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UniProt functional annotation for Q45589 | ||
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| UniProt code: Q45589. |
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| Organism: | |
Bacillus subtilis (strain 168). |
| Taxonomy: | |
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. |
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| Function: | |
One of 3 paralogous diadenylate cyclases (DAC) in this bacteria, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (Probable). Upon expression in E.coli leads to c-di- AMP synthesis (PubMed:23192352). Probably the main producer of c-di-AMP for the cell; is probably implicated in control of peptidogylcan synthesis (PubMed:22211522, PubMed:23192352, PubMed:26240071). In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess (PubMed:26240071). {ECO:0000269|PubMed:23192352, ECO:0000269|PubMed:26240071, ECO:0000305|PubMed:22211522}. |
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| Catalytic activity: | |
Reaction=2 ATP = 3',3'-c-di-AMP + 2 diphosphate; Xref=Rhea:RHEA:35655, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:71500; EC=2.7.7.85; Evidence={ECO:0000255|HAMAP-Rule:MF_01499}; |
| Activity regulation: | |
DAC activity is stimulated about 20-fold in E.coli by coexpression with CdaR (PubMed:23192352). {ECO:0000269|PubMed:23192352}. |
| Subunit: | |
Probably a homodimer (By similarity). Interacts with CdaR (PubMed:23192352, PubMed:26240071). May interact with GlmM (PubMed:26240071). {ECO:0000255|HAMAP-Rule:MF_01499, ECO:0000269|PubMed:23192352, ECO:0000269|PubMed:26240071}. |
| Subcellular location: | |
Cell membrane {ECO:0000255|HAMAP-Rule:MF_01499, ECO:0000269|PubMed:26240071}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01499}. |
| Induction: | |
Constitutively expressed, part of the cdaA-cdaR-glmM-glmS operon (PubMed:23192352). {ECO:0000269|PubMed:23192352}. |
| Disruption phenotype: | |
Increased sensitivity to the beta-lactam antibiotic cefuroxime (CEF), upon overexpression of the c-di-AMP phosphodiesterase GdpP greatly increased sensitivity to CEF (PubMed:22211522). Double disA-cdaA mutants cannot be made, suggesting they are lethal, while double disA-cdaS and cdaA-cdaS mutants are viable (PubMed:22211522, PubMed:23192352). Depletion of cdaA in double disA-cdaA deletion cells leads to cell lysis (PubMed:22211522). Exponentially growing cells are extremely sensitive to H(2)O(2), no change in response to methyl methanesulfonate (PubMed:25616256). {ECO:0000269|PubMed:22211522, ECO:0000269|PubMed:23192352, ECO:0000269|PubMed:25616256}. |
| Similarity: | |
Belongs to the adenylate cyclase family. DacA/CdaA subfamily. {ECO:0000255|HAMAP-Rule:MF_01499}. |
Annotations taken from UniProtKB at the EBI.