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 | ||||||||
| |||||||||
See also
References
- Bouveret E, Benedetti H, Rigal A, Loret E, Lazdunski C (October 1999). "In vitro characterization of peptidoglycan-associated lipoprotein (PAL)-peptidoglycan and PAL-TolB interactions". J. Bacteriol. 181 (20): 6306–11. doi:10.1128/JB.181.20.6306-6311.1999. PMC 103764. PMID 10515919.
- De Mot R, Proost P, Van Damme J, Vanderleyden J (February 1992). "Homology of the root adhesin of Pseudomonas fluorescens OE 28.3 with porin F of P. aeruginosa and P. syringae". Mol. Gen. Genet. 231 (3): 489–93. doi:10.1007/BF00292721. PMID 1538702. S2CID 7518948.
- Freudl R, Klose M, Henning U (June 1990). "Export and sorting of the Escherichia coli outer membrane protein OmpA". J. Bioenerg. Biomembr. 22 (3): 441–9. doi:10.1007/BF00763176. PMID 2202726. S2CID 22623025.
- Hosking ER, Vogt C, Bakker EP, Manson MD (December 2006). "The Escherichia coli MotAB proton channel unplugged". J. Mol. Biol. 364 (5): 921–37. doi:10.1016/j.jmb.2006.09.035. PMID 17052729.
- Selvaraj SK, Periandythevar P, Prasadarao NV (April 2007). "Outer membrane protein A of Escherichia coli K1 selectively enhances the expression of intercellular adhesion molecule-1 in brain microvascular endothelial cells". Microbes Infect. 9 (5): 547–57. doi:10.1016/j.micinf.2007.01.020. PMC 1993839. PMID 17368067.