CpaA is the best characterized and most abundant effector secreted by several medically relevant Acinetobacter strains. CpaA stability and secretion depend on the membrane-bound chaperone CpaB, which is encoded adjacent to CpaA. ...
A secreted and cell associated protease plays a role in anthrax virulence through cleavage of numerous host substrates including host proteins involved in the coagulation cascade so as to potentially facilitate circulatory dissemination of bacteria. A regulatory factor of adhesin BslA expression. ...
Highly conserved between members of the Chlamydiaceae. Secreted chlamydial serine protease mediating the evasion of the innate immune response. Inhibits the complement activation pathway by degrading complement factor C3 and B. Degrading the antimicrobial peptides with anti-chlamydial activity. ...
Increase adhesion and colonization. A surface exposed and conserved cysteine protease responsible for SlpA cleavage and the maturation of the S-layer in C. difficile. Involved in host tissue degradation and bacterial colonization by cleaving extracellular matrix components fibronectin, laminin, and vitronectin. ...
Encoded within the pO157 plasmid that belongs to the family of serine protease inhibitor. Secreted by a type II secretory apparatus also encoded within pO157 plasmid and is transcriptionally activated by the Ler, so the production of StcE is coupled with activation of the LEE genes. ...
Two classes of IgA1 proteases: cleavage at either a prolyl-seryl (type1) or four amino acids away at a prolyl-threoryl bond (type 2). Display polymorphisms and antigenic variation. ...
Secreted by type I secretion pathway. Consists of two domains: an N-terminal catalytic domain of about 230 residues and a C-terminal domain of similar size that is required for secretion of the enzyme across the periplasm into the external medium. PDB code: 1KAP. ...