IED ID | IndEnz0002001314 |
Enzyme Type ID | protease001314 |
Protein Name |
Collagenase EC 3.4.-.- Fragment |
Gene Name | prtC |
Organism | Porphyromonas gingivalis |
Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Porphyromonadaceae Porphyromonas Porphyromonas gingivalis |
Enzyme Sequence | DLYKIAEICRDKGVKSYLTVNTVIYDEDMTLMRSVIDAAQKAQISAIIASDVAAMTYANEIGVEVHLSTQLNISNAEALRFIALAMWSYWQRAEYGSGTYNPRDHRQGHICGPKGHPVRIEMFAHGALCMAVSGKCYLSLHEHNTSANRGACAQICRRGYTVKDSGLELDIENQYIMSPKDLKTIHFINKMMDAGVRVFKIEGRARGPEYVYTVCRCYKEAIEAYCNGTYDEESIGRWDEQLATVFNRGFWDGYYLGQRLGEWTHRYGSGRTRQKTYVGKGIKYFSRLGVAEFEIESGELHIGDEIVITGPTTGVIIQKVEEIRYELQTVEKATKGQRISIPVKEKVRPSDKLYRFDKREE |
Enzyme Length | 361 |
Uniprot Accession Number | P33437 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Activity somewhat enhanced by calcium ions, inhibited by zinc and Fe(3+) ions and by p-chloromercuribenzoic acid and EDTA. Activity is enhanced by salivary peptide cystatin and reduced by salivary peptide histatin. {ECO:0000269|PubMed:1317840}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.-.- |
Enzyme Function | FUNCTION: Has collagenase activity. Active on soluble collagen, reconstituted type I collagen, heat denatured type I collagen and azocoll, but not gelatin or the synthetic bacterial collagenase substrate PZ-PLGPA. May play a role in virulence. {ECO:0000269|PubMed:1317840}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Erroneous initiation (1); Non-terminal residue (1) |
Keywords | Hydrolase;Protease;Virulence |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 41,055 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |