ProGP246

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ProGP ID ProGP246
Validation Status Uncharacterized
Organism Information
Organism NameStaphylococcus aureus (ISP479C and PS767)
Domain Bacteria
Classification Family: Staphylococcaceae
Order: Bacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI) 367830
Genome Sequence(s)
GenBank CP000255 
EMBL CP000255 
Gene Information
Gene NamesraP
Protein Information
Protein NameSraP (serine-rich adhesin for platelets)
UniProtKB/SwissProt ID Q2FUW1
Sequence length 2271 AA
Subcellular LocationSurface (Secreted)
Function SraP, a cell wall-anchored glycoprotein, mediates the direct binding of S. aureus to platelets through a platelet-binding domain located within its N-terminal region. Its expression appears to be a virulence determinant in endovascular infection.
Glycosylation Status
Glycosylation Type O- (Ser/Thr) linked
Technique(s) used for Glycosylation DetectionCarbohydrate conntent analysis by glycan detection assay
Glycan Information
Glycan Annotation Glycosylated by GlcNAc-containing oligosaccharides in E. coli.
Protein Glycosylation linked (PGL) gene(s)
OST ProGT IDProGT79,ProGT80
Characterized Accessory Gene(s)gtfA and gtfB
Additional CommentE. coli was used as the in vivo glycosylation system for studying the glycosylation of SraP1–743 using GtfA and GtfB enzymes that transferred N-acetylglucosamine-containing oligosaccharides to the recombinant protein.
Literature
Year of Identification2005
Year of Identification Month Wise2005.04
ReferenceSiboo IR, Chambers HF, Sullam PM. (2005) Role of SraP, a Serine-Rich Surface Protein of Staphylococcus aureus, in binding to human platelets. Infect Immun., 73(4):2273-80.
AuthorSiboo IR, Chambers HF, Sullam PM
Research GroupDivision of Infectious Diseases, VA Medical Center (111W), 4150 Clement St., San Francisco, CA 94121, USA.
Corresponding Author Sullam PM
ContactDivision of Infectious Diseases, VA Medical Center (111W), 4150 Clement St., San Francisco, CA 94121, USA.