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P72197 (KGP66_PORGN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Lys-gingipain HG66
EC=3.4.22.47

Cleaved into the following 4 chains:

  1. Lys-gingipain catalytic subunit
  2. 39 kDa adhesin
  3. 15 kDa adhesin
  4. 44 kDa adhesin
Gene names
Name:kgp
OrganismPorphyromonas gingivalis
Taxonomic identifier837 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Porphyromonadaceae › Porphyromonas

Protein attributes

Sequence length1723 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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: Secreted › extracellular 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 By similarity. UniProtKB P72194 UniProtKB Q51817

Polymorphism

Several forms of kgp with differences at the C-terminus exist in different P.gingivalis strains. Ref.2

Sequence similarities

Belongs to the peptidase C25 family.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMZymogen
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

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 By similarity UniProtKB Q51817
PRO_0000395375
Chain229 – 17231495Lys-gingipain HG66 By similarity UniProtKB Q51817
PRO_0000395376
Chain229 – ?Lys-gingipain catalytic subunit By similarity UniProtKB Q51817PRO_0000395377
Chain738 – ?39 kDa adhesin By similarity UniProtKB Q51817PRO_0000395378
Chain1156 – ?15 kDa adhesin By similarity UniProtKB Q51817PRO_0000395379
Chain1291 – ?44 kDa adhesin By similarity UniProtKB Q51817PRO_0000395380

Sites

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

Sequences

Sequence LengthMass (Da)Tools
P72197 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 4508A7E50197CEBD

FASTA1,723186,832
        10         20         30         40         50         60 
MRKLLLLIAA SLLGVGLYAQ NAKIKLDAPT TRTTCTNNSF KQFDASFSFN EVELTKVETK 

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

       130        140        150        160        170        180 
MPHQPSMSKS DDPEKVPFAY 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 ALLIAGADSY WNPKIGQQTI KYAVQYYYNQ DHGYTDVYSY 

       430        440        450        460        470        480 
PKAPYTGCYS HLNTGVGFAN YTAHGSETSW ADPSVTATQV KALTNKNKYF LAIGNCCVTA 

       490        500        510        520        530        540 
QFDYPQPCFG EVMTRVKEKG AYAYIGSSPN SYWGEDYYWS VGANAVFGVQ PTFEGTSMGS 

       550        560        570        580        590        600 
YDATFLEDSY NTVNSIMWAG NLAATHAENI GNVTHIGAHY YWEAYHVLGD GSVMPYRAMP 

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

       670        680        690        700        710        720 
NYDVVITRSN YLPVIKQIQA GEPSPYQPVS NLTATTQGQK VTLKWDAPSA KKAEGSREVK 

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

       790        800        810        820        830        840 
GTASSNLYSA NFEYLIPANA 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 LTGSAVGQKV 

       970        980        990       1000       1010       1020 
TLKWDAPNGT PNPNPNPNPG TTTLSESFEN GIPASWKTID ADGDGHGWKP GNAPGIAGYN 

      1030       1040       1050       1060       1070       1080 
SNGCVYSESF GLGGIGVLTP DNYLITPALD LPNGGKLTFW VCAQDANYAS EHYAVYASST 

      1090       1100       1110       1120       1130       1140 
GNDASNFTNA LLEETITAKG VRSPEAIRGR IQGTWRQKTV DLPAGTKYVA FRHFQSTDMF 

      1150       1160       1170       1180       1190       1200 
YIDLDEVEIK ANGKRADFTE TFESSTHGEA PAEWTTIDAD GDGQGWLCLS SGQLDWLTAH 

      1210       1220       1230       1240       1250       1260 
GGTNVVASFS WNGMALNPDN YLISKDVTGA TKVKYYYAVN DGFPGDHYAV MISKTGTNAG 

      1270       1280       1290       1300       1310       1320 
DFTVVFEETP NGINKGGARF GLSTEADGAK PQSVWIERTV DLPAGTKYVA FRHYNCSDLN 

      1330       1340       1350       1360       1370       1380 
YILLDDIQFT MGGSPTPTDY TYTVYRDGTK IKEGLTETTF EEDGVATGNH EYCVEVKYTA 

      1390       1400       1410       1420       1430       1440 
GVSPKKCVNV TINPTQFNPV KNLKAQPDGG DVVLKWEAPS AKKAEGSREV KRIGDGLFVT 

      1450       1460       1470       1480       1490       1500 
IEPANDVRAN EAKVVLAADN VWGDNTGYQF LLDADHNTFG SVIPATGPLF TGTASSNLYS 

      1510       1520       1530       1540       1550       1560 
ANFEYLIPAN ADPVVTTQNI IVTGQGEVVI PGGVYDYCIT NPEPASGKMW IAGDGGNQPA 

      1570       1580       1590       1600       1610       1620 
RYDDFTFEAG KKYTFTMRRA GMGDGTDMEV EDDSPASYTY TVYRDGTKIK EGLTETTYRD 

      1630       1640       1650       1660       1670       1680 
AGMSAQSHEY CVEVKYAAGV SPKVCVDYIP DGVADVTAQK PYTLTVVGKT ITVTCQGEAM 

      1690       1700       1710       1720 
IYDMNGRRLA AGRNTVVYTA QGGYYAVMVV VDGKSYVEKL AVK

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References

[1]"Molecular cloning and characterization of Porphyromonas gingivalis lysine-specific gingipain. A new member of an emerging family of pathogenic bacterial cysteine proteinases."
Pavloff N., Pemberton P.A., Potempa J., Chen W.C., Pike R.N., Prochazka V., Kiefer M.C., Travis J., Barr P.J.
J. Biol. Chem. 272:1595-1600(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: HG66.
[2]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U54691 Genomic DNA. Translation: AAA99810.1.

3D structure databases

ProteinModelPortalP72197.
ModBaseSearch...

Protein family/group databases

MEROPSC25.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.4.22.47. 4997.

Family and domain databases

InterProIPR011628. Cleaved_adhesin.
IPR018832. Pept_C25_gingipain_C.
IPR001769. Peptidase_C25.
IPR005536. Peptidase_C25_Ig-like_domain.
IPR012600. Propeptide_C25.
[Graphical view]
PfamPF07675. Cleaved_Adhesin. 2 hits.
PF10365. DUF2436. 2 hits.
PF01364. Peptidase_C25. 1 hit.
PF03785. Peptidase_C25_C. 1 hit.
PF08126. Propeptide_C25. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL5664.

Entry information

Entry nameKGP66_PORGN
AccessionPrimary (citable) accession number: P72197
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: February 1, 1997
Last modified: March 6, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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