IED ID | IndEnz0005001246 |
Enzyme Type ID | lipase001246 |
Protein Name |
Cyclic GMP-AMP synthase c-GAMP synthase c-GMP-AMP synthase EC 2.7.7.- 3'3'-cGAMP synthase CD-NTase001 |
Gene Name | dncV DU321_04130 |
Organism | Escherichia coli |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli |
Enzyme Sequence | MPWDFNNYYSHNMDGLISKLKLSKTESDKLKALRQIVRERTRDVFQEARQVAIDVRRQALTLESVRLKLEKTNVRYLSPEERADLARLIFEMEDEARDDFIKFQPRFWTQGSFQYDTLNRPFHPGQEMDIDDGTYMPMTVFESEPSIGHTLLLLLVDTSLKSLEAENDGWVFEEKNTCGRIKIYREKTHIDVPMYAIPKEQFQKKQTAADSAHLIKSDSVFESFALNRGGREAYAVESDKVNLALREGVRRWSVSDPKIVEDWFNESCKRIGGHLRSVCRFMKAWRDAQWEVGGPSSISLMTAVVNILDRESHNGSDLTGTMKLIARLLPEEFNRGVESPDDTDEKPLFPAESNHNVHHRAIVETMEGLYGILLAAEQSESREEALRKINEAFGKRVTNALLITSSAAAPAFLNAPSKEPSSKPINKTMVSG |
Enzyme Length | 432 |
Uniprot Accession Number | Q6XGD8 |
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:0000269|PubMed:25865248; BINDING 297; /note=GTP; /evidence=ECO:0000269|PubMed:25865248; BINDING 344; /note=GTP; /evidence=ECO:0000269|PubMed:25865248 |
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:0000269|PubMed:30837338};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35648; Evidence={ECO:0000269|PubMed:30837338}; |
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-C(GA) CBASS system (PubMed:32839535). {ECO:0000303|PubMed:32839535, ECO:0000305}.; 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, respectively; however, 3'3'-cGAMP is the dominant molecule produced by DncV in vivo, contrary to the 2'3'-cGAMP produced by eukaryotes. By producing cGAMP, down-regulates csgD expression and expression of flagellum regulon genes, which leads to the down-regulation of rdar biofilm formation and flagellum-mediated swimming and swarming motility in a temperature-dependent manner (PubMed:30837338). 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 (By similarity). {ECO:0000250|UniProtKB:Q9KVG7, ECO:0000269|PubMed:30837338}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | NP_BIND 110..115; /note=GTP; /evidence=ECO:0000269|PubMed:25865248 |
Features | Beta strand (10); Binding site (5); Chain (1); Helix (19); Metal binding (3); Mutagenesis (2); Nucleotide binding (1); Region (1); Turn (3) |
Keywords | 3D-structure;ATP-binding;Antiviral defense;GTP-binding;Magnesium;Metal-binding;Nucleotide metabolism;Nucleotide-binding;Nucleotidyltransferase;Transferase |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 4XJ6; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 49,276 |
Kinetics | |
Metal Binding | METAL 129; /note="Magnesium"; /evidence="ECO:0000269|PubMed:25865248, ECO:0007744|PDB:4XJ6"; METAL 131; /note="Magnesium"; /evidence="ECO:0000269|PubMed:25865248, ECO:0007744|PDB:4XJ6"; METAL 191; /note="Magnesium"; /evidence="ECO:0000269|PubMed:25865248, ECO:0007744|PDB:4XJ6" |
Rhea ID | RHEA:35647; RHEA:35648 |
Cross Reference Brenda |