Search ProCGP (Characterized Glycoproteins) Search ProUGP (Uncharacterized Glycoproteins) Example Display Page Crystal Structures Homology Models Map Sequon Glyseq Extractor Blast Recent Reviews Related Tools & Databases Bibliography ProGlycProt ProGlyProt ID BU246 Organism Information Organism Name Porphyromonas gingivalis W50 Domain Bacteria Classification Family: Porphyromonadaceae Order: Bacteroidales Class: Bacteroidia Division or phylum: "Bacteroidetes" Taxonomic ID (NCBI) 837 Genome Sequence (s) GeneBank EMBL D26470 Gene Information Gene Name rgpA NCBI Gene ID Protein Information Protein Name Cysteine proteases (extracellular) Arg-gingipains UniProtKB/SwissProt ID P28784 NCBI RefSeq EMBL-CDS BAA05484.1 UniProtKB Sequence >sp|P28784|CPG1_PORGI Gingipain R1 OS=Porphyromonas gingivalis GN=rgpA PE=1 SV=2 MKNLNKFVSIALCSSLLGGMAFAQQTELGRNPNVRLLESTQQSVTKVQFRMDNLKFTEVQ TPKGMAQVPTYTEGVNLSEKGMPTLPILSRSLAVSDTREMKVEVVSSKFIEKKNVLIAPS KGMIMRNEDPKKIPYVYGKSYSQNKFFPGEIATLDDPFILRDVRGQVVNFAPLQYNPVTK TLRIYTEITVAVSETSEQGKNILNKKGTFAGFEDTYKRMFMNYEPGRYTPVEEKQNGRMI VIVAKKYEGDIKDFVDWKNQRGLRTEVKVAEDIASPVTANAIQQFVKQEYEKEGNDLTYV LLVGDHKDIPAKITPGIKSDQVYGQIVGNDHYNEVFIGRFSCESKEDLKTQIDRTIHYER NITTEDKWLGQALCIASAEGGPSADNGESDIQHENVIANLLTQYGYTKIIKCYDPGVTPK NIIDAFNGGISLVNYTGHGSETAWGTSHFGTTHVKQLTNSNQLPFIFDVACVNGDFLFSM PCFAEALMRAQKDGKPTGTVAIIASTINQSWASPMRGQDEMNEILCEKHPNNIKRTFGGV TMNGMFAMVEKYKKDGEKMLDTWTVFGDPSLLVRTLVPTKMQVTAPAQINLTDASVNVSC DYNGAIATISANGKMFGSAVVENGTATINLTGLTNESTLTLTVVGYNKETVIKTINTNGE PNPYQPVSNLTATTQGQKVTLKWDAPSTKTNATTNTARSVDGIRELVLLSVSDAPELLRS GQAEIVLEAHDVWNDGSGYQILLDADHDQYGQVIPSDTHTLWPNCSVPANLFAPFEYTVP ENADPSCSPTNMIMDGTASVNIPAGTYDFAIAAPQANAKIWIAGQGPTKEDDYVFEAGKK YHFLMKKMGSGDGTELTISEGGGSDYTYTVYRDGTKIKEGLTETTYRDAGMSAQSHEYCV EVKYAAGVSPKVCVDYIPDGVADVTAQKPYTLTVVGKTITVTCQGEAMIYDMNGRRLAAG RNTVVYTAQGGYYAVMVVVDGKSYVEKLAVK Sequence length 991 AA 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 PAS staining, biotin hydrazide labelling following periodate oxidation and subsequent abolishment of immunoreactivity wth MAb 1B5 and MAb 7B4 after deglycosylation. Literatures Reference(s) 1) Paramonov, N., Rangarajan, M., Hashim, A., Gallagher, A., Aduse-Opoku, J., Slaney, J.M., Hounsell, E. and Curtis, M.A. (2005) Structural analysis of a novel anionic polysaccharide from Porphyromonas gingivalis strain W50 related to Arg-gingipain glycans. Mol Microbiol, 58, 847-863. [PubMed: 16238632] 2) Rangarajan, M., Hashim, A., Aduse-Opoku, J., Paramonov, N., Hounsell, E.F. and Curtis, M.A. (2005) Expression of Arg-Gingipain RgpB is required for correct glycosylation and stability of monomeric Arg-gingipain RgpA from Porphyromonas gingivalis W50. Infect Immun, 73, 4864-4878. [PubMed: 16041000] 3) 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] 4) Rangarajan, M., Smith, S.J., U, S. and Curtis, M.A. (1997) Biochemical Year of Identification 1999