ID   TPR_PORGI               Reviewed;         481 AA.
AC   P25806;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2003, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Thiol protease;
DE            EC=3.4.22.-;
GN   Name=tpr; OrderedLocusNames=PG_1055;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=1322368; DOI=10.1128/iai.60.8.3186-3192.1992;
RA   Bourgeau G., Lapointe H., Peloquin P., Mayrand D.;
RT   "Cloning, expression, and sequencing of a protease gene (tpr) from
RT   Porphyromonas gingivalis W83 in Escherichia coli.";
RL   Infect. Immun. 60:3186-3192(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
CC   -!- FUNCTION: Thiol protease. Probably an important virulence factor.
CC   -!- ACTIVITY REGULATION: Inactive below 20 degrees Celsius and pH 6.0.
CC       Inhibited by divalent cations.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR   EMBL; M84471; AAA25652.1; -; Genomic_DNA.
DR   EMBL; AE015924; AAQ66170.1; -; Genomic_DNA.
DR   PIR; S27608; S27608.
DR   RefSeq; WP_005873455.1; NC_002950.2.
DR   AlphaFoldDB; P25806; -.
DR   SMR; P25806; -.
DR   STRING; 242619.PG_1055; -.
DR   MEROPS; C02.022; -.
DR   PRIDE; P25806; -.
DR   EnsemblBacteria; AAQ66170; AAQ66170; PG_1055.
DR   KEGG; pgi:PG_1055; -.
DR   eggNOG; ENOG50343N4; Bacteria.
DR   HOGENOM; CLU_039414_0_0_10; -.
DR   OrthoDB; 1643589at2; -.
DR   BRENDA; 3.4.22.B8; 756.
DR   Proteomes; UP000000588; Chromosome.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00044; CysPc; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   Pfam; PF00648; Peptidase_C2; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; Thiol protease; Virulence.
FT   CHAIN           1..481
FT                   /note="Thiol protease"
FT                   /id="PRO_0000207747"
FT   DOMAIN          169..481
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        229
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        406
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        426
FT                   /evidence="ECO:0000250"
FT   CONFLICT        274
FT                   /note="A -> AN (in Ref. 1; AAA25652)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   481 AA;  54991 MW;  9CC973EF01908383 CRC64;
     MEKKLVPQSI SKERLQKLEA QATLTPQQEE AKARKIEREK ARLKELNIPT ESKESKDCSP
     AGMINPYALT EVILERPLDW SNPRTTDIVE RVLGSSMQDL SKGDSVLRAG RDQNAEVKIV
     DSVLTKTQRG QDGLERILES FNDYDMPPEE KEEAAPKAKK AAQKLDIDDL REQALSSTTI
     TKEISKIILP TKNLRDDNNT VHQYREVGFQ SNGAHNLWDT VVQGIAGDCY MLAALSAIAW
     VWPALLNMDV DIMSNQDEWR LYRYFIGRSK QTYARPSGSG TSTNEILQEG YYKVPIFARS
     RYWFNGEYWP ALFEQAYANW KFPNDSKYNA ILQIGGGWPE EALCELSGDS WFTSSGKLML
     SSFTDLSLLN FMKSMCYSWK TIKPMVIVTP CWEPLPPMMP GIAAYHAYTV LGYTVSNGAY
     YLIIRNPWGV TEPTGDGVLS KRDWVIHFDN MKWFNLSKDD GIFALRLDKV RENFWYIAYM
     Y