OmpA_membrane

• PFAM accession number: PF01389
• Interpro abstract (IPR000498):

  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 [ (PUBMED:10554771) ]. 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 [ (PUBMED:1974149) ].

  OmpA consists of a regular, extended eight-stranded beta-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 beta-barrels [ (PUBMED:9808047) ]. The beta-barrel membrane anchor appears to be the outer membrane equivalent of the single-chain alpha-helix anchor of the inner membrane.

• GO component: cell outer membrane (GO:0009279), integral component of membrane (GO:0016021)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry OmpA_membrane