Omptin

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]

Omptin
Identifiers
SymbolOmptin
PfamPF01278
Pfam clanCL0193
PROSITEPDOC00657
MEROPSA26
SCOP21i78 / SCOPe / SUPFAM
OPM superfamily27
OPM protein2x55
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Omptins have been linked to bacterial pathogenesis.[1]

References

  1. 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. S2CID 7362500.
  2. 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


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