ProGlyProt ID BU248 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 mtRgpA 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 Biotin hydrazide labelling following periodate oxidation., chemical deglycosylation with TFMS and subsequent abolishment of immunoreactivity wth MAb 1B5 and MAb 7B4 after deglycosylation. 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