-
-
additional information
enzyme EptA catalyses the periplasmic addition of the positively charged substituent phosphoethanolamine to lipid A controlled by the PmrA transcriptional regulator and conferring resistance to cationic antimicrobial peptides, including polymyxin
723212
Salmonella enterica LT2
?
-
-
-
-
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
PmrA
te enzyme EptA is activated in a PmrA-dependent manner, overview
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
LpxT
role for LpxT in the reduction of enzyme EptA activity, the transcriptional regulation of lpxT gene is PmrA-independent. PmrA-dependent inhibition of LpxT is required for phosphoethanolamine decoration of lipid A
Escherichia coli
LpxT
role for LpxT in the reduction of enzyme EptA activity. Loss of Salmonella lpxT greatly increases modification of lipid A through enzyme EptA. LpxT catalyses the phosphorylation of lipid A at the 1-position
Salmonella enterica
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
periplasm
-
Escherichia coli
-
-
periplasm
-
Salmonella enterica
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe3+
required, the peptA (eptA promoter) is induced sevenfold in the presence of Fe3+
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
enzyme EptA catalyses the periplasmic addition of the positively charged substituent phosphoethanolamine to lipid A controlled by the PmrA transcriptional regulator and conferring resistance to cationic antimicrobial peptides, including polymyxin
723212
Salmonella enterica
?
-
-
-
-
additional information
enzyme EptA or PmrC catalyses the periplasmic addition of the positively charged substituent phosphoethanolamine to lipid A controlled by the PmrA transcriptional regulator and conferring resistance to cationic antimicrobial peptides, including polymyxin
723212
Escherichia coli
?
-
-
-
-
additional information
enzyme EptA catalyses the periplasmic addition of the positively charged substituent phosphoethanolamine to lipid A controlled by the PmrA transcriptional regulator and conferring resistance to cationic antimicrobial peptides, including polymyxin
723212
Salmonella enterica LT2
?
-
-
-
-
Expression
Organism
Commentary
Expression
Salmonella enterica
expression of EptA (PmrC) is under the control of PmrA/PmrB
additional information
Escherichia coli
the peptA (eptA promoter) is induced sevenfold in the presence of Fe3+, induction is lost in enzyme mutant strain CH020 (DELTApmrA)
up
General Information
General Information
Commentary
Organism
malfunction
eptA mutants show a 20fold decrease in polymyxin B resistanc. Overexpression of LpxT in trans in Escherichia coli strain WD101 results in loss of phosphoethanolamine modification and compromised WD101 polymyxin resistance
Escherichia coli
malfunction
although Salmonella lipid A is more prevalently modified with L-4-aminoarabinose, loss of Salmonella lpxT greatly increases modification of lipid A through enzyme EptA, and LpxT-dependent lipid A modification is not restored in the DELTAeptA mutant. LpxT catalyses the phosphorylation of lipid A at the 1-position forming 1-diphosphate lipid A increasing the negative charge of the bacterial surface
Salmonella enterica
metabolism
PmrA is activated under Mg2+ limiting growth conditions or upon exposure to cationic antimicrobial peptides. Under these conditions PmrA activation is mediated by a second two-component system, PhoP/PhoQ. activation of PhoP in Salmonella induces the synthesis of PmrD, which regulates PmrA activity post-transcriptionally by preventing dephosphorylation of PmrA
Salmonella enterica
physiological function
EptA-dependent lipid A modification is required for resistance to polymyxin B, EptA plays a dominant role in polymyxin resistance. Enzyme PmrA is not involved in transcription of LpxT, which catalyses the phosphorylation of lipid A at the 1-position forming 1-diphosphate lipid A increasing the negative charge of the bacterial surface. LpxT-dependent lipid A modification is regulated post-translationally. The regulation does not occur at the level of transcription, but rather following the assembly of LpxT into the inner membrane. PmrA-dependent inhibition of LpxT is required for phosphoethanolamine decoration of lipid A, which is critical for Escherichia coli to resist the bactericidal activity of polymyxin
Escherichia coli
physiological function
EptA-dependent lipid A modification is required for resistance to polymyxin B. Expression of EptA (PmrC) is under the control of PmrA/PmrB
Salmonella enterica
General Information (protein specific)
General Information
Commentary
Organism
malfunction
eptA mutants show a 20fold decrease in polymyxin B resistanc. Overexpression of LpxT in trans in Escherichia coli strain WD101 results in loss of phosphoethanolamine modification and compromised WD101 polymyxin resistance
Escherichia coli
malfunction
although Salmonella lipid A is more prevalently modified with L-4-aminoarabinose, loss of Salmonella lpxT greatly increases modification of lipid A through enzyme EptA, and LpxT-dependent lipid A modification is not restored in the DELTAeptA mutant. LpxT catalyses the phosphorylation of lipid A at the 1-position forming 1-diphosphate lipid A increasing the negative charge of the bacterial surface
Salmonella enterica
metabolism
PmrA is activated under Mg2+ limiting growth conditions or upon exposure to cationic antimicrobial peptides. Under these conditions PmrA activation is mediated by a second two-component system, PhoP/PhoQ. activation of PhoP in Salmonella induces the synthesis of PmrD, which regulates PmrA activity post-transcriptionally by preventing dephosphorylation of PmrA
Salmonella enterica
physiological function
EptA-dependent lipid A modification is required for resistance to polymyxin B, EptA plays a dominant role in polymyxin resistance. Enzyme PmrA is not involved in transcription of LpxT, which catalyses the phosphorylation of lipid A at the 1-position forming 1-diphosphate lipid A increasing the negative charge of the bacterial surface. LpxT-dependent lipid A modification is regulated post-translationally. The regulation does not occur at the level of transcription, but rather following the assembly of LpxT into the inner membrane. PmrA-dependent inhibition of LpxT is required for phosphoethanolamine decoration of lipid A, which is critical for Escherichia coli to resist the bactericidal activity of polymyxin
Escherichia coli
physiological function
EptA-dependent lipid A modification is required for resistance to polymyxin B. Expression of EptA (PmrC) is under the control of PmrA/PmrB
Salmonella enterica
Expression (protein specific)
Organism
Commentary
Expression
Salmonella enterica
expression of EptA (PmrC) is under the control of PmrA/PmrB
additional information
Escherichia coli
the peptA (eptA promoter) is induced sevenfold in the presence of Fe3+, induction is lost in enzyme mutant strain CH020 (DELTApmrA)
up
Other publictions for EC 2.7.8.43
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
738476
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7
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2
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739106
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Infect. Immun.
82
2170-2179
2014
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1
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2
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10
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2
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739495
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739786
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Acta Crystallogr. Sect. D
70
2730-2739
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1
1
6
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3
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2
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12
2
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3
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733965
Lewis
Phosphoethanolamine residues o ...
Neisseria gonorrhoeae
Infect. Immun.
81
33-42
2013
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2
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733966
Cullen
EptC of Campylobacter jejuni m ...
Campylobacter jejuni, Campylobacter jejuni 81-176
Infect. Immun.
81
430-4440
2013
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1
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3
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2
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734476
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425
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2013
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1
1
1
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740134
Bontemps-Gallo
Biosynthesis of osmoregulated ...
Escherichia coli
BioMed Res. Int.
2013
371429
2013
1
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1
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740516
Knirel
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Shigella flexneri
Glycobiology
23
475-485
2013
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733017
Anandan
Cloning, expression, purificat ...
Neisseria meningitidis, Neisseria meningitidis NMB
Acta Crystallogr. Sect. F
68
1494-1497
2012
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734190
Cullen
Trent, M.S.: Characterization ...
Campylobacter jejuni, Campylobacter jejuni 81-176
J. Biol. Chem.
287
326-3336
2012
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734198
Farizano
The PmrAB system-inducing cond ...
Salmonella enterica 14028s, Salmonella enterica
J. Biol. Chem.
287
38778-38789
2012
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3
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733107
Beceiro
Phosphoethanolamine modificati ...
Acinetobacter baumannii
Antimicrob. Agents Chemother.
55
3370-3379
2011
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3
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723212
Herrera
Activation of PmrA inhibits Lp ...
Escherichia coli, Salmonella enterica, Salmonella enterica LT2
Mol. Microbiol.
76
1444-1460
2010
1
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735157
Cullen
A link between the assembly of ...
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Proc. Natl. Acad. Sci. USA
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2010
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2
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733963
Lewis
Phosphoethanolamine substituti ...
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA19
Infect. Immun.
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2009
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6
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1
1
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733962
Takahashi
Modification of lipooligosacch ...
Neisseria meningitidis
Infect. Immun.
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2008
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1
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2
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734067
Tamayo
Identification of cptA, a PmrA ...
Salmonella enterica, Salmonella enterica LT2
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3391-3399
2005
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4
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4
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734151
Tran
Resistance to the antimicrobia ...
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium C5
J. Biol. Chem.
280
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2005
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5
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734064
Lee
The PmrA-regulated pmrC gene m ...
Salmonella enterica
J. Bacteriol.
186
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2004
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3
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734148
Tran
Periplasmic cleavage and modif ...
Helicobacter pylori
J. Biol. Chem.
279
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2004
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2
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734062
Cox
Phosphorylation of the lipid A ...
Neisseria meningitidis
J. Bacteriol.
185
3270-3277
2003
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2
2
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734138
Zhou
Lipid A modifications in polym ...
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium ATCC 14028
J. Biol. Chem.
276
43111-43121
2001
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1
1
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734706
Gunn
PmrA-PmrB-regulated genes nece ...
Salmonella enterica 14028s, Salmonella enterica
Mol. Microbiol.
27
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1998
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