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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]


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


Functional annotation
General category Metabolism
Detailed category Lipid metabolism and transport

Document:
Function annotation of SCOP domain superfamilies

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEO levelAnnotation (direct or inherited)
Enzyme Commission (EC)Acting on ester bonds0Least InformativeDirect
Enzyme Commission (EC)Carboxylic ester hydrolases0Moderately InformativeDirect
Enzyme Commission (EC)Phospholipase A(2)0Highly InformativeDirect

Document: EC annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEC levelAnnotation (direct or inherited)
Enzyme Commission (EC)Hydrolases0Least InformativeDirect
Enzyme Commission (EC)Carboxylic ester hydrolases0InformativeDirect

Document: EC annotation of SCOP domains

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 [PubMed12615538]. 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


PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

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Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.


Alignments of sequences to 1 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.


Browse and view proteins in genomes which have different domain combinations including a Outer membrane phospholipase A (OMPLA) domain.


Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.


Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 1 hidden Markov models representing the Outer membrane phospholipase A (OMPLA) superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.


Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Enzyme Commission (EC) · Internal database links ]