EC Number   |
General Information |
Reference |
|---|
   2.7.7.85 | evolution |
cyclic di-AMP (c-di-AMP) is the only second messenger known to be essential for bacterial growth. It is mainly found in Gram-positive bacteria, including pathogenic bacteria like Listeria monocytogenes. CdaA is the sole diadenylate cyclase in Listeria monocytogenes |
-, 761490 |
| 2.7.7.85 | evolution |
enzyme DacZ belongs to the proposed DacZ subfamily, sequence and structure comparisons with other DACs. The adenylate cyclase domains of proteins of the DacZ and DacY/CdaZ classes are found in a similar branch of the tree, which is distinct from other bacterial and archaeal classes, and this branch also contains several bacterial proteins. Homologues are identified in most euryarchaeal species, but no DACs are identified in crenarchaeota |
-, 761855 |
| 2.7.7.85 | 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 |
-, 761397 |
| 2.7.7.85 | malfunction |
a strain that possesses a V76G variation in CdaA produced less c-di-AMP and is highly susceptible to competence-stimulating peptide (CSP). Deletion of cabP and trkH restores the growth of these bacteria in medium with CSP. Peptide and amino acid transport systems are detrimental in c-di-AMP-deficient strains |
-, 761401 |
| 2.7.7.85 | malfunction |
a strain with decreased c-di-AMP levels exhibits an increased cell area in hypo-salt medium, implying impaired osmoregulation. Homologous overexpression of DacZ leads to cell death. Changed intracellular c-di-AMP levels causes increased cell volume in medium with low sodium chloride concentration |
-, 761855 |
| 2.7.7.85 | malfunction |
none of the corresponding genes is essential, but a strain lacking both DisA and CdaA is not viable under standard laboratory conditions |
-, 761397 |
| 2.7.7.85 | malfunction |
reduction of cyclic di-3',5'-adenylate levels by conditional depletion of the di-adenylate cyclase DacA leads to marked decreases in growth rates, both in vitro and in macrophages. Conditional depletion of dacA also leads to increased IFN-beta expression and a concomitant increase in host cell pyroptosis, a result of increased bacteriolysis and subsequent bacterial DNA release |
723084 |
| 2.7.7.85 | malfunction |
the essential role of Tyr187 is confirmed by mutation to Ala, leading to drastic loss of enzymatic activity |
-, 761490 |
| 2.7.7.85 | 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 |
-, 761397 |
| 2.7.7.85 | metabolism |
Listeria monocytogenes relies on the membrane-bound diadenylate cyclase CdaA for c-di-AMP production and degrades the nucleotide with two phosphodiesterases. The extracytoplasmic regulator CdaR interacts with CdaA via its transmembrane helix to modulate c-di-AMP production. The phosphoglucosamine mutase GlmM forms a complex with CdaA and inhibits the diadenylate cyclase activity in vitro. GlmM inhibits c-di-AMP production in Listeria monocytogenes when the bacteria encounter osmotic stress. Thus, GlmM is the major factor controlling the activity of CdaA in vivo. GlmM can be assigned to the class of moonlighting proteins because it is active in metabolism and adjusts the cellularturgor depending on environmental osmolarity. Phosphoglucosamine mutase GlmM is essential for cell wall biosynthesis. CdaA, CdaR and GlmM form a complex in vivo |
-, 760995 |
