| IED ID | IndEnz0002008900 |
| Enzyme Type ID | protease008900 |
| Protein Name |
Pre-pro-metalloprotease PrtV EC 3.4.24.- Cleaved into: Pro-metalloprotease PrtV; 37 kDa metalloprotease PrtV; 18 kDa metalloprotease PrtV |
| Gene Name | prtV VCM66_A0219 |
| Organism | Vibrio cholerae serotype O1 (strain M66-2) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio Vibrio cholerae Vibrio cholerae serotype O1 (strain M66-2) |
| Enzyme Sequence | MKTIKKTLLAAAIASFFSSGLYAQTPIDLGVVNEDKLIEMLVRTGQIPADASDVDKRIALERYLEEKIRSGFKGDAQFGKKALEQRAKILKVIDKQKGPHKARVFALDVGQKRTDKVLALLIDFPDLPWDDNRLTKEHTEMLYDRYEPSHYQDLLFSDKGYTGPNGENFISMRQYYESESGNSYSVSGQAAGWYRASKNAAYYGGNSPGTNNDMNARELVREALDQLARDPNINLADYDIEDRYDYNGNGNFREPDGVIDHLMIFHASVGEEAGGGVLGADAIWSHRFNLGRYHVLEGTKSNVPGRFNGQFAAFDYTIQPIDAAAGVCAHEYGHDLGLPDEYDTQYTGTGEPVSYWSIMSSGSWAGKIGGTQPTAFSSWAKQFLQNSIGGRWINHEQLSINELEAKPRVVTLFQTTDNSRPNMVKVTLPMKRVEGIKPAEGEFSFYSNRGDDLKNRMSRPLTIPAGSQATLRFKAWFQIEKDYDYARVLINGKPIAGNITTMDDPFKSGLVPAISGQSDGWVDAQFDLSAWAGQTVELAFDYLTDGGLAMEGLYVDDLRLEVDGNQTLIDNAEGTSSFAFQGFTKNGGFHEANHYYLLQWRSHNDVDQGLANLKRFGQLMSFEPGLLVWYVDESYADNWVGKHPGEGWLGVVDADQNALVWSKTGEVAQTRFQVRDATFSLFDQAPLKLVTADGNTLEDMNLTANASFSDDQDYSSPQAPDSGRKVMPFGLKIDLLSQSKENEYGVVRLSKVTTENIAPVARFELKVEGLSVMSQNTSSDSDGNIVSYLWDFGNGQTSTEAAPTWSYTKAGSYSVTLTVTDDKGDSDTHQQTIKVDTPNALPQASANYIHLGRWVTMWSTSTDSDGRIVDTEWTLPNGKIKRGRMFTAIFPSYGHHDVQLKVMDDRGAVTTITIKVKL |
| Enzyme Length | 918 |
| Uniprot Accession Number | C3LUP3 |
| Absorption | |
| Active Site | ACT_SITE 331; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Calcium plays an important structural role, providing stability to this protein in the cytoplasm. Outside the cell, the decrease of the calcium concentration triggers the autoproteolysis. {ECO:0000250|UniProtKB:Q9KMU6}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Metalloprotease that exhibits a cytotoxic effect leading to cell death. In host tissues, it could play a role in pathogenesis by modulating the stability of the extracellular matrix components such as fibronectin and fibrinogen. Also able to cleave plasminogen. {ECO:0000250|UniProtKB:Q9KMU6}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (9); Chain (3); Domain (2); Metal binding (6); Propeptide (2); Signal peptide (1) |
| Keywords | 3D-structure;Autocatalytic cleavage;Calcium;Cytolysis;Hydrolase;Metal-binding;Metalloprotease;Protease;Repeat;Secreted;Signal;Virulence;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9KMU6}. |
| Modified Residue | |
| Post Translational Modification | PTM: PrtV is expressed as an inactive, multidomain, 102 kDa pre-pro-metalloprotease. To form a catalytically active protease, PrtV is first secreted, and then it undergoes N- and C-terminal cleavages during envelope translocation to yield a 81 kDa pro-metalloprotease. Outside the cell, the 81 kDa pro-metalloprotease undergoes an auto-cleavage. The two major products of autoproteolysis (37 kDa and 18 kDa) together form the so called 55 kDa active complex. {ECO:0000250|UniProtKB:Q9KMU6}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4L9D; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 101,882 |
| Kinetics | |
| Metal Binding | METAL 330; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 334; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 757; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:23905008; METAL 782; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:23905008; METAL 821; /note=Calcium; /evidence=ECO:0000269|PubMed:23905008; METAL 825; /note=Calcium; /evidence=ECO:0000269|PubMed:23905008 |
| Rhea ID | |
| Cross Reference Brenda |