<p>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 [<cite idref="PUB00003748"/>], such as porin-like integral membrane proteins (such as ompA) [<cite idref="PUB00006250"/>], small lipid-anchored proteins (such as pal) [<cite idref="PUB00006564"/>], and MotB proton channels [<cite idref="PUB00035647"/>]. The N-terminal half is variable although some of the proteins in this group have the OmpA-like transmembrane domain <db_xref db="INTERPRO" dbkey="IPR000498"/> at the N terminus. OmpA from <taxon tax_id="562">Escherichia coli</taxon> is required for pathogenesis, and can interact with host receptor molecules [<cite idref="PUB00035646"/>]. 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 [<cite idref="PUB00035647"/>].</p> Outer membrane protein, OmpA/MotB, C-terminal