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Q51817

- KGP83_PORGN

UniProt

Q51817 - KGP83_PORGN

Protein

Lys-gingipain W83

Gene

kgp

Organism
Porphyromonas gingivalis
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria By similarity.By similarity

    Catalytic activityi

    Endopeptidase with strict specificity for lysyl bonds.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei444 – 4441Proton donorBy similarity
    Active sitei477 – 4771NucleophileBy similarity

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. pathogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Virulence

    Protein family/group databases

    MEROPSiC25.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lys-gingipain W83By similarity1 Publication (EC:3.4.22.47)
    Alternative name(s):
    Lysine specific cysteine proteaseImported1 Publication
    Lysine-specific cysteine proteinaseImported1 Publication
    PorphypainImported1 Publication
    PrtK481 Publication
    Cleaved into the following 4 chains:
    Lys-gingipain catalytic subunitBy similarity1 Publication
    39 kDa adhesin1 Publication
    Alternative name(s):
    PrtK391 Publication
    15 kDa adhesin1 Publication
    Alternative name(s):
    PrtK151 Publication
    44 kDa adhesin1 Publication
    Alternative name(s):
    PrtK441 Publication
    Gene namesi
    Name:kgpBy similarity
    Synonyms:prtKImported, prtPImported1 Publication
    OrganismiPorphyromonas gingivalis
    Taxonomic identifieri837 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas

    Subcellular locationi

    Chain Lys-gingipain catalytic subunit : Secretedextracellular space By similarity

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Propeptidei25 – 2282041 PublicationSequence AnalysisPRO_0000395381Add
    BLAST
    Chaini229 – 17321504Lys-gingipain W831 PublicationPRO_0000395382Add
    BLAST
    Chaini229 – ?Lys-gingipain catalytic subunit1 PublicationPRO_0000395383
    Chaini738 – ?39 kDa adhesin1 PublicationPRO_0000395384
    Chaini1157 – ?15 kDa adhesin1 PublicationPRO_0000395385
    Chaini1292 – ?44 kDa adhesin1 PublicationPRO_0000395386

    Post-translational modificationi

    Proteolytically cleaved into a catalytic subunit and three adhesins. Arg-gingipain is involved in this post-translational processing.By similarity1 Publication

    Keywords - PTMi

    Zymogen

    Structurei

    Secondary structure

    1
    1732
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi984 – 9874
    Beta strandi997 – 10015
    Beta strandi1010 – 10134
    Turni1014 – 10163
    Beta strandi1022 – 103211
    Turni1033 – 10364
    Beta strandi1043 – 10464
    Beta strandi1056 – 106611
    Beta strandi1073 – 10819
    Helixi1085 – 10873
    Beta strandi1090 – 10967
    Beta strandi1117 – 11237
    Beta strandi1129 – 11346
    Beta strandi1142 – 115211
    Beta strandi1428 – 14325
    Beta strandi1442 – 14487
    Beta strandi1454 – 14574
    Turni1459 – 14624
    Beta strandi1474 – 14807
    Turni1481 – 14833
    Beta strandi1489 – 14935
    Beta strandi1503 – 151311
    Beta strandi1520 – 15289
    Helixi1532 – 15343
    Beta strandi1539 – 15435
    Beta strandi1566 – 15727
    Beta strandi1578 – 15858
    Beta strandi1591 – 160111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3M1HX-ray1.56A/B/C/D1427-1602[»]
    4ITCX-ray1.55A982-1154[»]
    ProteinModelPortaliQ51817.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C25 family.Sequence Analysis

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.50.10390. 1 hit.
    3.40.50.1460. 1 hit.
    InterProiIPR029030. Caspase-like_dom.
    IPR011628. Cleaved_adhesin.
    IPR003961. Fibronectin_type3.
    IPR001769. Gingipain.
    IPR029031. Gingipain_N.
    IPR018832. Pept_C25_gingipain_C.
    IPR005536. Peptidase_C25_Ig-like_domain.
    IPR012600. Propeptide_C25.
    [Graphical view]
    PfamiPF07675. Cleaved_Adhesin. 3 hits.
    PF10365. DUF2436. 1 hit.
    PF01364. Peptidase_C25. 1 hit.
    PF03785. Peptidase_C25_C. 1 hit.
    PF08126. Propeptide_C25. 1 hit.
    [Graphical view]
    SMARTiSM00060. FN3. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q51817-1 [UniParc]FASTAAdd to Basket

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    MRKLLLLIAA SLLGVGLYAQ SAKIKLDAPT TRTTCTNNSF KQFDASFSFN     50
    EVELTKVETK GGTFASVSIP GAFPTGEVGS PEVPAVRKLI AVPVGATPVV 100
    RVKSFTEQVY SLNQYGSEKL MPHQPSMSKS DDPEKVPFVY NAAAYARKGF 150
    VGQELTQVEM LGTMRGVRIA ALTINPVQYD VVANQLKVRN NIEIEVSFQG 200
    ADEVATQRLY DASFSPYFET AYKQLFNRDV YTDHGDLYNT PVRMLVVAGA 250
    KFKEALKPWL TWKAQKGFYL DVHYTDEAEV GTTNASIKAF IHKKYNDGLA 300
    ASAAPVFLAL VGDTDVISGE KGKKTKKVTD LYYSAVDGDY FPEMYTFRMS 350
    ASSPEELTNI IDKVLMYEKA TMPDKSYLEK VLLIAGADYS WNSQVGQPTI 400
    KYGMQYYYNQ EHGYTDVYNY LKAPYTGCYS HLNTGVSFAN YTAHGSETAW 450
    ADPLLTTSQL KALTNKDKYF LAIGNCCITA QFDYVQPCFG EVITRVKEKG 500
    AYAYIGSSPN SYWGEDYYWS VGANAVFGVQ PTFEGTSMGS YDATFLEDSY 550
    NTVNSIMWAG NLAATHAGNI GNITHIGAHY YWEAYHVLGD GSVMPYRAMP 600
    KTNTYTLPAS LPQNQASYSI QASAGSYVAI SKDGVLYGTG VANASGVATV 650
    SMTKQITENG NYDVVITRSN YLPVIKQIQV GEPSPYQPVS NLTATTQGQK 700
    VTLKWEAPSA KKAEGSREVK RIGDGLFVTI EPANDVRANE AKVVLAADNV 750
    WGDNTGYQFL LDADHNTFGS VIPATGPLFT GTASSNLYSA NFEYLVPANA 800
    DPVVTTQNII VTGQGEVVIP GGVYDYCITN PEPASGKMWI AGDGGNQPAR 850
    YDDFTFEAGK KYTFTMRRAG MGDGTDMEVE DDSPASYTYT VYRDGTKIKE 900
    GLTATTFEED GVAAGNHEYC VEVKYTAGVS PKVCKDVTVE GSNEFAPVQN 950
    LTGSSVGQKV TLKWDAPNGT PNPNPNPNPN PGTTLSESFE NGIPASWKTI 1000
    DADGDGHGWK PGNAPGIAGY NSNGCVYSES FGLGGIGVLT PDNYLITPAL 1050
    DLPNGGKLTF WVCAQDANYA SEHYAVYASS TGNDASNFTN ALLEETITAK 1100
    GVRSPKAIRG RIQGTWRQKT VDLPAGTKYV AFRHFQSTDM FYIDLDEVEI 1150
    KANGKRADFT ETFESSTHGE APAEWTTIDA DGDGQGWLCL SSGQLDWLTA 1200
    HGGSNVVSSF SWNGMALNPD NYLISKDVTG ATKVKYYYAV NDGFPGDHYA 1250
    VMISKTGTNA GDFTVVFEET PNGINKGGAR FGLSTEANGA KPQSVWIERT 1300
    VDLPAGTKYV AFRHYNCSDL NYILLDDIQF TMGGSPTPTD YTYTVYRDGT 1350
    KIKEGLTETT FEEDGVATGN HEYCVEVKYT AGVSPKKCVD VTVNSTQFNP 1400
    VQNLTAEQAP NSMDAILKWN APASKRAEVL NEDFENGIPA SWKTIDADGD 1450
    GNNWTTTPPP GGSSFAGHNS AICVSSASHI NFEGPQNPDN YLVTPELSLP 1500
    GGGTLTFWVC AQDANYASEH YAVYASSTGN DASNFANALL EEVLTAKTVV 1550
    TAPEAIRGTR AQGTWYQKTV QLPAGTKYVA FRHFGCTDFF WINLDDVVIT 1600
    SGNAPSYTYT IYRNNTQIAS GVTETTYRDP DLATGFYTYG VKVVYPNGES 1650
    AIETATLNIT SLADVTAQKP YTLTVVGKTI TVTCQGEAMI YDMNGRRLAA 1700
    GRNTVVYTAQ GGHYAVMVVV DGKSYVEKLA VK 1732
    Length:1,732
    Mass (Da):187,875
    Last modified:November 1, 1996 - v1
    Checksum:i654271DBEF7BCAE4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti796 – 7961V → I in AAB60809. (PubMed:10219167)Curated
    Sequence conflicti1351 – 13511K → N in AAC26523. (PubMed:9632563)Curated
    Sequence conflicti1364 – 13641D → Y in AAC26523. (PubMed:9632563)Curated
    Sequence conflicti1390 – 13901D → N in AAB60809. (PubMed:10219167)Curated
    Sequence conflicti1448 – 14481D → H in AAC26523. (PubMed:9632563)Curated
    Sequence conflicti1479 – 14791H → Y in AAB60809. (PubMed:10219167)Curated

    Polymorphismi

    Several forms of kgp with differences at the C-terminus exist in different P.gingivalis strains.1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U42210 Genomic DNA. Translation: AAB06565.1.
    AF017059 Genomic DNA. Translation: AAC26523.1.
    U75366 Genomic DNA. Translation: AAB60809.1.
    PIRiT30836.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U42210 Genomic DNA. Translation: AAB06565.1 .
    AF017059 Genomic DNA. Translation: AAC26523.1 .
    U75366 Genomic DNA. Translation: AAB60809.1 .
    PIRi T30836.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3M1H X-ray 1.56 A/B/C/D 1427-1602 [» ]
    4ITC X-ray 1.55 A 982-1154 [» ]
    ProteinModelPortali Q51817.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C25.002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.10390. 1 hit.
    3.40.50.1460. 1 hit.
    InterProi IPR029030. Caspase-like_dom.
    IPR011628. Cleaved_adhesin.
    IPR003961. Fibronectin_type3.
    IPR001769. Gingipain.
    IPR029031. Gingipain_N.
    IPR018832. Pept_C25_gingipain_C.
    IPR005536. Peptidase_C25_Ig-like_domain.
    IPR012600. Propeptide_C25.
    [Graphical view ]
    Pfami PF07675. Cleaved_Adhesin. 3 hits.
    PF10365. DUF2436. 1 hit.
    PF01364. Peptidase_C25. 1 hit.
    PF03785. Peptidase_C25_C. 1 hit.
    PF08126. Propeptide_C25. 1 hit.
    [Graphical view ]
    SMARTi SM00060. FN3. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of the prtP gene encoding porphypain, a cysteine proteinase of Porphyromonas gingivalis."
      Barkocy-Gallagher G.A., Han N., Patti J.M., Whitlock J., Progulske-Fox A., Lantz M.S.
      J. Bacteriol. 178:2734-2741(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 328-343; 738-750; 851-861; 1281-1287; 1292-1299 AND 1561-1568.
      Strain: W12Imported.
    2. "IS195, an insertion sequence-like element associated with protease genes in Porphyromonas gingivalis."
      Lewis J.P., Macrina F.L.
      Infect. Immun. 66:3035-3042(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC BAA-308 / W83Imported.
    3. "Characterization of a Porphyromonas gingivalis gene prtK that encodes a lysine-specific cysteine proteinase and three sequence-related adhesins."
      Slakeski N., Cleal S.M., Bhogal P.S., Reynolds E.C.
      Oral Microbiol. Immunol. 14:92-97(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], POST-TRANSLATIONAL PROCESSING.
      Strain: ATCC 53978 / W50Imported.
    4. "A cell-associated protein complex of Porphyromonas gingivalis W50 composed of Arg- and Lys-specific cysteine proteinases and adhesins."
      Bhogal P.S., Slakeski N., Reynolds E.C.
      Microbiology 143:2485-2495(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 229-245; 738-763; 1157-1180 AND 1292-1313.
      Strain: ATCC 53978 / W501 Publication.
    5. "Distribution of Porphyromonas gingivalis biotypes defined by alleles of the kgp (Lys-gingipain) gene."
      Nadkarni M.A., Nguyen K.A., Chapple C.C., DeCarlo A.A., Jacques N.A., Hunter N.
      J. Clin. Microbiol. 42:3873-3876(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYMORPHISM.

    Entry informationi

    Entry nameiKGP83_PORGN
    AccessioniPrimary (citable) accession number: Q51817
    Secondary accession number(s): O07442, O52050
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 13, 2010
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 61 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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