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staphopain proregion domain-containing protein
This domain is the proregion of the cysteine protease staphopain. Like many papain type peptidases, staphopain is synthesised as an inactive precursor and cleavage of the proregion is required for activation. This proregion has a half-barrel or barrel-sandwich hybrid fold. The proregion blocks the active site cleft of the mature enzyme on one side of the nucleophilic cysteine [1] [1]. 15518582. Prostaphopain B structure: a comparison of proregion-mediated and staphostatin-mediated protease inhibition. Filipek R, Szczepanowski R, Sabat A, Potempa J, Bochtler M;. Biochemistry. 2004;43:14306-14315. (from Pfam)
C47 family peptidase
Staphopains are one of four major families of proteinases secreted by the Gram-positive Staphylococcus aureus. These staphylococcal cysteine proteases are secreted as preproenzymes that are proteolytically cleaved to generate the mature enzyme. [1]. 11767947. Molecular cloning and biochemical characterisation of proteases from Staphylococcus epidermidis. Dubin G, Chmiel D, Mak P, Rakwalska M, Rzychon M, Dubin A;. Biol Chem 2001;382:1575-1582. [2]. 11447146. Decreased amounts of cell wall-associated protein A and fibronectin-binding proteins in Staphylococcus aureus sarA mutants due to up-regulation of extracellular proteases. Karlsson A, Saravia-Otten P, Tegmark K, Morfeldt E, Arvidson S;. Infect Immun 2001;69:4742-4748. [3]. 12437090. Extracellular proteases of Staphylococcus spp. Dubin G;. Biol Chem 2002;383:1075-1086. (from Pfam)
cysteine protease staphopain
cysteine protease staphopain is a C47 family peptidase such as staphopain A that plays an important role in the inhibition of host innate immune response, cleaving host elastins found in connective tissues, pulmonary surfactant protein A in the lungs, and the chemokine receptor CXCR2 on leukocytes
cysteine protease staphopain A
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