CPG1_PORGN
ID CPG1_PORGN Reviewed; 991 AA.
AC P28784; Q45168;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Gingipain R1;
DE EC=3.4.22.37 {ECO:0000269|PubMed:1527017};
DE AltName: Full=Arg-gingipain;
DE AltName: Full=Gingipain 1;
DE AltName: Full=RGP-1;
DE Flags: Precursor;
GN Name=rgpA; Synonyms=rgp1;
OS Porphyromonas gingivalis.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=837;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 228-290 AND 517-541,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-1703 / FDC 381;
RX PubMed=7864651; DOI=10.1006/abbi.1995.1123;
RA Okamoto K., Misumi Y., Kadowaki T., Yoneda M., Yamamoto K., Ikehara Y.;
RT "Structural characterization of argingipain, a novel arginine-specific
RT cysteine proteinase as a major periodontal pathogenic factor from
RT Porphyromonas gingivalis.";
RL Arch. Biochem. Biophys. 316:917-925(1995).
RN [2]
RP PROTEIN SEQUENCE OF 228-270, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RC STRAIN=HG66;
RX PubMed=1527017; DOI=10.1016/s0021-9258(19)37045-0;
RA Chen Z., Potempa J., Polanowski A., Wikstrom M., Travis J.;
RT "Purification and characterization of a 50-kDa cysteine proteinase
RT (gingipain) from Porphyromonas gingivalis.";
RL J. Biol. Chem. 267:18896-18901(1992).
CC -!- FUNCTION: Thiol protease. Acts synergistically with RgpB to catalyze
CC the maturation of fimbrial subunits, such as FimA (By similarity). Its
CC proteolytic activity is a major factor in both periodontal tissue
CC destruction and in evasion of host defense mechanisms (Probable).
CC {ECO:0000250|UniProtKB:B2RKU0, 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:0000269|PubMed:1527017};
CC -!- ACTIVITY REGULATION: Requires cysteine for activation and Ca(2+) and/or
CC Mg(2+) for stabilization. It is stimulated by glycine-containing
CC dipeptides. It is resistant to inhibition by proteinase inhibitors in
CC human plasma. {ECO:0000269|PubMed:1527017}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1527017,
CC ECO:0000269|PubMed:7864651}.
CC -!- SIMILARITY: Belongs to the peptidase C25 family. {ECO:0000305}.
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DR EMBL; D26470; BAA05484.1; -; Genomic_DNA.
DR PIR; I40229; I40229.
DR AlphaFoldDB; P28784; -.
DR SMR; P28784; -.
DR MEROPS; C25.001; -.
DR BRENDA; 3.4.22.37; 756.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd10913; Peptidase_C25_N_gingipain; 1.
DR Gene3D; 2.60.40.10; -; 2.
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; IPR018832; Pept_C25_gingipain_C.
DR InterPro; IPR005536; Peptidase_C25_Ig-like_domain.
DR InterPro; IPR012600; Propeptide_C25.
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.
DR SUPFAM; SSF81296; SSF81296; 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..227
FT /evidence="ECO:0000269|PubMed:1527017,
FT ECO:0000269|PubMed:7864651"
FT /id="PRO_0000026533"
FT CHAIN 228..991
FT /note="Gingipain R1"
FT /id="PRO_0000026534"
FT ACT_SITE 438
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 471
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 330
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 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 485
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 519
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
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 523
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT BINDING 529
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P95493"
FT CONFLICT 264..265
FT /note="RT -> TK (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 991 AA; 108782 MW; 03EE3F43CEBE2544 CRC64;
MKNLNKFVSI ALCSSLLGGM AFAQQTELGR NPNVRLLEST QQSVTKVQFR MDNLKFTEVQ
TPKGMAQVPT YTEGVNLSEK GMPTLPILSR SLAVSDTREM KVEVVSSKFI EKKNVLIAPS
KGMIMRNEDP KKIPYVYGKS YSQNKFFPGE IATLDDPFIL RDVRGQVVNF APLQYNPVTK
TLRIYTEITV AVSETSEQGK NILNKKGTFA GFEDTYKRMF MNYEPGRYTP VEEKQNGRMI
VIVAKKYEGD IKDFVDWKNQ RGLRTEVKVA EDIASPVTAN AIQQFVKQEY EKEGNDLTYV
LLVGDHKDIP AKITPGIKSD QVYGQIVGND HYNEVFIGRF SCESKEDLKT QIDRTIHYER
NITTEDKWLG QALCIASAEG GPSADNGESD IQHENVIANL LTQYGYTKII KCYDPGVTPK
NIIDAFNGGI SLVNYTGHGS ETAWGTSHFG TTHVKQLTNS NQLPFIFDVA CVNGDFLFSM
PCFAEALMRA QKDGKPTGTV AIIASTINQS WASPMRGQDE MNEILCEKHP NNIKRTFGGV
TMNGMFAMVE KYKKDGEKML DTWTVFGDPS LLVRTLVPTK MQVTAPAQIN LTDASVNVSC
DYNGAIATIS ANGKMFGSAV VENGTATINL TGLTNESTLT LTVVGYNKET VIKTINTNGE
PNPYQPVSNL TATTQGQKVT LKWDAPSTKT NATTNTARSV DGIRELVLLS VSDAPELLRS
GQAEIVLEAH DVWNDGSGYQ ILLDADHDQY GQVIPSDTHT LWPNCSVPAN LFAPFEYTVP
ENADPSCSPT NMIMDGTASV NIPAGTYDFA IAAPQANAKI WIAGQGPTKE DDYVFEAGKK
YHFLMKKMGS GDGTELTISE GGGSDYTYTV YRDGTKIKEG LTETTYRDAG MSAQSHEYCV
EVKYAAGVSP KVCVDYIPDG VADVTAQKPY TLTVVGKTIT VTCQGEAMIY DMNGRRLAAG
RNTVVYTAQG GYYAVMVVVD GKSYVEKLAV K
