OmpA domain

In molecular biology, the OmpA domain is a conserved protein domain with a beta/alpha/beta/alpha-beta(2) structure found in the C-terminal region of many Gram-negative bacterial outer membrane proteins, such as porin-like integral membrane proteins (such as ompA), small lipid-anchored proteins (such as pal), and MotB proton channels.^[1][2][3][4] The N-terminal half of these proteins is variable although some of the proteins in this group have the OmpA-like transmembrane domain at the N terminus. OmpA from Escherichia coli is required for pathogenesis, and can interact with host receptor molecules.^[5] MotB (and MotA) serve 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.^[4]

OmpA family
crystal structure of tolb/pal complex
Identifiers
Symbol	OmpA
Pfam	PF00691
InterPro	IPR006665
PROSITE	PDOC00819
SCOP2	1r1m / SCOPe / SUPFAM
TCDB	1.B.6
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

See also

• OmpA-like transmembrane domain