The outer membrane efflux protein is a protein family member that forms trimeric (three-piece) channels allowing the export of a variety of substrates in gram-negative bacteria. Each efflux protein is composed of two repeats. The trimeric channel is composed of a 12-stranded beta-barrel that spans the outer membrane, and a long tail helical barrel that spans the periplasm.
| Outer membrane efflux protein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifiers | |||||||||
| Symbol | OEP | ||||||||
| Pfam | PF02321 | ||||||||
| InterPro | IPR003423 | ||||||||
| SCOP2 | 1ek9 / SCOPe / SUPFAM | ||||||||
| TCDB | 1.B.17 | ||||||||
| OPM superfamily | 34 | ||||||||
| OPM protein | 1yc9 | ||||||||
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Examples include the Escherichia coli TolC outer membrane protein, which is required for proper expression of outer membrane protein genes; the Rhizobium nodulation protein; and the Pseudomonas FusA protein, which is involved in resistance to fusaric acid.
References
edit- Johnson JM, Church GM (April 1999). "Alignment and structure prediction of divergent protein families: periplasmic and outer membrane proteins of bacterial efflux pumps". Journal of Molecular Biology. 287 (3): 695–715. CiteSeerX 10.1.1.73.559. doi:10.1006/jmbi.1999.2630. PMID 10092468.
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