ProGP170 (Cysteine proteases (extracellular) Arg-gingipains (RgpA))
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| ProGP ID | ProGP170 (Cysteine proteases (extracellular) Arg-gingipains (RgpA)) |
| Validation Status | Uncharacterized |
| Organism Information | |
| Organism Name | Porphyromonas gingivalis W50 |
| Domain | Bacteria |
| Classification | Phylum : Bacteroidetes Class : Bacteroidia Orders : Bacteroidales Family : Porphyromonadaceae Genus : Porphyromonas Species : gingivalis Strain : W50 |
| Taxonomic ID (NCBI) | 837 |
| Genome Information | |
| GenBank | D26470 |
| EMBL | D26470 |
| Organism Additional Information | Porphyromonas gingivalis is a Gram-negative anaerobic bacterium responsible for causing adult periodontal disease, a chronic inflammatory condition of the periodontal tissues. It is the source of a number of virulence factors that are thought to be important for deregulation of innate and inflammatory systems in the host. |
| Gene Information | |
| Gene Name | rgpA |
| Protein Information | |
| Protein Name | Cysteine proteases (extracellular) Arg-gingipains (RgpA) |
| UniProtKB/SwissProt ID | P28784 |
| 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 | |
| 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. |
| Glycan Information | |
| Glycan Annotation | Linkage: GalN(Ac)-Ser/Thr. Ara, Rha, Fuc,Man, Gal, Glc, GalN(Ac), GlcN(Ac), and N-acetylneuraminic acid (NANA) totalling 14.4% by weight of protein. The glycan chains are structurally and immunologically related to the cell surface polymer of this Gram-negative bacterium. |
| Literature | |
| Year of Identification | 1999 |
| Year of Identification Month Wise | 1999.5 |
| Reference | 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. Molecular microbiology, 58(3), pp.847-863. |
| Corresponding Author | Minnie Rangarajan |
| Contact | MRC Molecular Pathogenesis Group, Centre for Infectious Disease, Institute of Cell and Molecular Science, Barts and The London, Queen Mary's School of Medicine and Dentistry, 4 Newark Street, London E1 2AT, United Kingdom |
| Reference | 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. Infection and immunity, 73(8), pp.4864-4878. |
| Corresponding Author | Minnie Rangarajan |
| Contact | MRC Molecular Pathogenesis Group, Centre for Infectious Disease, Institute of Cell and Molecular Science, Barts and The London, Queen Mary's School of Medicine and Dentistry, 4 Newark Street, London E1 2AT, United Kingdom |
| Reference | 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. Infection and immunity, 67(8), pp.3816-3823. |
| Corresponding Author | Michael A. Curtis |
| Contact | MRC Molecular Pathogenesis Group, Department of Oral Microbiology, St. Bartholomew's and the Royal London School of Medicine and Dentistry, Queen Mary and Westfield College, London E1 2AA, United Kingdom |
| Reference | RANGARAJAN, M., SMITH, S.J., U, S. and CURTIS, M.A., 1997. Biochemical characterization of the arginine-specific proteases of Porphyromonas gingivalis W50 suggests a common precursor. Biochemical Journal, 323(3), pp.701-709. |
| Corresponding Author | M Rangarajan |
| Contact | MRC Molecular Pathogenesis Group, Department of Oral Microbiology, St. Bartholomew's and the Royal London School of Medicine and Dentistry, 32 Newark Street, London E1 2AA, U.K |