| IED ID | IndEnz0009000267 |
| Enzyme Type ID | chitinase000267 |
| Protein Name |
Collagenase ColA EC 3.4.24.3 120 kDa collagenase Microbial collagenase |
| Gene Name | colA CPE0173 |
| Organism | Clostridium perfringens (strain 13 / Type A) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Clostridiaceae Clostridium Clostridium perfringens Clostridium perfringens (strain 13 / Type A) |
| Enzyme Sequence | MKKNLKRGELTKLKLVERWSATFTLAAFILFNSSFKVLAADKKVENSNNGQITREINADQISKTELNNEVATDNNRPLGPSIAPSRARNNKIYTFDELNRMNYSDLVELIKTISYENVPDLFNFNDGSYTFFSNRDRVQAIIYGLEDSGRTYTADDDKGIPTLVEFLRAGYYLGFYNKQLSYLNTPQLKNECLPAMKAIQYNSNFRLGTKAQDGVVEALGRLIGNASADPEVINNCIYVLSDFKDNIDKYGSNYSKGNAVFNLMKGIDYYTNSVIYNTKGYDAKNTEFYNRIDPYMERLESLCTIGDKLNNDNAWLVNNALYYTGRMGKFREDPSISQRALERAMKEYPYLSYQYIEAANDLDLNFGGKNSSGNDIDFNKIKADAREKYLPKTYTFDDGKFVVKAGDKVTEEKIKRLYWASKEVKAQFMRVVQNDKALEEGNPDDILTVVIYNSPEEYKLNRIINGFSTDNGGIYIENIGTFFTYERTPEESIYTLEELFRHEFTHYLQGRYVVPGMWGQGEFYQEGVLTWYEEGTAEFFAGSTRTDGIKPRKSVTQGLAYDRNNRMSLYGVLHAKYGSWDFYNYGFALSNYMYNNNMGMFNKMTNYIKNNDVSGYKDYIASMSSDYGLNDKYQDYMDSLLNNIDNLDVPLVSDEYVNGHEAKDINEITNDIKEVSNIKDLSSNVEKSQFFTTYDMRGTYVGGRSQGEENDWKDMNSKLNDILKELSKKSWNGYKTVTAYFVNHKVDGNGNYVYDVVFHGMNTDTNTDVHVNKEPKAVIKSDSSVIVEEEINFDGTESKDEDGEIKAYEWDFGDGEKSNEAKATHKYNKTGEYEVKLTVTDNNGGINTESKKIKVVEDKPVEVINESEPNNDFEKANQIAKSNMLVKGTLSEEDYSDKYYFDVAKKGNVKITLNNLNSVGITWTLYKEGDLNNYVLYATGNDGTVLKGEKTLEPGRYYLSVYTYDNQSGTYTVNVKGNLKNEVKETAKDAIKEVENNNDFDKAMKVDSNSKIVGTLSNDDLKDIYSIDIQNPSDLNIVVENLDNIKMNWLLYSADDLSNYVDYANADGNKLSNTCKLNPGKYYLCVYQFENSGTGNYIVNLQNK |
| Enzyme Length | 1104 |
| Uniprot Accession Number | P43153 |
| Absorption | |
| Active Site | ACT_SITE 503; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Digestion of native collagen in the triple helical region at Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg at P3'.; EC=3.4.24.3; Evidence={ECO:0000250|UniProtKB:Q899Y1}; |
| DNA Binding | |
| EC Number | 3.4.24.3 |
| Enzyme Function | FUNCTION: Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen (By similarity). {ECO:0000250|UniProtKB:Q899Y1}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Metal binding (30); Propeptide (1); Region (7); Sequence conflict (8); Signal peptide (1) |
| Keywords | Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Virulence;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8282691}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..39; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 125,936 |
| Kinetics | |
| Metal Binding | METAL 477; /note="Calcium 1"; /evidence="ECO:0000250|UniProtKB:Q899Y1"; METAL 502; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:Q9X721, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 506; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:Q9X721, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 510; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:Q899Y1"; METAL 514; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:Q899Y1"; METAL 516; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:Q899Y1"; METAL 534; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 772; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 773; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 800; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 802; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 841; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 866; /note="Calcium 3"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 868; /note="Calcium 3"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 868; /note="Calcium 4"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 870; /note="Calcium 4"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 894; /note="Calcium 3"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 894; /note="Calcium 4"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 897; /note="Calcium 3"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 897; /note="Calcium 4"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 993; /note="Calcium 5"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 995; /note="Calcium 5"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 995; /note="Calcium 6"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 997; /note="Calcium 6"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 1016; /note="Calcium 5; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 1020; /note="Calcium 5"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 1020; /note="Calcium 6"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 1022; /note="Calcium 6; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 1023; /note="Calcium 5"; /evidence="ECO:0000250|UniProtKB:Q9X721"; METAL 1023; /note="Calcium 6"; /evidence="ECO:0000250|UniProtKB:Q9X721" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.3; |