SMART: Pfam domain OmpA

OmpA

PFAM accession number:	PF00691
Interpro abstract (IPR006665):	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 [ (PUBMED: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 [ (PUBMED:8636046) (PUBMED:15866878) ]. The OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan [ (PUBMED:14763978) ]. 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 [ (PUBMED:1538702) ], such as porin-like integral membrane proteins (such as ompA) [ (PUBMED:2202726) ], small lipid-anchored proteins (such as pal) [ (PUBMED:10515919) ], and MotB proton channels [ (PUBMED: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 [ (PUBMED: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 [ (PUBMED:17052729) ].

PFAM accession number:

PF00691

Interpro abstract (IPR006665):

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 [ (PUBMED: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 [ (PUBMED:8636046) (PUBMED:15866878) ].

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

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 [ (PUBMED:1538702) ], such as porin-like integral membrane proteins (such as ompA) [ (PUBMED:2202726) ], small lipid-anchored proteins (such as pal) [ (PUBMED:10515919) ], and MotB proton channels [ (PUBMED: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 [ (PUBMED: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 [ (PUBMED:17052729) ].

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