| IED ID | IndEnz0002002764 |
| Enzyme Type ID | protease002764 |
| Protein Name |
CD-NTase-associated protein 3 Probable metalloprotease Cap3 |
| Gene Name | cap3 VC_0181 |
| 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 | MMSDVELVFKDESDCLVVIMGHVVTRLLSYRQLHHLTPESAGVLIGERRGQHLVVCDISEPGSGDIRQRCRVDRRGVHHQSRVNEAFERSAGTHLYLGEWHTHPEDRPFPSATDRHSWRRNIVSDESMLLLIVGRKDFWLGKKERELITVFKKIES |
| Enzyme Length | 156 |
| Uniprot Accession Number | Q9KVG5 |
| Absorption | |
| Active Site | ACT_SITE 39; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:D4GTS4 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system (PubMed:32839535). {ECO:0000269|PubMed:31533127, ECO:0000303|PubMed:32839535}.; FUNCTION: Protects E.coli against phage P1 and T2 infection. When the 4 gene operon capV-dncV-cap2-cap3 is introduced in E.coli MG1655 there is about 100-fold protection against phages P1 and T2 (PubMed:31533127). Protects E.coli against phage T2 infection. When the CBASS operon (capV-dcnV-cap2-cap3) is introduced in E.coli MG1655 there is a more than 10(3) decrease in the efficiency of T2 plaque formation. Protects 100-fold against phage T5, offers no protection against T7 (PubMed:32544385). {ECO:0000269|PubMed:31533127, ECO:0000269|PubMed:32544385}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Metal binding (3) |
| Keywords | Antiviral defense;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | INDUCTION: Part of the CBASS operon consisting of capV-dncV-cap2-cap3. {ECO:0000305|PubMed:31533127, ECO:0000305|PubMed:32544385}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 18,065 |
| Kinetics | |
| Metal Binding | METAL 101; /note=Zinc; catalytic; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q8U1Y4; METAL 103; /note=Zinc; catalytic; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q8U1Y4; METAL 114; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q8U1Y4 |
| Rhea ID | |
| Cross Reference Brenda |