Domain

OmpA-like domain (IPR006665)

Short name: OmpA-like

Domain relationships

Description

This entry represents domain with a beta/alpha/beta/alpha-beta(2) structure found in the C-terminal region of many Gram-negative bacterial outer membrane proteins [PMID: 1538702], such as porin-like integral membrane proteins (such as ompA) [PMID: 2202726], small lipid-anchored proteins (such as pal) [PMID: 10515919], and MotB proton channels [PMID: 17052729]. The N-terminal half is variable although some of the proteins in this group have the OmpA-like transmembrane domain IPR000498 at the N terminus. OmpA from Escherichia coli is required for pathogenesis, and can interact with host receptor molecules [PMID: 17368067]. MotB (and MotA) serves two functions in E. coli, the MotA(4)-MotB(2) complex attaches to the cell wall via MotB to form the stator of the flagellar motor, and the MotA-MotB complex couples the flow of ions across the cell membrane to movement of the rotor [PMID: 17052729].

Other Gram-negative outer membrane proteins with this domain:

  • Outer membrane protein P5 from Haemophilus influenzae.
  • Outer membrane protein P.III/class IV from Neisseria.
  • Outer membrane porin F (gene oprF) from Pseudomonas.
  • Protein TpN50 from Treponema pallidum [PMID: 8112835].
  • Peptidoglycan-associated lipoprotein (gene pal) from Escherichia coli, Haemophilus influenzae, Legionella pneumophila and Pseudomonas putida.
  • Outer membrane lipoprotein P6 from Haemophilus influenzae.
  • Escherichia coli hypothetical lipoprotein yiaD.
  • Vibrio parahaemolyticus sodium-type flagellar protein motY [PMID: 8636046, PMID: 15866878].

The OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan [PMID: 14763978].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
CDD
Pfam
PROSITE profiles