D
IPR000498

Outer membrane protein OmpA-like, transmembrane domain

InterPro entry
Short nameOmpA-like_TM_dom
Overlapping
homologous
superfamilies
 

Description

The ompA-like transmembrane domain is present in a number of different outer membrane proteins of several Gram-negative bacteria. Many of the proteins having this domain in the N-terminal also have the conserved bacterial outer membrane protein domain
IPR006664
at the C terminus. The outer membrane protein A of Escherichia coli (OmpA), is one of the most studied proteins in this group
[1]
. It has a multifunctional role. OmpA is required for the action of colicins K and L and for the stabilisation of mating aggregates in conjugation. It also serves as a receptor for a number of T-even like phages and can act as a porin with low permeability that allows slow penetration of small solutes
[2]
.

OmpA consists of a regular, extended eight-stranded β-barrel and appears to be constructed like an inverse micelle with large water-filled cavities, but does not form a pore. The cavities seem to be highly conserved during evolution. The structure corroborates the concept that all outer membrane proteins consist of β-barrels
[3]
. The β-barrel membrane anchor appears to be the outer membrane equivalent of the single-chain α-helix anchor of the inner membrane.

References

1.Expression and secretion of proteins in E. coli. Pines O, Inouye M. Mol. Biotechnol. 12, 25-34, (1999). View articlePMID: 10554771

2.The role of the mature part of secretory proteins in translocation across the plasma membrane and in regulation of their synthesis in Escherichia coli. MacIntyre S, Henning U. Biochimie 72, 157-67, (1990). View articlePMID: 1974149

3.Structure of the outer membrane protein A transmembrane domain. Pautsch A, Schulz GE. Nat. Struct. Biol. 5, 1013-7, (1998). View articlePMID: 9808047

GO terms

biological process

  • None

molecular function

  • None
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