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Q51817 (KGP83_PORGN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Lys-gingipain catalytic subunit
  2. 39 kDa adhesin
    Alternative name(s):
    PrtK39
  3. 15 kDa adhesin
    Alternative name(s):
    PrtK15
  4. 44 kDa adhesin
    Alternative name(s):
    PrtK44
Gene names
Name:kgp
Synonyms:prtK, prtP
OrganismPorphyromonas gingivalis
Taxonomic identifier837 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas

Protein attributes

Sequence length1732 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. UniProtKB B2RLK2

Catalytic activity

Endopeptidase with strict specificity for lysyl bonds. UniProtKB B2RLK2

Subcellular location

Lys-gingipain catalytic subunit: Secretedextracellular space By similarity UniProtKB P72194.

Post-translational modification

Proteolytically cleaved into a catalytic subunit and three adhesins. Arg-gingipain is involved in this post-translational processing. Ref.3 UniProtKB P72194

Polymorphism

Several forms of kgp with differences at the C-terminus exist in different P.gingivalis strains. Ref.5

Sequence similarities

Belongs to the peptidase C25 family.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMZymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 228204 Ref.4
PRO_0000395381
Chain229 – 17321504Lys-gingipain W83 Ref.4
PRO_0000395382
Chain229 – ?Lys-gingipain catalytic subunit Ref.4PRO_0000395383
Chain738 – ?39 kDa adhesin Ref.4PRO_0000395384
Chain1157 – ?15 kDa adhesin Ref.4PRO_0000395385
Chain1292 – ?44 kDa adhesin Ref.4PRO_0000395386

Sites

Active site4441Proton donor By similarity UniProtKB P95493
Active site4771Nucleophile By similarity UniProtKB P95493

Experimental info

Sequence conflict7961V → I in AAB60809. Ref.3
Sequence conflict13511K → N in AAC26523. Ref.2
Sequence conflict13641D → Y in AAC26523. Ref.2
Sequence conflict13901D → N in AAB60809. Ref.3
Sequence conflict14481D → H in AAC26523. Ref.2
Sequence conflict14791H → Y in AAB60809. Ref.3

Secondary structure

...................................................... 1732
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q51817 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 654271DBEF7BCAE4

FASTA1,732187,875
        10         20         30         40         50         60 
MRKLLLLIAA SLLGVGLYAQ SAKIKLDAPT TRTTCTNNSF KQFDASFSFN EVELTKVETK 

        70         80         90        100        110        120 
GGTFASVSIP GAFPTGEVGS PEVPAVRKLI AVPVGATPVV RVKSFTEQVY SLNQYGSEKL 

       130        140        150        160        170        180 
MPHQPSMSKS DDPEKVPFVY NAAAYARKGF VGQELTQVEM LGTMRGVRIA ALTINPVQYD 

       190        200        210        220        230        240 
VVANQLKVRN NIEIEVSFQG ADEVATQRLY DASFSPYFET AYKQLFNRDV YTDHGDLYNT 

       250        260        270        280        290        300 
PVRMLVVAGA KFKEALKPWL TWKAQKGFYL DVHYTDEAEV GTTNASIKAF IHKKYNDGLA 

       310        320        330        340        350        360 
ASAAPVFLAL VGDTDVISGE KGKKTKKVTD LYYSAVDGDY FPEMYTFRMS ASSPEELTNI 

       370        380        390        400        410        420 
IDKVLMYEKA TMPDKSYLEK VLLIAGADYS WNSQVGQPTI KYGMQYYYNQ EHGYTDVYNY 

       430        440        450        460        470        480 
LKAPYTGCYS HLNTGVSFAN YTAHGSETAW ADPLLTTSQL KALTNKDKYF LAIGNCCITA 

       490        500        510        520        530        540 
QFDYVQPCFG EVITRVKEKG AYAYIGSSPN SYWGEDYYWS VGANAVFGVQ PTFEGTSMGS 

       550        560        570        580        590        600 
YDATFLEDSY NTVNSIMWAG NLAATHAGNI GNITHIGAHY YWEAYHVLGD GSVMPYRAMP 

       610        620        630        640        650        660 
KTNTYTLPAS LPQNQASYSI QASAGSYVAI SKDGVLYGTG VANASGVATV SMTKQITENG 

       670        680        690        700        710        720 
NYDVVITRSN YLPVIKQIQV GEPSPYQPVS NLTATTQGQK VTLKWEAPSA KKAEGSREVK 

       730        740        750        760        770        780 
RIGDGLFVTI EPANDVRANE AKVVLAADNV WGDNTGYQFL LDADHNTFGS VIPATGPLFT 

       790        800        810        820        830        840 
GTASSNLYSA NFEYLVPANA DPVVTTQNII VTGQGEVVIP GGVYDYCITN PEPASGKMWI 

       850        860        870        880        890        900 
AGDGGNQPAR YDDFTFEAGK KYTFTMRRAG MGDGTDMEVE DDSPASYTYT VYRDGTKIKE 

       910        920        930        940        950        960 
GLTATTFEED GVAAGNHEYC VEVKYTAGVS PKVCKDVTVE GSNEFAPVQN LTGSSVGQKV 

       970        980        990       1000       1010       1020 
TLKWDAPNGT PNPNPNPNPN PGTTLSESFE NGIPASWKTI DADGDGHGWK PGNAPGIAGY 

      1030       1040       1050       1060       1070       1080 
NSNGCVYSES FGLGGIGVLT PDNYLITPAL DLPNGGKLTF WVCAQDANYA SEHYAVYASS 

      1090       1100       1110       1120       1130       1140 
TGNDASNFTN ALLEETITAK GVRSPKAIRG RIQGTWRQKT VDLPAGTKYV AFRHFQSTDM 

      1150       1160       1170       1180       1190       1200 
FYIDLDEVEI KANGKRADFT ETFESSTHGE APAEWTTIDA DGDGQGWLCL SSGQLDWLTA 

      1210       1220       1230       1240       1250       1260 
HGGSNVVSSF SWNGMALNPD NYLISKDVTG ATKVKYYYAV NDGFPGDHYA VMISKTGTNA 

      1270       1280       1290       1300       1310       1320 
GDFTVVFEET PNGINKGGAR FGLSTEANGA KPQSVWIERT VDLPAGTKYV AFRHYNCSDL 

      1330       1340       1350       1360       1370       1380 
NYILLDDIQF TMGGSPTPTD YTYTVYRDGT KIKEGLTETT FEEDGVATGN HEYCVEVKYT 

      1390       1400       1410       1420       1430       1440 
AGVSPKKCVD VTVNSTQFNP VQNLTAEQAP NSMDAILKWN APASKRAEVL NEDFENGIPA 

      1450       1460       1470       1480       1490       1500 
SWKTIDADGD GNNWTTTPPP GGSSFAGHNS AICVSSASHI NFEGPQNPDN YLVTPELSLP 

      1510       1520       1530       1540       1550       1560 
GGGTLTFWVC AQDANYASEH YAVYASSTGN DASNFANALL EEVLTAKTVV TAPEAIRGTR 

      1570       1580       1590       1600       1610       1620 
AQGTWYQKTV QLPAGTKYVA FRHFGCTDFF WINLDDVVIT SGNAPSYTYT IYRNNTQIAS 

      1630       1640       1650       1660       1670       1680 
GVTETTYRDP DLATGFYTYG VKVVYPNGES AIETATLNIT SLADVTAQKP YTLTVVGKTI 

      1690       1700       1710       1720       1730 
TVTCQGEAMI YDMNGRRLAA GRNTVVYTAQ GGHYAVMVVV DGKSYVEKLA VK 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U42210 Genomic DNA. Translation: AAB06565.1.
AF017059 Genomic DNA. Translation: AAC26523.1.
U75366 Genomic DNA. Translation: AAB60809.1.
PIRT30836.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3M1HX-ray1.56A/B/C/D1427-1602[»]
4ITCX-ray1.55A982-1154[»]
ProteinModelPortalQ51817.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC25.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.10390. 1 hit.
3.40.50.1460. 1 hit.
InterProIPR029030. 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]
PfamPF07675. 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]
SMARTSM00060. FN3. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKGP83_PORGN
AccessionPrimary (citable) accession number: Q51817
Secondary accession number(s): O07442, O52050
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references