KGP66_PORGN
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 03-AUG-2022, entry version 81.
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; Porphyromonadaceae;
OC 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., Prochazka V.,
RA Kiefer M.C., Travis J., Barr P.J.;
RT "Molecular cloning and characterization of Porphyromonas gingivalis lysine-
RT specific gingipain. A new member of an emerging family of pathogenic
RT 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 of
RT the kgp (Lys-gingipain) gene.";
RL J. Clin. Microbiol. 42:3873-3876(2004).
CC -!- FUNCTION: Cysteine proteinase with a strong preference for substrates
CC with Lys in the P1 position (PubMed:8999833). Hydrolyzes bovine
CC hemoglobin, bovine serum albumin, casein, human placental type I
CC collagen and human IgA and IgG. Disrupts the functions of
CC polymorphonuclear leukocytes. May act as a virulence factor in the
CC development of peridontal disease. Involved in the coaggregation of
CC P.gingivalis with other oral bacteria (By similarity).
CC {ECO:0000250|UniProtKB:B2RLK2, ECO:0000269|PubMed:8999833}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase with strict specificity for lysyl bonds.;
CC EC=3.4.22.47; Evidence={ECO:0000269|PubMed:8999833};
CC -!- SUBCELLULAR LOCATION: [Lys-gingipain catalytic subunit]: Secreted
CC {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-terminus
CC exist in different P.gingivalis strains. {ECO:0000269|PubMed:15297553}.
CC -!- SIMILARITY: Belongs to the peptidase C25 family. {ECO:0000255}.
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DR EMBL; U54691; AAA99810.1; -; Genomic_DNA.
DR AlphaFoldDB; P72197; -.
DR SMR; P72197; -.
DR ChEMBL; CHEMBL5664; -.
DR MEROPS; C25.002; -.
DR PRIDE; P72197; -.
DR BRENDA; 3.4.22.37; 756.
DR BRENDA; 3.4.22.47; 756.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
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 another organism; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 2.60.40.3800; -; 1.
DR Gene3D; 3.40.50.10390; -; 1.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR011628; Cleaved_adhesin.
DR InterPro; IPR001769; Gingipain.
DR InterPro; IPR029031; Gingipain_N_sf.
DR InterPro; IPR038490; Gingipain_propep_sf.
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
FT /evidence="ECO:0000255"
FT PROPEP 25..228
FT /evidence="ECO:0000250|UniProtKB:Q51817, ECO:0000255"
FT /id="PRO_0000395375"
FT CHAIN 229..1723
FT /note="Lys-gingipain HG66"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT /id="PRO_0000395376"
FT CHAIN 229..?
FT /note="Lys-gingipain catalytic subunit"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT /id="PRO_0000395377"
FT CHAIN 738..?
FT /note="39 kDa adhesin"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT /id="PRO_0000395378"
FT CHAIN 1156..?
FT /note="15 kDa adhesin"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT /id="PRO_0000395379"
FT CHAIN 1291..?
FT /note="44 kDa adhesin"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT /id="PRO_0000395380"
FT REGION 965..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 444
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT ACT_SITE 477
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 482
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 491
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 987
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 989
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1000
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1002
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1004
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1006
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1021
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1023
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1042
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT SITE 228..229
FT /note="Cleavage; site 1"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT SITE 737..738
FT /note="Cleavage; site 2"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT SITE 1155..1156
FT /note="Cleavage; site 3"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT SITE 1290..1291
FT /note="Cleavage; site 4"
FT /evidence="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
