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Database: UniProt
Entry: P72197
LinkDB: P72197
Original site: P72197 
ID   KGP66_PORGN             Reviewed;        1723 AA.
AC   P72197;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   10-MAY-2017, entry version 67.
DE   RecName: Full=Lys-gingipain HG66 {ECO:0000303|PubMed:15297553, ECO:0000303|PubMed:8999833, ECO:0000312|EMBL:AAA99810.1};
DE            EC=3.4.22.47 {ECO:0000269|PubMed:8999833};
DE   Contains:
DE     RecName: Full=Lys-gingipain catalytic subunit {ECO:0000250|UniProtKB:B2RLK2, ECO:0000250|UniProtKB:Q51817};
DE   Contains:
DE     RecName: Full=39 kDa adhesin {ECO:0000250|UniProtKB:Q51817};
DE   Contains:
DE     RecName: Full=15 kDa adhesin {ECO:0000250|UniProtKB:Q51817};
DE   Contains:
DE     RecName: Full=44 kDa adhesin {ECO:0000250|UniProtKB:Q51817};
DE   Flags: Precursor;
GN   Name=kgp {ECO:0000312|EMBL:AAA99810.1};
OS   Porphyromonas gingivalis.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Porphyromonadaceae; Porphyromonas.
OX   NCBI_TaxID=837;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAA99810.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=HG66 {ECO:0000269|PubMed:8999833};
RX   PubMed=8999833; DOI=10.1074/jbc.272.3.1595;
RA   Pavloff N., Pemberton P.A., Potempa J., Chen W.C., Pike R.N.,
RA   Prochazka V., Kiefer M.C., Travis J., Barr P.J.;
RT   "Molecular cloning and characterization of Porphyromonas gingivalis
RT   lysine-specific gingipain. A new member of an emerging family of
RT   pathogenic bacterial cysteine proteinases.";
RL   J. Biol. Chem. 272:1595-1600(1997).
RN   [2] {ECO:0000305}
RP   POLYMORPHISM.
RX   PubMed=15297553; DOI=10.1128/JCM.42.8.3873-3876.2004;
RA   Nadkarni M.A., Nguyen K.A., Chapple C.C., DeCarlo A.A., Jacques N.A.,
RA   Hunter N.;
RT   "Distribution of Porphyromonas gingivalis biotypes defined by alleles
RT   of the kgp (Lys-gingipain) gene.";
RL   J. Clin. Microbiol. 42:3873-3876(2004).
CC   -!- FUNCTION: Cysteine proteinase with a strong preference for
CC       substrates with Lys in the P1 position (PubMed:8999833).
CC       Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human
CC       placental type I collagen and human IgA and IgG. Disrupts the
CC       functions of polymorphonuclear leukocytes. May act as a virulence
CC       factor in the development of peridontal disease. Involved in the
CC       coaggregation of P.gingivalis with other oral bacteria (By
CC       similarity). {ECO:0000250|UniProtKB:B2RLK2,
CC       ECO:0000269|PubMed:8999833}.
CC   -!- CATALYTIC ACTIVITY: Endopeptidase with strict specificity for
CC       lysyl bonds. {ECO:0000269|PubMed:8999833}.
CC   -!- SUBCELLULAR LOCATION: Lys-gingipain catalytic subunit: Secreted,
CC       extracellular space {ECO:0000269|PubMed:8999833}.
CC   -!- PTM: Proteolytically cleaved into a catalytic subunit and three
CC       adhesins. Arg-gingipain is involved in this post-translational
CC       processing (By similarity). {ECO:0000250|UniProtKB:P72194,
CC       ECO:0000250|UniProtKB:Q51817}.
CC   -!- POLYMORPHISM: Several forms of kgp with differences at the C-
CC       terminus exist in different P.gingivalis strains.
CC       {ECO:0000269|PubMed:15297553}.
CC   -!- SIMILARITY: Belongs to the peptidase C25 family. {ECO:0000255}.
DR   EMBL; U54691; AAA99810.1; -; Genomic_DNA.
DR   ProteinModelPortal; P72197; -.
DR   SMR; P72197; -.
DR   ChEMBL; CHEMBL5664; -.
DR   PRIDE; P72197; -.
DR   BRENDA; 3.4.22.47; 756.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0044179; P:hemolysis in other organism; ISS:UniProtKB.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.40.10; -; 4.
DR   Gene3D; 3.40.50.10390; -; 1.
DR   InterPro; IPR029030; Caspase-like_dom.
DR   InterPro; IPR011628; Cleaved_adhesin.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR001769; Gingipain.
DR   InterPro; IPR029031; Gingipain_N.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR018832; Pept_C25_gingipain_C.
DR   InterPro; IPR005536; Peptidase_C25_Ig-like_domain.
DR   InterPro; IPR012600; Propeptide_C25.
DR   Pfam; PF07675; Cleaved_Adhesin; 2.
DR   Pfam; PF10365; DUF2436; 2.
DR   Pfam; PF01364; Peptidase_C25; 1.
DR   Pfam; PF03785; Peptidase_C25_C; 1.
DR   Pfam; PF08126; Propeptide_C25; 1.
DR   SUPFAM; SSF52129; SSF52129; 1.
PE   1: Evidence at protein level;
KW   Calcium; Hydrolase; Metal-binding; Protease; Secreted; Signal;
KW   Thiol protease; Virulence; Zymogen.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   PROPEP       25    228       {ECO:0000250|UniProtKB:Q51817,
FT                                ECO:0000255}.
FT                                /FTId=PRO_0000395375.
FT   CHAIN       229   1723       Lys-gingipain HG66.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT                                /FTId=PRO_0000395376.
FT   CHAIN       229      ?       Lys-gingipain catalytic subunit.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT                                /FTId=PRO_0000395377.
FT   CHAIN       738      ?       39 kDa adhesin.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT                                /FTId=PRO_0000395378.
FT   CHAIN      1156      ?       15 kDa adhesin.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT                                /FTId=PRO_0000395379.
FT   CHAIN      1291      ?       44 kDa adhesin.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT                                /FTId=PRO_0000395380.
FT   ACT_SITE    444    444       Proton donor.
FT                                {ECO:0000250|UniProtKB:P95493}.
FT   ACT_SITE    477    477       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P95493}.
FT   METAL       313    313       Calcium 1.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL       337    337       Calcium 2.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL       339    339       Calcium 2.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL       341    341       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL       343    343       Calcium 2.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL       482    482       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL       491    491       Calcium 1.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL       987    987       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL       989    989       Calcium 3.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL      1000   1000       Calcium 4.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL      1002   1002       Calcium 4.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL      1004   1004       Calcium 4.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL      1006   1006       Calcium 4; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL      1021   1021       Calcium 3.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL      1023   1023       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL      1042   1042       Calcium 4.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL      1145   1145       Calcium 3.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   METAL      1146   1146       Calcium 3.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   SITE        228    229       Cleavage; site 1.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   SITE        737    738       Cleavage; site 2.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   SITE       1155   1156       Cleavage; site 3.
FT                                {ECO:0000250|UniProtKB:Q51817}.
FT   SITE       1290   1291       Cleavage; site 4.
FT                                {ECO:0000250|UniProtKB:Q51817}.
SQ   SEQUENCE   1723 AA;  186832 MW;  4508A7E50197CEBD CRC64;
     MRKLLLLIAA SLLGVGLYAQ NAKIKLDAPT TRTTCTNNSF KQFDASFSFN EVELTKVETK
     GGTFASVSIP GAFPTGEVGS PEVPAVRKLI AVPVGATPVV RVKSFTEQVY SLNQYGSEKL
     MPHQPSMSKS DDPEKVPFAY NAAAYARKGF VGQELTQVEM LGTMRGVRIA ALTINPVQYD
     VVANQLKVRN NIEIEVSFQG ADEVATQRLY DASFSPYFET AYKQLFNRDV YTDHGDLYNT
     PVRMLVVAGA KFKEALKPWL TWKAQKGFYL DVHYTDEAEV GTTNASIKAF IHKKYNDGLA
     ASAAPVFLAL VGDTDVISGE KGKKTKKVTD LYYSAVDGDY FPEMYTFRMS ASSPEELTNI
     IDKVLMYEKA TMPDKSYLEK ALLIAGADSY WNPKIGQQTI KYAVQYYYNQ DHGYTDVYSY
     PKAPYTGCYS HLNTGVGFAN YTAHGSETSW ADPSVTATQV KALTNKNKYF LAIGNCCVTA
     QFDYPQPCFG EVMTRVKEKG AYAYIGSSPN SYWGEDYYWS VGANAVFGVQ PTFEGTSMGS
     YDATFLEDSY NTVNSIMWAG NLAATHAENI GNVTHIGAHY YWEAYHVLGD GSVMPYRAMP
     KTNTYTLPAS LPQNQASYSI QASAGSYVAI SKDGVLYGTG VANASGVATV NMTKQITENG
     NYDVVITRSN YLPVIKQIQA GEPSPYQPVS NLTATTQGQK VTLKWDAPSA KKAEGSREVK
     RIGDGLFVTI EPANDVRANE AKVVLAADNV WGDNTGYQFL LDADHNTFGS VIPATGPLFT
     GTASSNLYSA NFEYLIPANA DPVVTTQNII VTGQGEVVIP GGVYDYCITN PEPASGKMWI
     AGDGGNQPAR YDDFTFEAGK KYTFTMRRAG MGDGTDMEVE DDSPASYTYT VYRDGTKIKE
     GLTATTFEED GVAAGNHEYC VEVKYTAGVS PKVCKDVTVE GSNEFAPVQN LTGSAVGQKV
     TLKWDAPNGT PNPNPNPNPG TTTLSESFEN GIPASWKTID ADGDGHGWKP GNAPGIAGYN
     SNGCVYSESF GLGGIGVLTP DNYLITPALD LPNGGKLTFW VCAQDANYAS EHYAVYASST
     GNDASNFTNA LLEETITAKG VRSPEAIRGR IQGTWRQKTV DLPAGTKYVA FRHFQSTDMF
     YIDLDEVEIK ANGKRADFTE TFESSTHGEA PAEWTTIDAD GDGQGWLCLS SGQLDWLTAH
     GGTNVVASFS WNGMALNPDN YLISKDVTGA TKVKYYYAVN DGFPGDHYAV MISKTGTNAG
     DFTVVFEETP NGINKGGARF GLSTEADGAK PQSVWIERTV DLPAGTKYVA FRHYNCSDLN
     YILLDDIQFT MGGSPTPTDY TYTVYRDGTK IKEGLTETTF EEDGVATGNH EYCVEVKYTA
     GVSPKKCVNV TINPTQFNPV KNLKAQPDGG DVVLKWEAPS AKKAEGSREV KRIGDGLFVT
     IEPANDVRAN EAKVVLAADN VWGDNTGYQF LLDADHNTFG SVIPATGPLF TGTASSNLYS
     ANFEYLIPAN ADPVVTTQNI IVTGQGEVVI PGGVYDYCIT NPEPASGKMW IAGDGGNQPA
     RYDDFTFEAG KKYTFTMRRA GMGDGTDMEV EDDSPASYTY TVYRDGTKIK EGLTETTYRD
     AGMSAQSHEY CVEVKYAAGV SPKVCVDYIP DGVADVTAQK PYTLTVVGKT ITVTCQGEAM
     IYDMNGRRLA AGRNTVVYTA QGGYYAVMVV VDGKSYVEKL AVK
//
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