Outer membrane phospholipase A (OMPLA) superfamily

SCOP classification

• Root: SCOP hierarchy in SUPERFAMILY [ 0] (11)
• Class: Membrane and cell surface proteins and peptides [ 56835] (58)
• Fold: Transmembrane beta-barrels [ 56924] (6)
• Superfamily: Outer membrane phospholipase A (OMPLA) [ 56931]
• Families: Outer membrane phospholipase A (OMPLA) [ 56932]

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Superfamily statistics

	Genomes (559)	Uniprot 2018_03 genome	PDB chains (SCOP 1.75)
Domains	573	4,675	3
Proteins	573	4,669	3

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Functional annotation

• General category: Metabolism
• Detailed category: Lipid metabolism and transport

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Enzyme Commission (EC)

Highlighted in gray are those with FDR_all>0.001

	EC term	FDR (all)	IC level	SDEO level	Annotation (direct or inherited)
Enzyme Commission (EC)	Phospholipase A(1)	0	2.259	--	DIRECT
Enzyme Commission (EC)	Hydrolases	0	0.04271	--	DIRECT
Enzyme Commission (EC)	Acting on ester bonds	0	0.4665	Least Informative	DIRECT
Enzyme Commission (EC)	Carboxylic ester hydrolases	0	1.217	Moderately Informative	DIRECT
Enzyme Commission (EC)	Phospholipase A(2)	0	2.083	Highly Informative	DIRECT

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Enzyme Commission (EC)

Highlighted in gray are those with FDR_all>0.001

	EC term	FDR (all)	IC level	SDEC level	Annotation (direct or inherited)
Enzyme Commission (EC)	Phospholipase A(2)	0	2.253	--	DIRECT
Enzyme Commission (EC)	Phospholipase A(1)	0	2.651	--	DIRECT
Enzyme Commission (EC)	Acting on ester bonds	0	0.7559	--	DIRECT
Enzyme Commission (EC)	Hydrolases	0	0.3541	Least Informative	DIRECT
Enzyme Commission (EC)	Carboxylic ester hydrolases	0	1.408	Informative	DIRECT

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InterPro annotation

• Cross references: IPR003187 SSF56931 Protein matches
• Abstract:

  Outer membrane phospholipase A (OMPLA) is an integral membrane phospholipase, which is present in many Gram-negative bacteria and has a broad substrate specificity . The role of OMPLA has been most thoroughly studied in Escherichia coli, where it participates in the secretion of bacteriocins. Bacteriocin release is triggered by a lysis protein (bacteriocin release protein or BRP), followed by a phospholipase dependent accumulation of lysophospholipids and free fatty acids in the outer membrane [12615538]. The reaction products enhance the permeability of the outer membrane, which allows the semispecific secretion of bacteriocins. One speculative function of OMPLA is related to organic solvent tolerance in bacteria.

  Structurally, it consists of a 12-stranded antiparallel beta-barrel with a convex and a flat side. The active site residues are exposed on the exterior of the flat face of the beta-barrel. The activity of the enzyme is regulated by reversible dimerisation. Dimer interactions occur exclusively in the membrane-embedded parts of the flat side of the beta-barrel, with polar residues embedded in an apolar environment forming the key interactions. The active site His and Ser residues are located at the exterior of the beta-barrel, at the outer leaflet side of the membrane. This location indicates that under normal conditions the substrate and the active site are physically separated, since in E. coli phospholipids are exclusively located in the inner leaflet of the outer membrane.

InterPro database

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