CPG2_PORG3
ID CPG2_PORG3 Reviewed; 736 AA.
AC B2RKU0;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Gingipain R2;
DE EC=3.4.22.37 {ECO:0000250|UniProtKB:P95493};
DE AltName: Full=Arg-gingipain;
DE Flags: Precursor;
GN Name=rgpB {ECO:0000312|EMBL:BAG33985.1};
GN OrderedLocusNames=PGN_1466 {ECO:0000312|EMBL:BAG33985.1};
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:BAG33985.1, 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 RgpA 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 (By similarity).
CC {ECO:0000250|UniProtKB:P95493, ECO:0000269|PubMed:9786913}.
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:P95493};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P95493}.
CC -!- SIMILARITY: Belongs to the peptidase C25 family. {ECO:0000305}.
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DR EMBL; AP009380; BAG33985.1; -; Genomic_DNA.
DR RefSeq; WP_012458292.1; NZ_CP025930.1.
DR AlphaFoldDB; B2RKU0; -.
DR SMR; B2RKU0; -.
DR STRING; 431947.PGN_1466; -.
DR MEROPS; C25.001; -.
DR PRIDE; B2RKU0; -.
DR EnsemblBacteria; BAG33985; BAG33985; PGN_1466.
DR GeneID; 29256649; -.
DR KEGG; pgn:PGN_1466; -.
DR eggNOG; COG2957; Bacteria.
DR HOGENOM; CLU_376783_0_0_10; -.
DR OMA; KENGRMI; -.
DR BioCyc; PGIN431947:G1G2V-1668-MON; -.
DR BRENDA; 3.4.22.37; 756.
DR PHI-base; PHI:7888; -.
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; -; 1.
DR Gene3D; 2.60.40.3800; -; 1.
DR Gene3D; 3.40.50.10390; -; 1.
DR InterPro; IPR029030; Caspase-like_dom_sf.
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; IPR041333; M60_C.
DR InterPro; IPR005536; Peptidase_C25_Ig-like_domain.
DR InterPro; IPR012600; Propeptide_C25.
DR InterPro; IPR026444; Secre_tail.
DR Pfam; PF01364; Peptidase_C25; 1.
DR Pfam; PF03785; Peptidase_C25_C; 1.
DR Pfam; PF18630; Peptidase_M60_C; 1.
DR Pfam; PF08126; Propeptide_C25; 1.
DR SUPFAM; SSF52129; SSF52129; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR04183; Por_Secre_tail; 1.
PE 3: Inferred from homology;
KW Calcium; Hydrolase; Metal-binding; Protease; Secreted; Signal;
KW Thiol protease; Virulence; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..229
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT /id="PRO_0000436616"
FT CHAIN 230..736
FT /note="Gingipain R2"
FT /id="PRO_5002780319"
FT ACT_SITE 440
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT ACT_SITE 473
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 478
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 487
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 521
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 522
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 525
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 531
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 613
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 639
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P95493"
SQ SEQUENCE 736 AA; 80930 MW; EB8E64FDD148A069 CRC64;
MKKNFSRIVS IVAFSSLLGG MAFAQPAERG RNPQVRLLSA EQSMSKVQFR MDNLQFTDVQ
TSKGVAQVPT FTEGVNISEK GTPILPILSR SLAVSETRAM KVEVVSSKFI EKKDVLIAPS
KGVISRAENP DQIPYVYGQS YNEDKFFPGE IATLSDPFIL RDVRGQVVNF APLQYNPVTK
TLRIYTEIVV AVSETAEAGQ NTISLVKNST FTGFEDIYKS VFMNYEATRY TPVEEKENGR
MIVIVAKKYE GDIKDFVDWK NQRGLRTEVK VAEDIASPVT ANAIQQFVKQ EYEKEGNDLT
YVLLVGDHKD IPAKITPGIK SDQVYGQIVG NDHYNEVFIG RFSCESKEDL KTQIDRTIHY
ERNITTEDKW LGQALCIASA EGGPSADNGE SDIQHENVIA NLLTQYGYTK IIKCYDPGVT
PKNIIDAFNG GISLVNYTGH GSETAWGTSH FGTTHVKQLT NSNQLPFIFD VACVNGDFLF
SMPCFAEALM RAQKDGKPTG TVAIIASTIN QSWASPMRGQ DEMNEILCEK HPNNIKRTFG
GVTMNGMFAM VEKYKKDGEK MLDTWTVFGD PSLLVRTLVP TEMQVTAPAN ISASAQTFEV
ACDYNGAIAT LSDDGDMVGT AIVKDGKAII KLNESIADET NLTLTVVGYN KVTVIKDVKV
EGTSIADVAN DKPYTVAVSG KTITVESPAA GLTIFDMNGR RVATAKNRMV FEAQNGVYAV
RIATEGKTYT EKVIVK
