Omptin
| 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. 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.
Omptins have been linked to bacterial pathogenesis.