LMPD Database

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LMP007646

UniProt Annotations

Entry Information
Gene Nameouter membrane phospholipase A
Protein EntryPA1_ECOLI
UniProt IDP0A921
SpeciesE. coli
Comments
Comment typeDescription
Catalytic ActivityPhosphatidylcholine + H(2)O = 1- acylglycerophosphocholine + a carboxylate.
Catalytic ActivityPhosphatidylcholine + H(2)O = 2- acylglycerophosphocholine + a carboxylate.
CofactorName=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10537112}; Note=Binds 1 Ca(2+) ion per monomer. In the dimeric form the Ca(2+) is bound by different amino acids with binding of each Ca(2+) shared with ligands coming from each monomer (Arg-167 and Ser-172 from 1 monomer, Ser-126 of the other). The Ca(2+) ion may have a role in catalysis. {ECO:0000269|PubMed:10537112};
Enzyme RegulationBy membrane damage, for example, by phage- induced lysis or temperature shock. The protein is inactive in the monomeric form and active in the dimeric form; calcium is essential for dimer stability. {ECO:0000269|PubMed:10322034, ECO:0000269|PubMed:9013551}.
FunctionHas broad substrate specificity including hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. Strong expression leads to outer membrane breakdown and cell death; is dormant in normal growing cells. Required for efficient secretion of bacteriocins.
InteractionP37641:yhjC; NbExp=1; IntAct=EBI-1119179, EBI-849303;
SimilarityBelongs to the phospholipase A1 family. {ECO:0000305}.
Subcellular LocationCell outer membrane {ECO:0000269|PubMed:6397463}; Multi-pass membrane protein {ECO:0000269|PubMed:6397463}. Note=One of the very few enzymes located there.
SubunitHomodimer; dimerization is reversible, and the dimeric form is the active one. {ECO:0000269|PubMed:10322034, ECO:0000269|PubMed:10537112, ECO:0000269|PubMed:9013551}.