Omptin
| Omptin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Omptin | ||||||||
| Pfam | PF01278 | ||||||||
| Pfam clan | CL0193 | ||||||||
| PROSITE | PDOC00657 | ||||||||
| MEROPS | A26 | ||||||||
| SCOP | 1i78 | ||||||||
| SUPERFAMILY | 1i78 | ||||||||
| 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 extra-cellular loops. These loops are responsible for the various substrate specificities. These proteases rely upon binding of lipopolysaccharide for activity.[2]
Omptins have been linked with pathogenesis in several bacteria.[1]
References
- 1 2 Hritonenko V, Stathopoulos C (2007). "Omptin proteins: an expanding family of outer membrane proteases in Gram-negative Enterobacteriaceae". Mol. Membr. Biol. 24 (5–6): 395–406. doi:10.1080/09687680701443822. PMID 17710644.
- ↑ 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". Int. J. Med. Microbiol. 294 (1): 7–14. doi:10.1016/j.ijmm.2004.01.003. PMID 15293449.
Further reading
- Haiko J, Laakkonen L, Juuti K, Kalkkinen N, Korhonen TK (September 2010). "The omptins of Yersinia pestis and Salmonella enterica cleave the reactive center loop of plasminogen activator inhibitor 1". J. Bacteriol. 192 (18): 4553–61. doi:10.1128/JB.00458-10. PMC 2937412. PMID 20639337. Retrieved 2011-04-10.
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