Global InformationOmptin information
| Omptin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Omptin | ||||||||
| Pfam | PF01278 | ||||||||
| Pfam clan | CL0193 | ||||||||
| PROSITE | PDOC00657 | ||||||||
| MEROPS | A26 | ||||||||
| SCOP2 | 1i78 / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 27 | ||||||||
| OPM protein | 2x55 | ||||||||
| |||||||||
Omptins (EC 3.4.23.49, protease VII, protease A, gene ompT proteins, ompT protease, protein a, Pla, OmpT) are a family of bacterial proteases.[1] They are aspartate proteases, which cleave peptides with the use of a water molecule. Found in the outer membrane of gram-negative enterobacteria such as Shigella flexneri, Yersinia pestis, Escherichia coli, and Salmonella enterica. Omptins consist of a widely conserved beta barrel spanning the membrane with 5 extracellular loops. These loops are responsible for the various substrate specificities. These proteases rely upon binding of lipopolysaccharide for activity.[2]
Omptins have been linked to bacterial pathogenesis.[1]
- ^ a b Hritonenko V, Stathopoulos C (2007). "Omptin proteins: an expanding family of outer membrane proteases in Gram-negative Enterobacteriaceae". Molecular Membrane Biology. 24 (5–6): 395–406. doi:10.1080/09687680701443822. PMID 17710644. S2CID 7362500.
- ^ Kukkonen M, Korhonen TK (July 2004). "The omptin family of enterobacterial surface proteases/adhesins: from housekeeping in Escherichia coli to systemic spread of Yersinia pestis". International Journal of Medical Microbiology. 294 (1): 7–14. doi:10.1016/j.ijmm.2004.01.003. PMID 15293449.