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P95493

- CPG2_PORGI

UniProt

P95493 - CPG2_PORGI

Protein

Gingipain R2

Gene

rgpB

Organism
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (03 Oct 2003)
      Previous versions | rss
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    Functioni

    Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Its proteolytic activity is a major factor in both periodontal tissue destruction and in bacterial host defense mechanisms. Activates complement C3 and C5 By similarity.By similarity

    Catalytic activityi

    Hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1.

    Enzyme regulationi

    Inhibited by human histatin-3 1/24 (histatin-5).1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei440 – 4401Proton donor
    Active sitei473 – 4731Nucleophile

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: InterPro
    2. protein binding Source: IntAct

    GO - Biological processi

    1. pathogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Virulence

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    BioCyciPGIN242619:GHX8-458-MONOMER.
    BRENDAi3.4.22.37. 4997.
    SABIO-RKP95493.

    Protein family/group databases

    MEROPSiC25.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gingipain R2 (EC:3.4.22.37)
    Alternative name(s):
    Arg-gingipain
    Gingipain 2
    RGP-2
    Gene namesi
    Name:rgpB
    Synonyms:prtRII, rgp2
    Ordered Locus Names:PG_0506
    OrganismiPorphyromonas gingivalis (strain ATCC BAA-308 / W83)
    Taxonomic identifieri242619 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas
    ProteomesiUP000000588: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424By similarityAdd
    BLAST
    Propeptidei25 – 2292051 PublicationPRO_0000026535Add
    BLAST
    Chaini230 – 736507Gingipain R2PRO_0000026536Add
    BLAST

    Keywords - PTMi

    Zymogen

    Proteomic databases

    PRIDEiP95493.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HTN3P155167EBI-8505881,EBI-738783From a different organism.

    Protein-protein interaction databases

    IntActiP95493. 1 interaction.
    MINTiMINT-8415911.
    STRINGi242619.PG0506.

    Structurei

    Secondary structure

    1
    736
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 416
    Beta strandi44 – 507
    Beta strandi55 – 617
    Beta strandi64 – 707
    Beta strandi87 – 937
    Beta strandi96 – 11217
    Helixi130 – 1323
    Helixi139 – 1424
    Beta strandi151 – 1544
    Beta strandi158 – 1603
    Beta strandi163 – 1708
    Beta strandi173 – 1764
    Turni177 – 1804
    Beta strandi181 – 19818
    Helixi215 – 2217
    Beta strandi240 – 2456
    Helixi247 – 2526
    Helixi254 – 2629
    Beta strandi266 – 2716
    Helixi272 – 2754
    Helixi281 – 29313
    Beta strandi299 – 3068
    Turni308 – 3103
    Beta strandi314 – 3163
    Beta strandi319 – 3224
    Helixi323 – 3264
    Beta strandi329 – 3335
    Beta strandi336 – 3427
    Helixi347 – 36216
    Turni369 – 3724
    Beta strandi373 – 3786
    Helixi387 – 3893
    Helixi392 – 40615
    Beta strandi409 – 41810
    Helixi421 – 43010
    Beta strandi433 – 4397
    Beta strandi443 – 4464
    Turni447 – 4493
    Turni453 – 4553
    Helixi456 – 4583
    Beta strandi467 – 4748
    Beta strandi480 – 4823
    Helixi485 – 4917
    Beta strandi502 – 5098
    Beta strandi512 – 5143
    Helixi515 – 52713
    Helixi535 – 5373
    Helixi539 – 56426
    Beta strandi565 – 5695
    Beta strandi589 – 5924
    Beta strandi596 – 6049
    Beta strandi608 – 6136
    Beta strandi616 – 6227
    Beta strandi627 – 6315
    Beta strandi640 – 6478
    Beta strandi654 – 6618

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CVRX-ray2.00A230-664[»]
    4IEFX-ray2.30A/C/E/G25-229[»]
    B/D/F/H230-662[»]
    ProteinModelPortaliP95493.
    SMRiP95493. Positions 230-661.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP95493.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C25 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    KOiK08589.
    OMAiKENGRMI.
    OrthoDBiEOG6BGNW2.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.40.50.10390. 1 hit.
    3.40.50.1460. 1 hit.
    InterProiIPR029030. Caspase-like_dom.
    IPR001769. Gingipain.
    IPR029031. Gingipain_N.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR005536. Peptidase_C25_Ig-like_domain.
    IPR012600. Propeptide_C25.
    IPR026444. Secre_tail.
    [Graphical view]
    PfamiPF01364. Peptidase_C25. 1 hit.
    PF03785. Peptidase_C25_C. 1 hit.
    PF08126. Propeptide_C25. 1 hit.
    [Graphical view]
    SUPFAMiSSF81296. SSF81296. 1 hit.
    TIGRFAMsiTIGR04183. Por_Secre_tail. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P95493-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKNFSRIVS IVAFSSLLGG MAFAQPAERG RNPQVRLLSA EQSMSKVQFR    50
    MDNLQFTGVQ TSKGVAQVPT FTEGVNISEK GTPILPILSR SLAVSETRAM 100
    KVEVVSSKFI EKKDVLIAPS KGVISRAENP DQIPYVYGQS YNEDKFFPGE 150
    IATLSDPFIL RDVRGQVVNF APLQYNPVTK TLRIYTEIVV AVSETAEAGQ 200
    NTISLVKNST FTGFEDIYKS VFMNYEATRY TPVEEKENGR MIVIVPKKYE 250
    EDIEDFVDWK NQRGLRTEVK VAEDIASPVT ANAIQQFVKQ EYEKEGNDLT 300
    YVLLVGDHKD IPAKITPGIK SDQVYGQIVG NDHYNEVFIG RFSCESKEDL 350
    KTQIDRTIHY ERNITTEDKW LGQALCIASA EGGPSADNGE SDIQHENIIA 400
    NLLTQYGYTK IIKCYDPGVT PKNIIDAFNG GISLANYTGH GSETAWGTSH 450
    FGTTHVKQLT NSNQLPFIFD VACVNGDFLY NVPCFAEALM RAQKDGKPTG 500
    TVAIIASTIN QSWASPMRGQ DEMNEILCEK HPNNIKRTFG GVTMNGMFAM 550
    VEKYKKDGEK MLDTWTVFGD PSLLVRTLVP TKMQVTAPAN ISASAQTFEV 600
    ACDYNGAIAT LSDDGDMVGT AIVKDGKAII KLNESIADET NLTLTVVGYN 650
    KVTVIKDVKV EGTSIADVAN DKPYTVAVSG KTITVESPAA GLTIFDMNGR 700
    RVATAKNRMV FEAQNGVYAV RIATEGKTYT EKVIVK 736
    Length:736
    Mass (Da):80,967
    Last modified:October 3, 2003 - v2
    Checksum:iC848DD3FAB420833
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti58 – 581G → D in AAB41892. (PubMed:9705298)Curated
    Sequence conflicti246 – 2461P → A in AAB41892. (PubMed:9705298)Curated
    Sequence conflicti251 – 2511E → G in AAB41892. (PubMed:9705298)Curated
    Sequence conflicti254 – 2541E → K in AAB41892. (PubMed:9705298)Curated
    Sequence conflicti398 – 3981I → V in AAB41892. (PubMed:9705298)Curated
    Sequence conflicti435 – 4351A → V in AAB41892. (PubMed:9705298)Curated
    Sequence conflicti480 – 4823YNV → FSM in AAB41892. (PubMed:9705298)Curated
    Sequence conflicti510 – 5101N → D AA sequence (PubMed:9705298)Curated
    Sequence conflicti512 – 5121S → Y AA sequence (PubMed:9705298)Curated
    Sequence conflicti515 – 5151S → P AA sequence (PubMed:9705298)Curated
    Sequence conflicti560 – 5601K → N in AAB41892. (PubMed:9705298)Curated
    Sequence conflicti582 – 5821K → E in AAB41892. (PubMed:9705298)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U85038 Genomic DNA. Translation: AAB41892.1.
    AF007124 Genomic DNA. Translation: AAC26371.1.
    AE015924 Genomic DNA. Translation: AAQ65700.1.
    RefSeqiNP_904801.1. NC_002950.2.
    WP_010956050.1. NC_002950.2.

    Genome annotation databases

    EnsemblBacteriaiAAQ65700; AAQ65700; PG_0506.
    GeneIDi2552233.
    KEGGipgi:PG0506.
    PATRICi22978106. VBIPorGin134034_0464.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U85038 Genomic DNA. Translation: AAB41892.1 .
    AF007124 Genomic DNA. Translation: AAC26371.1 .
    AE015924 Genomic DNA. Translation: AAQ65700.1 .
    RefSeqi NP_904801.1. NC_002950.2.
    WP_010956050.1. NC_002950.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CVR X-ray 2.00 A 230-664 [» ]
    4IEF X-ray 2.30 A/C/E/G 25-229 [» ]
    B/D/F/H 230-662 [» ]
    ProteinModelPortali P95493.
    SMRi P95493. Positions 230-661.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P95493. 1 interaction.
    MINTi MINT-8415911.
    STRINGi 242619.PG0506.

    Protein family/group databases

    MEROPSi C25.003.

    Proteomic databases

    PRIDEi P95493.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAQ65700 ; AAQ65700 ; PG_0506 .
    GeneIDi 2552233.
    KEGGi pgi:PG0506.
    PATRICi 22978106. VBIPorGin134034_0464.

    Phylogenomic databases

    eggNOGi NOG12793.
    KOi K08589.
    OMAi KENGRMI.
    OrthoDBi EOG6BGNW2.

    Enzyme and pathway databases

    BioCyci PGIN242619:GHX8-458-MONOMER.
    BRENDAi 3.4.22.37. 4997.
    SABIO-RK P95493.

    Miscellaneous databases

    EvolutionaryTracei P95493.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.40.50.10390. 1 hit.
    3.40.50.1460. 1 hit.
    InterProi IPR029030. Caspase-like_dom.
    IPR001769. Gingipain.
    IPR029031. Gingipain_N.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR005536. Peptidase_C25_Ig-like_domain.
    IPR012600. Propeptide_C25.
    IPR026444. Secre_tail.
    [Graphical view ]
    Pfami PF01364. Peptidase_C25. 1 hit.
    PF03785. Peptidase_C25_C. 1 hit.
    PF08126. Propeptide_C25. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81296. SSF81296. 1 hit.
    TIGRFAMsi TIGR04183. Por_Secre_tail. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Comparative properties of two cysteine proteinases (gingipains R), the products of two related but individual genes of Porphyromonas gingivalis."
      Potempa J., Mikolajczyk-Pawlinska J., Brassell D., Nelson D., Thoegersen I.B., Enghild J.J., Travis J.
      J. Biol. Chem. 273:21648-21657(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 230-651.
      Strain: HG66.
    2. "Characterization of a second cell-associated Arg-specific cysteine proteinase of Porphyromonas gingivalis and identification of an adhesin-binding motif involved in association of the prtR and prtK proteinases and adhesins into large complexes."
      Slakeski N., Bhogal P.S., O'Brien-Simpson N.M., Reynolds E.C.
      Microbiology 144:1583-1592(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 53978 / W50.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-308 / W83.
    4. "Salivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontal disease."
      Gusman H., Travis J., Helmerhorst E.J., Potempa J., Troxler R.F., Oppenheim F.G.
      Infect. Immun. 69:1402-1408(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    5. "Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold."
      Eichinger A., Beisel H.-G., Jacob U., Huber R., Medrano F.-J., Banbula A., Potempa J., Travis J., Bode W.
      EMBO J. 18:5453-5462(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).

    Entry informationi

    Entry nameiCPG2_PORGI
    AccessioniPrimary (citable) accession number: P95493
    Secondary accession number(s): O33441
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: October 3, 2003
    Last modified: October 1, 2014
    This is version 114 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3