| ProGlyProt ID | BU247 | | Organism Information | | Organism Name | Porphyromonas gingivalis W50 | | Domain | Bacteria | | Classification | Family: Porphyromonadaceae
Order: Bacteroidales
Class: Bacteroidia
Division or phylum: "Bacteroidetes" | | Taxonomic ID (NCBI) | | | Genome Sequence (s) | | GeneBank | | | EMBL | | | Gene Information | | Gene Name | | | NCBI Gene ID | | | Protein Information | | Protein Name | HRgpA | | UniProtKB/SwissProt ID | | | NCBI RefSeq | | | EMBL-CDS | | | UniProtKB Sequence | | | Sequence length | | | 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. | | Literatures | | 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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