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Literature summary extracted from

  • Herrera, C.M.; Hankins, J.V.; Trent, M.S.
    Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides (2010), Mol. Microbiol., 76, 1444-1460.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.8.43 PmrA te enzyme EptA is activated in a PmrA-dependent manner, overview Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.8.43 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
2.7.8.43 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

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.2.43 plasma membrane
-
 Escherichia coli 5886
-
2.7.8.43 periplasm
-
 Salmonella enterica
-
-
2.7.8.43 periplasm
-
 Escherichia coli
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.8.43 Fe3+ required, the peptA (eptA promoter) is induced sevenfold in the presence of Fe3+ Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.43 Escherichia coli P76473
-
-
2.7.8.43 Escherichia coli P30845 W3110, gene eptA or pmrC
-
2.7.8.43 Salmonella enterica P36555 serovar typhimurium, gene eptA or pmrC
-
2.7.8.43 Salmonella enterica LT2 P36555 serovar typhimurium, gene eptA or pmrC
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.8.43 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 Salmonella enterica ?
-
 ?
2.7.8.43 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 Escherichia coli ?
-
 ?
2.7.8.43 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 Salmonella enterica LT2 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.2.43 arnT
-
 Escherichia coli
2.7.8.43 EptA
-
 Salmonella enterica
2.7.8.43 EptA
-
 Escherichia coli
2.7.8.43 PmrC
-
 Salmonella enterica
2.7.8.43 PmrC
-
 Escherichia coli

Expression

EC Number Organism Comment Expression
2.7.8.43 Salmonella enterica expression of EptA (PmrC) is under the control of PmrA/PmrB additional information
2.7.8.43 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

EC Number General Information Comment Organism
2.4.2.43 malfunction LpxT-dependent lipid A modification is not restored in arnT or eptA mutants Escherichia coli
2.4.2.43 physiological function PmrA controls synthesis of both ArnT and EptA Escherichia coli
2.7.8.43 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
2.7.8.43 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
2.7.8.43 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
2.7.8.43 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
2.7.8.43 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