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WxL protein host-binding domain-containing protein
This domain (previously known as DUF3324) is found in WxL interacting proteins (WxLIP) which play a role in virulence and are widely distributed in firmicutes. The WxL proteins usually occur within a gene cluster that contains two WxL proteins and a WxL interacting protein composed of three domains: peptidoglycan binding domain (PGBD), host binding domain (HBD), and transmembrane helix (TMH). The domain represented by this entry is likely to interact with proteins on the surface of eukaryotic host endothelial cells. This HBD domain is frequently found in combination with PGBD domain (Pfam:PF06030) and both were shown to function synergistically as a single unit that binds to the peptidoglycan and interacts with the eukaryotic host [1]. The HBD domain is predicted to adopt a beta-sandwich with an Ig-like topology. [1]. 37833244. DUF916 and DUF3324 in the WxL protein cluster bind to WxL and link bacterial and host surfaces. Hassan MU, Chaudhuri RR, Williamson MP;. Protein Sci. 2023;32:e4806. (from Pfam)
WxL protein peptidoglycan domain-containing protein
This domain (previously known as DUF916) is found in WxL interacting proteins (WxLIP) which play a role in virulence and are widely distributed in firmicutes. The WxL proteins usually occur within a gene cluster that contains two WxL proteins and a WxL interacting protein composed of three domains: peptidoglycan binding domain (PGBD), host binding domain (HBD), and transmembrane helix (TMH). The domain represented by this entry is involved in binding to peptidoglycan and to WxL, and anchoring the protein cluster onto the bacterial surface. This PGBD domain is frequently found in combination with HBD domain (Pfam:PF11797) and both were shown to function synergistically as a single unit that binds to the peptidoglycan and interacts with the eukaryotic host [1]. The PGBD domain is predicted to adopt a beta-sandwich with an Ig-like topology. [1]. 37833244. DUF916 and DUF3324 in the WxL protein cluster bind to WxL and link bacterial and host surfaces. Hassan MU, Chaudhuri RR, Williamson MP;. Protein Sci. 2023;32:e4806. (from Pfam)
DUF916 and DUF3324 domain-containing protein
LPXTG cell wall anchor domain-containing protein
This model describes the LPXTG motif-containing region found at the C-terminus of many surface proteins of Streptococcus and Streptomyces species. Cleavage between the Thr and Gly by sortase or a related enzyme leads to covalent anchoring at the new C-terminal Thr to the cell wall. Hits that do not lie at the C-terminus or are not found in Gram-positive bacteria are probably false-positive. A common feature of this proteins containing this domain appears to be a high proportion of charged and zwitterionic residues immediatedly upstream of the LPXTG motif. This model differs from other descriptions of the LPXTG region by including a portion of that upstream charged region.
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