ProGlyProt IDBU247
Organism Information
Organism NamePorphyromonas gingivalis W50
DomainBacteria
ClassificationFamily: 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 NameHRgpA
UniProtKB/SwissProt ID
NCBI RefSeq
EMBL-CDS
UniProtKB Sequence
Sequence length
Subcellular LocationExtracellular
FunctionCysteine 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 TypeInformation currently not available with us.
Technique(s) used for Glycosylation DetectionCarbohydrate 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 Identification1999