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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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BbHtrA
(High temperature requirement A) |
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HtrA belongs to a highly conserved family of serine proteases that are found in higher life forms such as humans as well as prokaryotes like bacteria. Numerous bacteria have been convincingly reported to deliver HtrA directly into the extracellular space including Gram-negative and Gram-positive pathogens such as Helicobacter pylori, Campylobacter jejuni, Borrelia burgdorferi, Bacillus anthracis, and Chlamydia species. B. burgdorferi exhibited HtrA proteins both in membrane-anchored and soluble forms. ... |
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| Lon |
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The ATP-dependent Lon protease is a member of the AAA+ (ATPases associated with a variety of cellular activities) superfamily. Based on sequence and structure information, Lon proteases are divided into three subfamilies. LonA proteases are found mainly in bacteria and eukaryotes, whereas LonB proteases are found only in Archaea, LonC is less well characterized. Unlike most bacteria encoding only one Lon homolog, B. burgdorferi encodes two Lon homlogs: Lon-1 (~90.7 kDa), Lon-2 (~90.3 kDa). ... |
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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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