| IED ID | IndEnz0002015988 |
| Enzyme Type ID | protease015988 |
| Protein Name |
Microbial collagenase EC 3.4.24.3 prtVp |
| Gene Name | prt VPA0459 |
| Organism | Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio Vibrio harveyi group Vibrio parahaemolyticus Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) |
| Enzyme Sequence | MSHIRFFPRHRLALACMLASVSSFSFAQNQCAVADLQQSRDLAAAVSGAEYDCYHAWFSAPSATLNDIYSEASLSRIQVALDQEIARYRGEAEQARVLENLGEFVRAAYYVRYNAGTGTPEFSEALSQRFAQSTNLFLNNPHALDQGREQVGAMKSLTLMVDNVKQLPLTMDSMMAALMHFNRDTAKDTQWVDGLNNLFRSMAGHAANDAFYRYMANNTHHIDTLARFASDNAWALDTDANFIVFNALRETGRLLASPDQETKRKALAVMQQVMQRYPLGSEHDKLWLAAVEMMSYYAPEGLNGLNLEQAKQDLAARVMPNRFECQGPAIIRSEDLTDAQAAKACEVLAAKEADFHQVANTGNQPVADDLNDRVEVAVFASNDSYVDYSSFLFGNTTDNGGQYLEGTPSRADNTARFVAYRYANGEDLSILNLEHEYTHYLDARFNQYGSFSDNLAHGHIVWWLEGFAEYMHYKQGYKAAIDLIPSGKLSLSTVFDTTYSHDSNRIYRWGYLAVRFMLENHPQDVESLLALSRSGQFAQWAQQVTVLGQQYDAEFERWLDTLEVVVEPEQPGTDPEEPSEPTDPEVQVTELAANQSLQLSGEAYSEKLFYVDVPANTVRFNVSIEGAGDADLYMSYNKVAHYYDFEMSQYADGSNEEIQFAPEQNGYVKAGRYYISLTGRDSYDSVNLVAALEVEAQTPPTQVQDDLAPVVLESGEAKVLTVHQQRYAAVYVPEGVKEVRVWMSSQSNANDPYGAGNVDLYASRKHWPTAEQHEYASNYAGSNEYLAIPVTEAGYVHFSLQAPQQGDDVEMLVYFF |
| Enzyme Length | 816 |
| Uniprot Accession Number | Q56696 |
| Absorption | |
| Active Site | ACT_SITE 436; /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; |
| DNA Binding | |
| EC Number | 3.4.24.3 |
| Enzyme Function | FUNCTION: Possesses gelatinolytic activity. Can cause weak haemolysis on blood agar. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Frameshift (1); Metal binding (2); Sequence conflict (5); Signal peptide (1) |
| Keywords | Collagen degradation;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 91,444 |
| Kinetics | |
| Metal Binding | METAL 435; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 439; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.3; |