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Q51817

- KGP83_PORGN

UniProt

Q51817 - KGP83_PORGN

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Protein

Lys-gingipain W83

Gene
kgp, prtK, prtP
Organism
Porphyromonas gingivalis
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 donor By similarityBy similarity
Active sitei477 – 4771Nucleophile By similarityBy similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
Complete GO annotation...

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 W83 (EC:3.4.22.47)
Alternative name(s):
Lysine specific cysteine protease
Lysine-specific cysteine proteinase
Porphypain
PrtK48
Cleaved into the following 4 chains:
Alternative name(s):
PrtK39
Alternative name(s):
PrtK15
Alternative name(s):
PrtK44
Gene namesi
Name:kgp
Synonyms:prtK, prtP
OrganismiPorphyromonas gingivalis
Taxonomic identifieri837 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas

Subcellular locationi

Chain Lys-gingipain catalytic subunit : Secretedextracellular space By similarity By similarity

GO - Cellular componenti

  1. extracellular space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424 Reviewed predictionAdd
BLAST
Propeptidei25 – 2282041 PublicationPRO_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.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C25 family.

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

Polymorphismi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti796 – 7961V → I in AAB60809. 1 Publication
Sequence conflicti1351 – 13511K → N in AAC26523. 1 Publication
Sequence conflicti1364 – 13641D → Y in AAC26523. 1 Publication
Sequence conflicti1390 – 13901D → N in AAB60809. 1 Publication
Sequence conflicti1448 – 14481D → H in AAC26523. 1 Publication
Sequence conflicti1479 – 14791H → Y in AAB60809. 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: W12.
  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 / W83.
  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 / W50.
  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 / W50.
  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: June 11, 2014
This is version 60 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

Similar proteinsi