ID   PRTC2_PORGN             Reviewed;         361 AA.
AC   P33437;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 3.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Collagenase {ECO:0000303|PubMed:1317840};
DE            EC=3.4.-.-;
DE   Flags: Fragment;
GN   Name=prtC {ECO:0000303|PubMed:1317840};
OS   Porphyromonas gingivalis.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=837;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION, COFACTOR,
RP   AND SUBUNIT.
RC   STRAIN=ATCC 53977;
RX   PubMed=1317840; DOI=10.1128/jb.174.12.3889-3895.1992;
RA   Kato T., Takahashi N., Kuramitsu H.K.;
RT   "Sequence analysis and characterization of the Porphyromonas gingivalis
RT   prtC gene, which expresses a novel collagenase activity.";
RL   J. Bacteriol. 174:3889-3895(1992).
CC   -!- FUNCTION: Has collagenase activity. Active on soluble collagen,
CC       reconstituted type I collagen, heat denatured type I collagen and
CC       azocoll, but not gelatin or the synthetic bacterial collagenase
CC       substrate PZ-PLGPA. May play a role in virulence.
CC       {ECO:0000269|PubMed:1317840}.
CC   -!- COFACTOR:
CC       Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC         Evidence={ECO:0000305|PubMed:1317840};
CC   -!- ACTIVITY REGULATION: Activity somewhat enhanced by calcium ions,
CC       inhibited by zinc and Fe(3+) ions and by p-chloromercuribenzoic acid
CC       and EDTA. Activity is enhanced by salivary peptide cystatin and reduced
CC       by salivary peptide histatin. {ECO:0000269|PubMed:1317840}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1317840}.
CC   -!- SIMILARITY: Belongs to the peptidase U32 family. {ECO:0000305}.
CC   -!- CAUTION: Upon comparison to genes from other strains this is probably a
CC       fragment, and may have a number of sequencing errors. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA25650.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; M60404; AAA25650.1; ALT_INIT; Genomic_DNA.
DR   PIR; A41881; A41881.
DR   AlphaFoldDB; P33437; -.
DR   SMR; P33437; -.
DR   ChEMBL; CHEMBL1909489; -.
DR   MEROPS; U32.001; -.
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; 2.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   PROSITE; PS01276; PEPTIDASE_U32; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Protease; Virulence.
FT   CHAIN           1..361
FT                   /note="Collagenase"
FT                   /id="PRO_0000028523"
FT   NON_TER         1
SQ   SEQUENCE   361 AA;  41055 MW;  C31DE39008E7487D CRC64;
     DLYKIAEICR DKGVKSYLTV NTVIYDEDMT LMRSVIDAAQ KAQISAIIAS DVAAMTYANE
     IGVEVHLSTQ LNISNAEALR FIALAMWSYW QRAEYGSGTY NPRDHRQGHI CGPKGHPVRI
     EMFAHGALCM AVSGKCYLSL HEHNTSANRG ACAQICRRGY TVKDSGLELD IENQYIMSPK
     DLKTIHFINK MMDAGVRVFK IEGRARGPEY VYTVCRCYKE AIEAYCNGTY DEESIGRWDE
     QLATVFNRGF WDGYYLGQRL GEWTHRYGSG RTRQKTYVGK GIKYFSRLGV AEFEIESGEL
     HIGDEIVITG PTTGVIIQKV EEIRYELQTV EKATKGQRIS IPVKEKVRPS DKLYRFDKRE
     E