Structural highlights
Function
SSPA_STAAU Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Prokesová L, Potuzníková B, Potempa J, Zikán J, Radl J, Hachová L, Baran K, Porwit-Bobr Z, John C. Cleavage of human immunoglobulins by serine proteinase from Staphylococcus aureus. Immunol Lett. 1992 Feb 15;31(3):259-65. PMID:1372285 doi:10.1016/0165-2478(92)90124-7
- ↑ Drapeau GR, Boily Y, Houmard J. Purification and properties of an extracellular protease of Staphylococcus aureus. J Biol Chem. 1972 Oct 25;247(20):6720-6 PMID:4627743
