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Literature summary for 2.7.7.85 extracted from
- Making and breaking of an essential poison the cyclases and phosphodiesterases that produce and degrade the essential second messenger cyclic di-AMP in bacteria (2019), J. Bacteriol., 201, e00462-18 .
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Bacillus subtilis |  |
| Mg2+ | required | Streptococcus pneumoniae | |
| Mg2+ | required | Listeria monocytogenes EGD | |
| Mg2+ | required | Staphylococcus aureus | |
| Mg2+ | required | Mycoplasma pneumoniae | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 ATP | Bacillus subtilis | - |
2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | Streptococcus pneumoniae | - |
2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | Listeria monocytogenes EGD | - |
2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | Staphylococcus aureus | - |
2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | Mycoplasma pneumoniae | - |
2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | Listeria monocytogenes EGD EGD-e | - |
2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | Bacillus subtilis 168 | - |
2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | Mycoplasma pneumoniae M129 | - |
2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | Listeria monocytogenes EGD ATCC BAA-679 | - |
2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | Mycoplasma pneumoniae ATCC 29342 | - |
2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | A0A6M3Z9Z6 | - |
- |
| Bacillus subtilis | O31854 | - |
- |
| Bacillus subtilis | P37573 | - |
- |
| Bacillus subtilis 168 | A0A6M3Z9Z6 | - |
- |
| Bacillus subtilis 168 | O31854 | - |
- |
| Bacillus subtilis 168 | P37573 | - |
- |
| Listeria monocytogenes EGD | Q8Y5E4 | - |
- |
| Listeria monocytogenes EGD ATCC BAA-679 | Q8Y5E4 | - |
- |
| Listeria monocytogenes EGD EGD-e | Q8Y5E4 | - |
- |
| Mycoplasma pneumoniae | P75528 | - |
- |
| Mycoplasma pneumoniae ATCC 29342 | P75528 | - |
- |
| Mycoplasma pneumoniae M129 | P75528 | - |
- |
| Staphylococcus aureus | Q9RL70 | - |
- |
| Streptococcus pneumoniae | A0A0B7L730 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 ATP | - |
Bacillus subtilis | 2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | - |
Streptococcus pneumoniae | 2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | - |
Listeria monocytogenes EGD | 2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | - |
Staphylococcus aureus | 2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | - |
Mycoplasma pneumoniae | 2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | - |
Listeria monocytogenes EGD EGD-e | 2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | - |
Bacillus subtilis 168 | 2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | - |
Mycoplasma pneumoniae M129 | 2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | - |
Listeria monocytogenes EGD ATCC BAA-679 | 2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
| 2 ATP | - |
Mycoplasma pneumoniae ATCC 29342 | 2 diphosphate + cyclic di-3',5'-adenylate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CdaA | - |
Listeria monocytogenes EGD |
| CdaA | - |
Bacillus subtilis |
| CdaA | - |
Staphylococcus aureus |
| CdaS | - |
Bacillus subtilis |
| Cyclic di-AMP synthase | - |
Bacillus subtilis |
| Dac | - |
Streptococcus pneumoniae |
| Dac | - |
Listeria monocytogenes EGD |
| Dac | - |
Bacillus subtilis |
| Dac | - |
Staphylococcus aureus |
| Dac | - |
Mycoplasma pneumoniae |
| dacA | - |
Streptococcus pneumoniae |
| dacA | - |
Listeria monocytogenes EGD |
| dacA | - |
Bacillus subtilis |
| dacA | - |
Staphylococcus aureus |
| DacB | - |
Mycoplasma pneumoniae |
| disA | - |
Bacillus subtilis |
| DNA integrity scanning protein DisA | - |
Bacillus subtilis |
| ybbP | - |
Streptococcus pneumoniae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | most bacteria possess only one diadenylate cyclase, either CdaA or DisA. In contrast, the spore-forming Gram-positive model organism Bacillus subtilis has the three enzymes, DisA, CdaA, and CdaS. The presence of three diadenylate cyclases is limited to members of the spore-forming genus Bacillus | Bacillus subtilis |
| malfunction | none of the corresponding genes is essential, but a strain lacking both DisA and CdaA is not viable under standard laboratory conditions | Bacillus subtilis |
| metabolism | CdaS is unable to replace the other enzymes since it is expressed only late during sporulation in the forespore but not in growing cells | Bacillus subtilis |
| additional information | the DAC domain is essential for activity | Bacillus subtilis |
| additional information | the DAC domain is essential for activity | Streptococcus pneumoniae |
| additional information | the DAC domain is essential for activity | Listeria monocytogenes EGD |
| additional information | the DAC domain is essential for activity | Staphylococcus aureus |
| additional information | the DAC domain is essential for activity | Mycoplasma pneumoniae |
| physiological function | in the diadenylate cyclases, one type of catalytic domain, the diadenylate cyclase (DAC) domain, is coupled to various other domains that control the localization, the protein-protein interactions, and the regulation of the enzymes | Streptococcus pneumoniae |
| physiological function | in the diadenylate cyclases, one type of catalytic domain, the diadenylate cyclase (DAC) domain, is coupled to various other domains that control the localization, the protein-protein interactions, and the regulation of the enzymes | Listeria monocytogenes EGD |
| physiological function | in the diadenylate cyclases, one type of catalytic domain, the diadenylate cyclase (DAC) domain, is coupled to various other domains that control the localization, the protein-protein interactions, and the regulation of the enzymes | Staphylococcus aureus |
| physiological function | in the diadenylate cyclases, one type of catalytic domain, the diadenylate cyclase (DAC) domain, is coupled to various other domains that control the localization, the protein-protein interactions, and the regulation of the enzymes | Mycoplasma pneumoniae |
| physiological function | in the diadenylate cyclases, one type of catalytic domain, the diadenylate cyclase (DAC) domain, is coupled to various other domains that control the localization, the protein-protein interactions, and the regulation of the enzymes. None of the corresponding genes is essential | Bacillus subtilis |
| physiological function | in the diadenylate cyclases, one type of catalytic domain, the diadenylate cyclase (DAC) domain, is coupled to various other domains that control the localization, the protein-protein interactions, and the regulation of the enzymes. None of the corresponding genes is essential. CdaS is unable to replace the other enzymes since it is expressed only late during sporulation in the forespore but not in growing cells | Bacillus subtilis |
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