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| ShdA |
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ShdA passenger domain consists of ~1,500 amino acid residues that can be divided into two regions based on features of the primary amino acid sequence: an N-terminal nonrepeat region followed by a repeat region composed of two types of imperfect direct amino acid repeats, called type A and type B. The repeat region bound fibronectin with an affinity similar to that for the complete ShdA passenger domain. ... |
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| SinH |
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N-terminal 350 residues exhibits homology with invasin of Yersinia pseudotuberculosis (49.5% identity) and intimin of E. coli O111 (enteropathogenic E. coli) (48% identity). The amino termini of invasin and intimin serve as membrane-spanning anchors in the bacterial outer membrane. ... |
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IcsA (VirG)
(Ics for intercellular spread) |
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Three distinctive domains: the N-terminal signal sequence (1-52), the 706 α-domain (53-758), the 344 C-terminal β-core. β-core embedded in the outer membrane, the C-terminal ~220 aa of IcsAα (509-729) are essential for the unipolar distribution of IcsA, the residues (103-433) are the binding site for N-WASP. residues (53-506) is the region of vinculin interaction and is essential for F-actin assembly. ... |
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| Clumping factor |
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Belongs to MSCRAMMs family. Ser-Asp rich fibrinogen-binding proteins (the proteins having the SD dipeptide repeats have so far been found only in S. aureus and S. epidermidis). The clfA and clfB genes are not allelic variants but are distinct genes. They are not closely linked, in contrast to the fnbA and fnbB genes. ... |
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CNA
(Collagen binding protein) |
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Belongs to MSCRAMMs family. Consists of an N-terminal signal peptide, a non-repetitive A region, one to four repeated units (B-region), followed by a cell wall anchor region, a transmembrane segment, and a short positively charged cytoplasmic tail. The A region of CNA-(30-531) was found to be fully responsible for the collagen binding activity of CNA. PDB code : 1AMX. ... |
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Eap/Map
(Extracellular adherence protein/MHC analogous protein) |
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Belongs to MSCRAMMs family. Unusual property: Eap can bind back to the S. aureus cell wall. No cell-wall-spanning domain or a membrane anchor and LPXTG motif. Comprises six repeats of a 110 amino acid residue motif with a central portion composed of a subdomain with high homology to the peptide-binding groove of mammalian major histocompatibility complex class II (MHCII) molecules. ... |
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EbpS
(Elastin-binding protein) |
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Belongs to MSCRAMMs family. An integral membrane protein, the elastin-binding domain is located at the N-terminus and is exposed at the surface. Lacks a signal sequence and the C-terminal LPXTG motif. ... |
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FnBPs
(Fibronectin binding proteins) |
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Belongs to MSCRAMMs family. Most strains of S. aureus express two related Fn-binding proteins FnBPA and FnBPB, which are encoded by closely linked genes. ... |
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SDr
(Ser-Asp rich proteins) |
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Characterized by the R domain containing Ser-Asp dipeptide repeats. Structural organization similar to that of ClfA and ClfB, except for an additional B repeat comprising 110-113 residues located between A domain and the R domain. The function of B domain is unknown. Each repeat has high affinity Ca2+ -binding sites. Bound Ca2+ is required to promote the rigid rod-like structure of the B repeat array. ... |
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| C5a peptidase |
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All group A streptococcal serotypes and group B, C, and G streptococci of human origin produce the C5a peptidase. The enzyme is highly conserved. ... |
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