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ProGlyProt ID
BU247
Organism Information
Organism Name
Porphyromonas (Bacteroides) gingivalis W50
Domain
Bacteria
Classification
Family: Porphyromonadaceae
Order: Bacteroidales
Class: Bacteroidia
Division or phylum: "Bacteroidetes"
 
 
Protein Information
Protein Name
HRgpA
Subcellular Location
Extracellular
Function
Cysteine proteases cause the degradation of several physiologically important proteins, including collagens, fibrin and fibrinogen and fibronectin. They also account for deregulatory effects on several host systems and are therefore considered important virulence determinants. The adhesin domains of Arg-gingipains mediate the adherence of P. gingivalis to epithelial cells.
 
 
Glycosylation Status
Glycosylation Type
Information currently not available with us.
Technique(s) used for Glycosylation Detection
Carbohydrate determination by methanolysis and GC-MS after beta-elimination.
 
 
Glycan Information
Glycan Annotation
Rha, Man, Gal, Glc, GalN(Ac), and GlcN(Ac) (i.e.,lacking Ara, Fuc, and NANA) totalling 2.1% by weight of protein.
 
 
Literature
Reference(s)
1) Curtis, M.A., Thickett, A., Slaney, J.M., Rangarajan, M., Aduse-Opoku, J., Shepherd, P., Paramonov, N. and Hounsell, E.F. (1999) Variable carbohydrate modifications to the catalytic chains of the RgpA and RgpB proteases of Porphyromonas gingivalis W50. Infect Immun, 67, 3816-3823. [PubMed: 10417143]
Year of Identification
1999
 
 
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