ID   PRTC1_PORGI             Reviewed;         414 AA.
AC   P59916;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Collagenase;
DE            EC=3.4.-.-;
GN   Name=prtC; OrderedLocusNames=PG_1542;
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 [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: Has collagenase activity. Hydrolyzes type I collagen. May
CC       play a role in virulence (By similarity).
CC       {ECO:0000250|UniProtKB:P33437}.
CC   -!- COFACTOR:
CC       Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC         Evidence={ECO:0000250|UniProtKB:P33437};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250, ECO:0000250|UniProtKB:P33437}.
CC   -!- SIMILARITY: Belongs to the peptidase U32 family. {ECO:0000305}.
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DR   EMBL; AE015924; AAQ66580.1; -; Genomic_DNA.
DR   RefSeq; WP_010956336.1; NC_002950.2.
DR   AlphaFoldDB; P59916; -.
DR   STRING; 242619.PG_1542; -.
DR   MEROPS; U32.001; -.
DR   DNASU; 2553029; -.
DR   EnsemblBacteria; AAQ66580; AAQ66580; PG_1542.
DR   KEGG; pgi:PG_1542; -.
DR   eggNOG; COG0826; Bacteria.
DR   HOGENOM; CLU_011540_0_1_10; -.
DR   Proteomes; UP000000588; Chromosome.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR001539; Peptidase_U32.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   Pfam; PF01136; Peptidase_U32; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   PROSITE; PS01276; PEPTIDASE_U32; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; Virulence.
FT   CHAIN           1..414
FT                   /note="Collagenase"
FT                   /id="PRO_0000028522"
SQ   SEQUENCE   414 AA;  46673 MW;  7FCB907E02C20425 CRC64;
     MNVNDFEIMA PVGSYESLMA AIKAGADSVY FGIEGLNMRA RSANNFTTED LYKIAEICRD
     KGVKSYLTVN TVIYDEDIAL MRSVIDAAQK AQISAIIASD VAAMMYANEI GVEVHLSTQL
     NISNAEALRF YSRFADVVVL ARELNMDQVR TIHETIVRDN ICGPKGHPVR IEMFAHGALC
     MAVSGKCYLS LHEHNSSANR GACAQICRRG YTVKDKDSGL ELDIENQYIM SPKDLKTIHF
     INKMMDAGVR VFKIEGRARG PEYVYTVCRC YKEAIEAYCN GTYDEEAIGR WDEQLATVFN
     RGFWDGYYLG QRLGEWTHRY GSGATRQKIY VGKGIKYFSR LGVAEFEIES GELHIGDEIV
     ITGPTTGVII QKVEEIRYEL QTVEKATKGQ RISIPVKEKV RPSDKLYRFD KREE