ProGP171

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ProGP ID ProGP171
Validation Status Uncharacterized
Organism Information
Organism NamePorphyromonas gingivalis W50
Domain Bacteria
Classification Family: Porphyromonadaceae
Order: Bacteroidales
Class: Bacteroidia
Division or phylum: "Bacteroidetes"
Taxonomic ID (NCBI) 837
Genome Sequence(s)
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 NamergpA
Protein Information
Protein NameCysteine proteases (extracellular) Arg-gingipains (RgpA)
UniProtKB/SwissProt ID P28784
EMBL-CDSBAA05484.1
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 LocationExtracellular
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 DetectionPAS 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 Identification1999
Year of Identification Month Wise1999.5
ReferenceParamonov, 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]
AuthorParamonov, N., Rangarajan, M., Hashim, A., Gallagher, A., Aduse-Opoku, J., Slaney, J.M., Hounsell, E. Curtis, M.A.
Research GroupMRC Molecular Pathogenesis Group, Centre for Infectious Disease, Institute of Cell and Molecular Science, Barts and The London, Queen Marys School of Medicine and Dentistry, 4 Newark Street, London
Corresponding Author Curtis, M.A.
ContactMRC Molecular Pathogenesis Group, Centre for Infectious Disease, Institute of Cell and Molecular Science, Barts and The London, Queen Marys School of Medicine and Dentistry, 4 Newark Street, London
ReferenceRangarajan, 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]
AuthorRangarajan, M., Hashim, A., Aduse-Opoku, J., Paramonov, N., Hounsell, E.F. Curtis, M.A.
Research GroupMRC Molecular Pathogenesis Group, Centre for Infectious Disease, Institute of Cell and Molecular Science, Barts and The London, Queen Marys School of Medicine and Dentistry, 4 Newark Street, London E1 2AT, United Kingdom
Corresponding Author Curtis, M.A.
ContactMRC Molecular Pathogenesis Group, Centre for Infectious Disease, Institute of Cell and Molecular Science, Barts and The London, Queen Marys School of Medicine and Dentistry, 4 Newark Street, London E1 2AT, United Kingdom
ReferenceCurtis, 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.
AuthorCurtis, M.A., Thickett, A., Slaney, J.M., Rangarajan, M., Aduse-Opoku, J., Shepherd, P., Paramonov, N. Hounsell, E.F.
Research GroupMRC Molecular Pathogenesis Group, Department of Oral Microbiology, St. Bartholomews and the Royal London School of Medicine and Dentistry, Queen Mary and Westfield College, London E1 2AA, United Kingdom
Corresponding Author Hounsell, E.F.
ContactMRC Molecular Pathogenesis Group, Department of Oral Microbiology, St. Bartholomews and the Royal London School of Medicine and Dentistry, Queen Mary and Westfield College, London E1 2AA, United Kingdom
ReferenceRangarajan, 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. Biochem J, 323 ( Pt 3), 701-709. [PubMed: 9169603]
AuthorRangarajan, M., Smith, S.J., U, S. and Curtis, M.A.
Research GroupMRC Molecular Pathogenesis Group, Department of Oral Microbiology, St. Bartholomews and the Royal London School of Medicine and Dentistry, 32 Newark Street, London E1 2AA, U.K
Corresponding Author Curtis, M.A.
ContactMRC Molecular Pathogenesis Group, Department of Oral Microbiology, St. Bartholomews and the Royal London School of Medicine and Dentistry, 32 Newark Street, London E1 2AA, U.K