CPG1_PORG3
ID CPG1_PORG3 Reviewed; 1703 AA.
AC B2RM93;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Gingipain R1;
DE EC=3.4.22.37 {ECO:0000250|UniProtKB:P28784};
DE AltName: Full=Arg-gingipain;
DE Flags: Precursor;
GN Name=rgpA {ECO:0000312|EMBL:BAG34488.1};
GN OrderedLocusNames=PGN_1970 {ECO:0000312|EMBL:BAG34488.1};
OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS 12257 / NCTC 11834 / 2561).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=431947;
RN [1] {ECO:0000312|EMBL:BAG34488.1, ECO:0000312|Proteomes:UP000008842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC {ECO:0000312|Proteomes:UP000008842};
RX PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA Nakayama K.;
RT "Determination of the genome sequence of Porphyromonas gingivalis strain
RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT rearrangements in P. gingivalis.";
RL DNA Res. 15:215-225(2008).
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX PubMed=9786913; DOI=10.1074/jbc.273.44.29072;
RA Kadowaki T., Nakayama K., Yoshimura F., Okamoto K., Abe N., Yamamoto K.;
RT "Arg-gingipain acts as a major processing enzyme for various cell surface
RT proteins in Porphyromonas gingivalis.";
RL J. Biol. Chem. 273:29072-29076(1998).
CC -!- FUNCTION: Thiol protease. Acts synergistically with RgpB to catalyze
CC the maturation of fimbrial subunits, such as FimA (PubMed:9786913). Its
CC proteolytic activity is a major factor in both periodontal tissue
CC destruction and in evasion of host defense mechanisms (Probable).
CC {ECO:0000269|PubMed:9786913, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins and small molecule substrates, with a
CC preference for Arg in P1.; EC=3.4.22.37;
CC Evidence={ECO:0000250|UniProtKB:P28784};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P28784}.
CC -!- SIMILARITY: Belongs to the peptidase C25 family. {ECO:0000305}.
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; AP009380; BAG34488.1; -; Genomic_DNA.
DR AlphaFoldDB; B2RM93; -.
DR SMR; B2RM93; -.
DR STRING; 431947.PGN_1970; -.
DR MEROPS; C25.001; -.
DR PRIDE; B2RM93; -.
DR EnsemblBacteria; BAG34488; BAG34488; PGN_1970.
DR KEGG; pgn:PGN_1970; -.
DR eggNOG; COG1974; Bacteria.
DR HOGENOM; CLU_240727_0_0_10; -.
DR OMA; NAKIWIA; -.
DR PHI-base; PHI:3702; -.
DR PHI-base; PHI:7887; -.
DR Proteomes; UP000008842; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd10913; Peptidase_C25_N_gingipain; 1.
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; IPR039392; Gingipain_N.
DR InterPro; IPR029031; Gingipain_N_sf.
DR InterPro; IPR038490; Gingipain_propep_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
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.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 3: Inferred from homology;
KW Calcium; Hydrolase; Metal-binding; Protease; Secreted; Signal;
KW Thiol protease; Virulence; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..224
FT /evidence="ECO:0000250|UniProtKB:P28784"
FT /id="PRO_0000436615"
FT CHAIN 225..1703
FT /note="Gingipain R1"
FT /id="PRO_5002781759"
FT REGION 940..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 435
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT ACT_SITE 468
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 331
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 482
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 516
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 517
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 520
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 526
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P95493"
SQ SEQUENCE 1703 AA; 185325 MW; A1EB26D102B2B026 CRC64;
MNKFVSIALC SSLLGGMAFA QQTELGRNPN VRLLESTQQS VTKVQFRMDN LKFTEVQTPK
GMAQVPTYTE GVNLSEKGMP TLPILSRSLA VSDTREMKVE VVSSKFIEKK NVLIAPSKGM
IMRNEDPKKI PYVYGKSYSQ NKFFPGEIAT LDDPFILRDV RGQVVNFAPL QYNPVTKTLR
IYTEITVAVS ETSEQGKNIL NKKGTFAGFE DTYKRMFMNY EPGRYTPVEE KQNGRMIVIV
AKKYEGDIKD FVDWKNQRGL RTEVKVAEDI ASPVTANAIQ QFVKQEYEKE GNDLTYVLLV
GDHKDIPAKI TPGIKSDQVY GQIVGNDHYN EVFIGRFSCE SKEDLKTQID RTIHYERNIT
TEDKWLGQAL CIASAEGGPS ADNGESDIQH ENVIANLLTQ YGYTKIIKCY DPGVTPKNII
DAFNGGISLV NYTGHGSETA WGTSHFGTTH VKQLTNSNQL PFIFDVACVN GDFLFSMPCF
AEALMRAQKD GKPTGTVAII ASTINQSWAS PMRGQDEMNE ILCEKHPNNI KRTFGGVTMN
GMFAMVEKYK KDGEKMLDTW TVFGDPSLLV RTLVPTKMQV TAPAQINLTD ASVNVSCDYN
GAIATISANG KMFGSAVVEN GTATINLTGL TNESTLTLTV VGYNKETVIK TINTNGEPNP
YQPVSNLTAT TQGQKVTLKW DAPSTKTNAT TNTARSVDGI RELVLLSVSD APELLRSGQA
EIVLEAHDVW NDGSGYQILL DADHDQYGQV IPSDTHTLWP NCSVPANLFA PFEYTVPENA
DPSCSPTNMI MDGTASVNIP AGTYDFAIAA PQANAKIWIA GQGPTKEDDY VFEAGKKYHF
LMKKMGSGDG TELTISEGGG SDYTYTVYRD GTKIKEGLTA TTFEEDGVAT GNHEYCVEVK
YTAGVSPKVC KDVTVEGSNE FAPVQNLTGS AVGQKVTLKW DAPNGTPNPN 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
GLSTEANGAK PQSVWIERTV DLPAGTKYVA FRHYNCSDLN YILLDDIQFT MGGSPTPTDY
TYTVYRDGTK IKEGLTETTF EEDGVATGNH EYCVEVKYTA GVSPKECVNV TINPTQFNPV
KNLKAQPDGG DVVLKWEAPS AKKTEGSREV 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
