Protein Domain : OmpA-like domain superfamily IPR036737

Type	Homologous_superfamily
Description	This entry represents a domain superfamily with a β/α/β/α-β(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 []. The N-terminal half 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 [ ]. 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 [].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 [ ].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 [ , ].The OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan [].
Short Name	OmpA-like_sf