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CpaA
(Coagulation targeting metallo-endopeptidase of A. baumannii) |
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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. ... |
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InhA
(Immune inhibitor A) |
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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. ... |
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CPAF
(Chlamydial protease-like activating factor ) |
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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. ... |
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| alpha-clostripain |
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Heterodimeric enzyme composed of two polypeptide chains of molecular masses 43,000 kDa and15,400 kDa, for the heavy and light chains, respectively. The two chains are held together by strong noncovalent forces. Both polypeptide chains of native clostripain are encoded by a single gene. clostripain is synthesized as an inactive prepro-enzyme. In the presence of calcium ions, the core protein (amino acids 51-526) is able to catalyse the removal of the linker nonapeptide (residues 182-190). The linker has been shown to function as an intramolecular chaperon. ... |
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Cwp84
(Cell wall protein 84) |
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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. ... |
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| kappa-toxin |
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Clostridial collagenases include C. perfringens ColA, C. histolyticum ColG and ColH. Clostridial collagenases consist of three different segments. Segment 1 represents the catalytic domain containing the consensus motif for zinc proteases, HEXXH. Segment 2 is thought to be a spacing domain of unknown function. Segment 3 is the collagen binding domain. Collagen-binding domains are known to bind various types of collagen. The mode of binding is specific recognition of triple-helical conformation of collagen, not a nonspecific hydrophobic interaction. ... |
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| mu-toxin |
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The mu-toxin contain two conserved calcium-binding EF-hand loop sequences and a dockerin (Doc)-like sequence at its C terminus. ... |
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| Sialidase |
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Collagens and hyaluronic acids are major fibrous proteins constituting the extracellular matrix, while sialic acid-containing glycoconjugates cover the outer surface of the cytoplasmic membrane, some participating in the connection with the extracellular matrix components or cell-cell interactions. C. perfringens produces two different sialidases, NanI and NanJ are secreted sialidases while NanH is a cytoplasmic sialidase. ... |
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| Zmp1 |
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A proline-proline specific metalloprotease involved in the regulation of the adhesion-motility balance of C. difficile through cleavage of the putative adhesins CD2831 and CD3246. Release from the bacterial surface of CD2831 and the Zmp1 expression are both regulated by intra-cellular concentrations of cyclic di-GMP. ... |
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| Gelatinase |
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A member of the matrix metalloproteinase (MMP) family. Gelatinase expression is controlled via the global virulence-regulating locus, Fsr. ... |
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