KGP38_PORGN
ID KGP38_PORGN Reviewed; 1723 AA.
AC P72194;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Lys-gingipain 381 {ECO:0000303|PubMed:15297553, ECO:0000303|PubMed:8889827, ECO:0000312|EMBL:BAA11870.1};
DE EC=3.4.22.47;
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:BAA11870.1};
OS Porphyromonas gingivalis.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=837;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA11870.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 229-253, SUBCELLULAR
RP LOCATION, AND POST-TRANSLATIONAL PROCESSING.
RC STRAIN=ATCC BAA-1703 / FDC 381 {ECO:0000312|EMBL:BAA11870.1};
RX PubMed=8889827; DOI=10.1093/oxfordjournals.jbchem.a021426;
RA Okamoto K., Kadowaki T., Nakayama K., Yamamoto K.;
RT "Cloning and sequencing of the gene encoding a novel lysine-specific
RT cysteine proteinase (Lys-gingipain) in Porphyromonas gingivalis: structural
RT relationship with the arginine-specific cysteine proteinase (Arg-
RT gingipain).";
RL J. Biochem. 120:398-406(1996).
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. Hydrolyzes bovine hemoglobin, bovine serum
CC albumin, casein, human placental type I collagen and human IgA and IgG.
CC Disrupts the functions of polymorphonuclear leukocytes. May act as a
CC virulence factor in the development of peridontal disease. Involved in
CC the coaggregation of P.gingivalis with other oral bacteria (By
CC similarity). {ECO:0000250|UniProtKB:B2RLK2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase with strict specificity for lysyl bonds.;
CC EC=3.4.22.47; Evidence={ECO:0000250|UniProtKB:B2RLK2};
CC -!- SUBCELLULAR LOCATION: [Lys-gingipain catalytic subunit]: Secreted
CC {ECO:0000269|PubMed:8889827}.
CC -!- PTM: Proteolytically cleaved into a catalytic subunit and three
CC adhesins. Arg-gingipain is involved in this post-translational
CC processing. {ECO:0000250|UniProtKB:Q51817, ECO:0000269|PubMed:8889827}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D83258; BAA11870.1; -; Genomic_DNA.
DR AlphaFoldDB; P72194; -.
DR SMR; P72194; -.
DR MEROPS; C25.002; -.
DR PRIDE; P72194; -.
DR GeneID; 29256891; -.
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; 3.
DR Pfam; PF10365; DUF2436; 1.
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; Direct protein sequencing; Hydrolase; Metal-binding; Protease;
KW Secreted; Signal; Thiol protease; Virulence; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..228
FT /evidence="ECO:0000255, ECO:0000269|PubMed:8889827"
FT /id="PRO_0000395369"
FT CHAIN 229..1723
FT /note="Lys-gingipain 381"
FT /evidence="ECO:0000305|PubMed:8889827"
FT /id="PRO_0000395370"
FT CHAIN 229..?
FT /note="Lys-gingipain catalytic subunit"
FT /evidence="ECO:0000305|PubMed:8889827"
FT /id="PRO_0000395371"
FT CHAIN 738..?
FT /note="39 kDa adhesin"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT /id="PRO_0000395372"
FT CHAIN 1156..?
FT /note="15 kDa adhesin"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT /id="PRO_0000395373"
FT CHAIN 1291..?
FT /note="44 kDa adhesin"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT /id="PRO_0000395374"
FT REGION 964..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 BINDING 1430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1432
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1446
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1448
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1450
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1480
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1495
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT BINDING 1585
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q51817"
FT SITE 228..229
FT /note="Cleavage; site 1"
FT /evidence="ECO:0000250|UniProtKB:Q51817,
FT ECO:0000269|PubMed:8889827"
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; 187262 MW; 5628963D251493EB CRC64;
MRKLLLLIAA SLLGVGLYAQ SAKIKLDAPT TRTTCTNNSF KQFDASFSFN EVELTKVETK
GGTFASVSIP GAFPTGEVGS PEVPAVRKLI AVPVGATPVV RVKSFTEQVY SLNQYGSEKL
MPHQPSMSKS DDPEKVPFVY 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 ADPSLTATQV KALTNKDKYF LAIGNCCVTA
QFDYPQPCFG EVMTRVKEKG AYAYIGSSPN SYWGEDYYWS VGANAVFGVQ PTFEGTSMGS
YDATFLEDSY NTVNSIMWAG NLAATHAGNI GNITHIGAHY YWEAYHVLGD GSVMPYRAMP
KTNTYTLPAS LPQNQASYSI QASAGSYVAI SKDGVLYGTG VANASGVATV NMTKQITENG
NYDVVITRSN YLPVIKQIQA GEPSPYQPVS NLTATTQGQK VTLKWDAPSA KKAEASREVK
RIGDGLFVTI EPANDVRANE AKVVLAADNV WGDNTGYQFL LDADHNTFGS VIPATGPLFT
GTASSNLYSA NFEYLIPANA DPVVTTQNII VTGQGEVVIP GGVYDYCITN PEPASGKMWI
AGDGGNQPAR YDDFTFEAGK KYTFTMRRAG MGDGTDMEVE DDSPASYTYT VYRDGTKIQE
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 GDGQDWLCLS SGQLDWLTAH
GGTNVVASFS WNGMALNPDN YLISKDVTGA TKVKYYYAVN DGFPGDHYAV MISKTGTNAG
DFTVVFEETP NGINKGGARF GLSTEANGAK PQSVWIERTV DLPAGTKYVA FRHYNCSDLN
YILLDDIQFT MGGSPTPTDY TYTVYRDGTK IKEGLTETTF EEDGVATGNH EYCVEVKYTA
GVSPKVCVNV TINPTQFNPV KNLKAQPDGG DVVLKWEAPS GKRGELLNED FEGDAIPTGW
TALDADGDGN NWDITLNEFT RGERHVLSPL RASNVAISYS SLLQGQEYLP LTPNNFLITP
KVEGAKKITY KVGSPGLPQW SHDHYALCIS KSGTAAADFE VIFEETMTYT QGGANLTREK
DLPAGTKYVA FRHYNCTDVL GIMIDDVVIT GEGEGPSYTY TVYRDGTKIQ EGLTETTYRD
AGMSAQSHEY CVEVKYAAGV SPKVCVDYIP DGVADVTAQK PYTLTVVGKT ITVTCQGEAM
IYDMNGRRLA AGRNTVVYTA QGGYYAVMVV VDGKSYVEKL AIK
