| IED ID | IndEnz0005000896 |
| Enzyme Type ID | lipase000896 |
| 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 VC_A0223 |
| Organism | Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio Vibrio cholerae Vibrio cholerae O1 Vibrio cholerae O1 biovar El Tor Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) |
| Enzyme Sequence | MKTIKKTLLAAAIASFFSSGLYAQTPIDLGVVNEDKLIEMLVRTGQIPADASDVDKRIALERYLEEKIRSGFKGDAQFGKKALEQRAKILKVIDKQKGPHKARVFALDVGQKRTDKVLALLIDFPDLPWDDNRLTKEHTEMLYDRYEPSHYQDLLFSDKGYTGPNGENFISMRQYYESESGNSYSVSGQAAGWYRASKNAAYYGGNSPGTNNDMNARELVREALDQLARDPNINLADYDIEDRYDYNGNGNFREPDGVIDHLMIFHASVGEEAGGGVLGADAIWSHRFNLGRYHVLEGTKSNVPGRFNGQFAAFDYTIQPIDAAAGVCAHEYGHDLGLPDEYDTQYTGTGEPVSYWSIMSSGSWAGKIGGTQPTAFSSWAKQFLQNSIGGRWINHEQLSINELEAKPRVVTLFQTTDNSRPNMVKVTLPMKRVEGIKPAEGEFSFYSNRGDDLKNRMSRPLTIPAGSQATLRFKAWFQIEKDYDYARVLINGKPIAGNITTMDDPFKSGLVPAISGQSDGWVDAQFDLSAWAGQTVELAFDYLTDGGLAMEGLYVDDLRLEVDGNQTLIDNAEGTSSFAFQGFTKNGGFHEANHYYLLQWRSHNDVDQGLANLKRFGQLMSFEPGLLVWYVDESYADNWVGKHPGEGWLGVVDADQNALVWSKTGEVAQTRFQVRDATFSLFDQAPLKLVTADGNTLEDMNLTANASFSDDQDYSSPQAPDSGRKVMPFGLKIDLLSQSKENEYGVVRLSKVTTENIAPVARFELKVEGLSVMSQNTSSDSDGNIVSYLWDFGNGQTSTEAAPTWSYTKAGSYSVTLTVTDDKGDSDTHQQTIKVDTPNALPQASANYIHLGRWVTMWSTSTDSDGRIVDTEWTLPNGKIKRGRMFTAIFPSYGHHDVQLKVMDDRGAVTTITIKVKL |
| Enzyme Length | 918 |
| Uniprot Accession Number | Q9KMU6 |
| 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. PrtV activity is increased by 25 mM of Sr(2+) or Mg(2+) and to some extent by Ba(2+); however, Ba(2+) inhibits PrtV at higher concentrations. Completely inhibited by EDTA and 1,10-phenanthroline. {ECO:0000269|PubMed:18479458}. |
| 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:0000269|PubMed:18479458, ECO:0000269|PubMed:24492010, ECO:0000305|PubMed:9371455}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (3); Domain (2); Helix (3); Metal binding (6); Propeptide (2); Signal peptide (1) |
| Keywords | 3D-structure;Autocatalytic cleavage;Calcium;Cytolysis;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Virulence;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18479458}. |
| 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:0000269|PubMed:18479458, ECO:0000269|PubMed:24492010}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000305|PubMed:18479458 |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 5ABK; |
| 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:0000250|UniProtKB:C3LUP3; METAL 782; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:C3LUP3; METAL 821; /note=Calcium; /evidence=ECO:0000250|UniProtKB:C3LUP3; METAL 825; /note=Calcium; /evidence=ECO:0000250|UniProtKB:C3LUP3 |
| Rhea ID | |
| Cross Reference Brenda |