| IED ID | IndEnz0005001446 |
| Enzyme Type ID | lipase001446 |
| Protein Name |
Cyclic GMP-AMP synthase c-GAMP synthase c-GMP-AMP synthase EC 2.7.7.- 3'3'-cGAMP synthase Cyclic AMP-GMP synthase c-AMP-GMP synthase Dinucleotide cyclase DncV |
| Gene Name | dncV ESG_RS0100135 |
| Organism | Escherichia coli |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli |
| Enzyme Sequence | MHWDLNNYYSNNMDGLISKLKLSKTESTKLKELRQIVRERTRDVFKEARAVAADVKKHTLTLEGVRLKLGQTNVRYLSTADQAEVARLIFEMDDDARNDFINLQPRFWTQGSFQYDTLNKPFQPGQEMDIDDGTYMPMTVFESEPRIGHTLLLLLVDTSLKSLEAENDGWRFEEKNTCGRIKIPHEKTHIDVPMYAIPKNQFQTKQTAADSAHILKSESIFESVALNRDSREAYLVESDKVNLALREGAKRWSISDPKIVEDWFNDSCKRIGGHVRSICRFMKAWRDAQWDVGGPSSISLMTAVVNILNREEHNDSDLAGTMKLVAKLLPDEFNRGLESPDDTDTKLLFPAEWDQNVHQKTIVETMKTLYEILVDAENANTREDALHKMNEAFGKRVTNAQLITSIAAAPAFHVSPSREPEPRKINKTMVSG |
| Enzyme Length | 432 |
| Uniprot Accession Number | P0DTF0 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 180; /note=ATP; /evidence=ECO:0000250|UniProtKB:Q9KVG7; BINDING 255; /note=ATP; /evidence=ECO:0000250|UniProtKB:Q9KVG7; BINDING 283; /note=GTP; /evidence=ECO:0000250|UniProtKB:Q9KVG7; BINDING 297; /note=GTP; /evidence=ECO:0000250|UniProtKB:Q9KVG7; BINDING 344; /note=GTP; /evidence=ECO:0000250|UniProtKB:Q9KVG7 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + GTP = 3',3'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:35647, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:71501; Evidence={ECO:0000250|UniProtKB:Q9KVG7};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35648; Evidence={ECO:0000250|UniProtKB:Q9KVG7}; |
| DNA Binding | |
| EC Number | 2.7.7.- |
| 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: Catalyzes the synthesis of 3'3'-cyclic GMP-AMP (3'3'-cGAMP) from GTP and ATP, a second messenger in cell signal transduction. Is also able to produce c-di-AMP and c-di-GMP from ATP and GTP. Controls the activity of cGAMP-activated phospholipase CapV, a patatin-like lipase that is a direct 3',3'-cGAMP receptor encoded in the dncV operon. {ECO:0000250|UniProtKB:Q9KVG7}.; FUNCTION: Protects E.coli against phage infection. When capV and dncV are introduced in E.coli MG1655 there is 1000-fold protection against phage P1; protection against other phage (T2, T4, T5, T6 and lambda-vir) requires the 2 subsequent genes (cap2 and cap3). {ECO:0000269|PubMed:31533127}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 110..115; /note=GTP; /evidence=ECO:0000250|UniProtKB:Q9KVG7 |
| Features | Binding site (5); Chain (1); Metal binding (3); Mutagenesis (1); Nucleotide binding (1) |
| Keywords | ATP-binding;Antiviral defense;GTP-binding;Magnesium;Metal-binding;Nucleotide metabolism;Nucleotide-binding;Nucleotidyltransferase;Transferase |
| Interact With | |
| Induction | INDUCTION: Part of the CBASS operon consisting of capV-dncV-cap2-cap3. {ECO:0000305|PubMed:31533127}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,317 |
| Kinetics | |
| Metal Binding | METAL 129; /note=Magnesium; catalytic; /evidence=ECO:0000250|UniProtKB:Q9KVG7; METAL 131; /note=Magnesium; catalytic; /evidence=ECO:0000250|UniProtKB:Q9KVG7; METAL 191; /note=Magnesium; catalytic; /evidence=ECO:0000250|UniProtKB:Q9KVG7 |
| Rhea ID | RHEA:35647; RHEA:35648 |
| Cross Reference Brenda |