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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
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
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
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
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
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
malfunction
none of the corresponding genes is essential, but a strain lacking both DisA and CdaA is not viable under standard laboratory conditions
malfunction
the essential role of Tyr187 is confirmed by mutation to Ala, leading to drastic loss of enzymatic activity
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
-
malfunction
Streptococcus pneumoniae serotype 2 D39 NCTC 7466
-
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
-
malfunction
-
none of the corresponding genes is essential, but a strain lacking both DisA and CdaA is not viable under standard laboratory conditions
-
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
-
malfunction
-
the essential role of Tyr187 is confirmed by mutation to Ala, leading to drastic loss of enzymatic activity
-
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
-
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
-
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
-
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
-
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
-
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
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
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
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
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
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
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
metabolism
-
regulation of diadenylate cyclase activity in bacteria, replenishing the cyclic-di-AMP pool, overview. The intracellular pool of c-di-AMP is maintained by the activities of diadenylate cyclase (DAC) and phosphodiesterase (PDE) enzymes, as well as possibly via c-di-AMP export. Transient regulation of DAC enzyme in the CdaA-CdaR-GlmM protein complex
-
physiological function
-
cyclic di-3',5'-adenylate coordinates bacterial growth, cell wall stability, and responses to stress and plays a crucial role in the establishment of bacterial infection
physiological function
the enzyme signals DNA structures that interfere with chromosome segregation cyclic di-3',5'-adenylate. The enzyme activity is unaffected by linear DNA or DNA ends but strongly suppressed by branched nucleic acids such as Holliday junctions
physiological function
the intracellular bacterial pathogen Listeria monocytogenes secretes cyclic di-3',5'-adenylate into the cytosol of the host, where it triggers a cytosolic pathway of innate immunity
physiological function
-
the signaling nucleotide cyclic di-3',5'-adenylate is essential for the viability of Bacillus subtilis. However, excess cyclic di-3',5'-adenylate also harms the cells. The activity of the cyclases is subject to regulation. The activity of the diadenylate cyclases is controlled by distinct molecular mechanisms. Isoenzyme CdaA is stimulated by a regulatory interaction with the CdaR protein. In contrast, the activity of CdaS seems to be intrinsically restricted, and a single amino acid substitution is sufficient to drastically increase the activity of the enzyme
physiological function
enzyme forms a complex with the regulatory protein CdaR and the glucosamine-6-phosphate mutase GlmM. cCaA, cdaR, and GlmM form a gene cluster that is conserved throughout the firmicutes. Data suggest that GlmM and GlmS are involved in the control of cyclic di-AMP synthesis. They convert glutamine and fructose-6-phosphate to glutamate and glucosamine-1-phosphate. Cyclic di-AMP synthesis is enhanced if the cells are grown in the presence of glutamate compared to that in glutamine-grown cells
physiological function
in-frame deletion of the cdaA gene causes decreased cyclic di-AMP levels, increased sensitivity to hydrogen peroxide and increased production of extracellular polysaccharides. More than 200 genes are significantly upregulated or downregulated in the cdaA mutant. Genes with increased or decreased expression are clustered in cellular polysaccharide biosynthetic processes and oxidoreductase activity respectively. The expression of several genomic islands, such as GTFB/C, TnSmu, CRISPR1-Cas and CRISPR2-Cas, is altered in the cdaA mutant
physiological function
introduction of single nucleotide polymorphism G206S into an isogenic highly resistant but slower growing strain reduces resistance and increases its growth rate, suggesting a direct connection between the dacA mutation and the phenotypic differences of these strains. The dacA mutation decreases cyclic di-AMP levels resulting in reduced autolysis, increased salt tolerance and a reduction in the basal expression of the cell wall stress stimulon
physiological function
regulator protein CdaR negatively influences CdaA activity and the role of CdaR is most evident at a high growth temperature. A cdaR mutant strain is less susceptible to lysozyme. CdaA contributes to cell division, and cells depleted of CdaA are prone to lysis. The growth defect of a CdaA depletion strain can be partially restored by increasing the osmolarity of the growth medium
physiological function
-
the mutation I154F in phosphoglucosamine mutase gene GlmM results in a lowering of the cyclic di-AMP level and a reduction in the key peptidoglycan precursor UDP-N-acetylglucosamine. Cyclic di-AMP synthesis by CdaA is inhibited by GlmM mutant I154F more than GlmM and GlmM mutant I154F binds more strongly to CdaA than GlmM. Mutations in the cdaA restore osmoresistance in phosphodiesterase gdpP-defective mutants
physiological function
transcription of CdaS is initiated by the sporulation-specific sigma factor sigma(H) and the deletion of CdaS significantly delays sporulation and parasporal crystal formation. Deletion of all the three diadenylate cyclase genes from a single strain is unsuccessful
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
physiological function
c-di-AMP is synthesized by diadenylate cyclases from two molecules of ATP. The second messenger cyclic di-AMP (c-di-AMP) is essential for growth of many bacteria because it controls osmolyte homeostasis. c-di-AMP can regulate the synthesis of potassium uptake systems in some bacteria and it also directly inhibits and activates potassium import and export systems, respectively. Therefore, c-di-AMP production and degradation have to be tightly regulated depending on the environmental osmolarity. 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 cellular turgor depending on environmental osmolarity. CdaA, CdaR and GlmM form a complex in vivo
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
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
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
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
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
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
physiological function
Streptococcus pneumoniae encodes an essential diadenylate cyclase, CdaA, c-di-AMP is produced by diadenylate cyclase, CdaA, and cleaved by phosphodiesterases Pde1 and Pde2. c-di-AMP binds a transporter of K+ (Trk) family protein, CabP, which subsequently halts K+ uptake via the transporter TrkH. The c-di-AMP-binding protein, CabP, is a mediator of potassium uptake and c-di-AMP homeostasis. c-di-AMP homeostasis must be maintained for competence program integrity. A DELTApde1 DELTApde2 strain exhibits reduced transformation efficiency compared to wild-type bacteria, which is c-di-AMP dependent. Transformation efficiency was also directly related to the [K+] in the medium, suggesting a link between c-di-AMP function and the pneumococcal competence state. Role for c-di-AMP in the competence program of Streptococcus pneumoniae. c-di-AMP affects the pneumococcal transcriptome, and c-di-AMP affects transformation, responsiveness to CSP, and growth under stress conditions, detailed overview. c-di-AMP influences the competence program of Streptococcus pneumoniae partly through modulating K+ uptake. c-di-AMP signaling can mediate pneumococcal survival under several environmental conditions, including differential pH and glycine concentrations
physiological function
the DAC encoding gene (dacZ) is essential, but homologous overexpression of DacZ leads to cell death, suggesting the need for tight regulation of c-di-AMP levels. A central target of c-di-AMP signaling in bacteria is cellular osmohomeostasis and a comparable function in euryarchaeon Haloferax volcanii is suggested. Osmoregulation is likely to be a common function of c-di-AMP in bacteria and archaea
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
the DAC encoding gene (dacZ) is essential, but homologous overexpression of DacZ leads to cell death, suggesting the need for tight regulation of c-di-AMP levels. A central target of c-di-AMP signaling in bacteria is cellular osmohomeostasis and a comparable function in euryarchaeon Haloferax volcanii is suggested. Osmoregulation is likely to be a common function of c-di-AMP in bacteria and archaea
-
physiological function
Streptococcus pneumoniae serotype 2 D39 NCTC 7466
-
Streptococcus pneumoniae encodes an essential diadenylate cyclase, CdaA, c-di-AMP is produced by diadenylate cyclase, CdaA, and cleaved by phosphodiesterases Pde1 and Pde2. c-di-AMP binds a transporter of K+ (Trk) family protein, CabP, which subsequently halts K+ uptake via the transporter TrkH. The c-di-AMP-binding protein, CabP, is a mediator of potassium uptake and c-di-AMP homeostasis. c-di-AMP homeostasis must be maintained for competence program integrity. A DELTApde1 DELTApde2 strain exhibits reduced transformation efficiency compared to wild-type bacteria, which is c-di-AMP dependent. Transformation efficiency was also directly related to the [K+] in the medium, suggesting a link between c-di-AMP function and the pneumococcal competence state. Role for c-di-AMP in the competence program of Streptococcus pneumoniae. c-di-AMP affects the pneumococcal transcriptome, and c-di-AMP affects transformation, responsiveness to CSP, and growth under stress conditions, detailed overview. c-di-AMP influences the competence program of Streptococcus pneumoniae partly through modulating K+ uptake. c-di-AMP signaling can mediate pneumococcal survival under several environmental conditions, including differential pH and glycine concentrations
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
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
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
introduction of single nucleotide polymorphism G206S into an isogenic highly resistant but slower growing strain reduces resistance and increases its growth rate, suggesting a direct connection between the dacA mutation and the phenotypic differences of these strains. The dacA mutation decreases cyclic di-AMP levels resulting in reduced autolysis, increased salt tolerance and a reduction in the basal expression of the cell wall stress stimulon
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
the signaling nucleotide cyclic di-3',5'-adenylate is essential for the viability of Bacillus subtilis. However, excess cyclic di-3',5'-adenylate also harms the cells. The activity of the cyclases is subject to regulation. The activity of the diadenylate cyclases is controlled by distinct molecular mechanisms. Isoenzyme CdaA is stimulated by a regulatory interaction with the CdaR protein. In contrast, the activity of CdaS seems to be intrinsically restricted, and a single amino acid substitution is sufficient to drastically increase the activity of the enzyme
-
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
-
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
-
physiological function
-
enzyme forms a complex with the regulatory protein CdaR and the glucosamine-6-phosphate mutase GlmM. cCaA, cdaR, and GlmM form a gene cluster that is conserved throughout the firmicutes. Data suggest that GlmM and GlmS are involved in the control of cyclic di-AMP synthesis. They convert glutamine and fructose-6-phosphate to glutamate and glucosamine-1-phosphate. Cyclic di-AMP synthesis is enhanced if the cells are grown in the presence of glutamate compared to that in glutamine-grown cells
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
regulator protein CdaR negatively influences CdaA activity and the role of CdaR is most evident at a high growth temperature. A cdaR mutant strain is less susceptible to lysozyme. CdaA contributes to cell division, and cells depleted of CdaA are prone to lysis. The growth defect of a CdaA depletion strain can be partially restored by increasing the osmolarity of the growth medium
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
transcription of CdaS is initiated by the sporulation-specific sigma factor sigma(H) and the deletion of CdaS significantly delays sporulation and parasporal crystal formation. Deletion of all the three diadenylate cyclase genes from a single strain is unsuccessful
-
physiological function
-
the DAC encoding gene (dacZ) is essential, but homologous overexpression of DacZ leads to cell death, suggesting the need for tight regulation of c-di-AMP levels. A central target of c-di-AMP signaling in bacteria is cellular osmohomeostasis and a comparable function in euryarchaeon Haloferax volcanii is suggested. Osmoregulation is likely to be a common function of c-di-AMP in bacteria and archaea
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
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
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
c-di-AMP is synthesized by diadenylate cyclases from two molecules of ATP. The second messenger cyclic di-AMP (c-di-AMP) is essential for growth of many bacteria because it controls osmolyte homeostasis. c-di-AMP can regulate the synthesis of potassium uptake systems in some bacteria and it also directly inhibits and activates potassium import and export systems, respectively. Therefore, c-di-AMP production and degradation have to be tightly regulated depending on the environmental osmolarity. 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 cellular turgor depending on environmental osmolarity. CdaA, CdaR and GlmM form a complex in vivo
-
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
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
the DAC encoding gene (dacZ) is essential, but homologous overexpression of DacZ leads to cell death, suggesting the need for tight regulation of c-di-AMP levels. A central target of c-di-AMP signaling in bacteria is cellular osmohomeostasis and a comparable function in euryarchaeon Haloferax volcanii is suggested. Osmoregulation is likely to be a common function of c-di-AMP in bacteria and archaea
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
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
-
physiological function
-
in-frame deletion of the cdaA gene causes decreased cyclic di-AMP levels, increased sensitivity to hydrogen peroxide and increased production of extracellular polysaccharides. More than 200 genes are significantly upregulated or downregulated in the cdaA mutant. Genes with increased or decreased expression are clustered in cellular polysaccharide biosynthetic processes and oxidoreductase activity respectively. The expression of several genomic islands, such as GTFB/C, TnSmu, CRISPR1-Cas and CRISPR2-Cas, is altered in the cdaA mutant
-
physiological function
-
the DAC encoding gene (dacZ) is essential, but homologous overexpression of DacZ leads to cell death, suggesting the need for tight regulation of c-di-AMP levels. A central target of c-di-AMP signaling in bacteria is cellular osmohomeostasis and a comparable function in euryarchaeon Haloferax volcanii is suggested. Osmoregulation is likely to be a common function of c-di-AMP in bacteria and archaea
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
the DAC encoding gene (dacZ) is essential, but homologous overexpression of DacZ leads to cell death, suggesting the need for tight regulation of c-di-AMP levels. A central target of c-di-AMP signaling in bacteria is cellular osmohomeostasis and a comparable function in euryarchaeon Haloferax volcanii is suggested. Osmoregulation is likely to be a common function of c-di-AMP in bacteria and archaea
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
the DAC encoding gene (dacZ) is essential, but homologous overexpression of DacZ leads to cell death, suggesting the need for tight regulation of c-di-AMP levels. A central target of c-di-AMP signaling in bacteria is cellular osmohomeostasis and a comparable function in euryarchaeon Haloferax volcanii is suggested. Osmoregulation is likely to be a common function of c-di-AMP in bacteria and archaea
-
physiological function
-
the DAC encoding gene (dacZ) is essential, but homologous overexpression of DacZ leads to cell death, suggesting the need for tight regulation of c-di-AMP levels. A central target of c-di-AMP signaling in bacteria is cellular osmohomeostasis and a comparable function in euryarchaeon Haloferax volcanii is suggested. Osmoregulation is likely to be a common function of c-di-AMP in bacteria and archaea
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
physiological function
-
a broadly conserved second messenger is cyclic-di-AMP (c-di-AMP) which regulates a range of processes including cell wall homeostasis, potassium uptake, DNA repair, fatty acid synthesis, biofilm formation and central metabolism in bacteria. Regulators of the membrane-bound enzyme CdaA are the membrane-bound CdaR and the phosphoglucosamine mutase GlmM which both bind directly to the DAC
-
additional information
flexibility of tyrosine 187 side chain involved in locking the adenine ring after ATP binding, residue Y187 is essential for enzyme activity. Structure analysis of the active site of dimeric CdaA with bound c-di-AMP, overview. In the monomeric CdaA-AMP complex, the tyrosine is rotated inward at the active site and stacks on the adenine in an almost coplanar orientation. In contrast, in the dimeric c-di-AMP complex, the tyrosine side chain is flipped outward, as the Thr202 side chain of the other subunit packs against the adenine ring
additional information
the DAC domain is essential for activity
additional information
the DAC domain is essential for activity
additional information
the DAC domain is essential for activity
additional information
the DAC domain is essential for activity
additional information
the DAC domain is essential for activity
additional information
the DAC domain is essential for activity
additional information
the DAC domain is essential for activity
additional information
-
the DAC domain is essential for activity
-
additional information
-
the DAC domain is essential for activity
-
additional information
-
the DAC domain is essential for activity
-
additional information
-
the DAC domain is essential for activity
-
additional information
-
flexibility of tyrosine 187 side chain involved in locking the adenine ring after ATP binding, residue Y187 is essential for enzyme activity. Structure analysis of the active site of dimeric CdaA with bound c-di-AMP, overview. In the monomeric CdaA-AMP complex, the tyrosine is rotated inward at the active site and stacks on the adenine in an almost coplanar orientation. In contrast, in the dimeric c-di-AMP complex, the tyrosine side chain is flipped outward, as the Thr202 side chain of the other subunit packs against the adenine ring
-
additional information
-
the DAC domain is essential for activity
-
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?
x * 43000, SDS-PAGE
?
x * 41100, calculated from sequence
?
-
x * 43000, SDS-PAGE
-
?
-
x * 41100, calculated from sequence
-
dimer
2 * 23000, calculated, plus hexamer and monomer
dimer
-
2 * 23000, calculated, plus hexamer and monomer
-
hexamer
6 * 23000, calculated, plus monomer and dimer
hexamer
-
6 * 23000, calculated, plus monomer and dimer
-
hexamer
6 * 22000, SDS-PAGe, 6 * 23300, calculated
hexamer
-
6 * 22000, SDS-PAGe, 6 * 23300, calculated
-
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
the CdaA-CdaA dimer interface buries about 605 A2 of the accessible surface area (7.3%) and is stabilized by six hydrogen bonds and two salt bridges. Additional interactions between the monomers are mediated by the ligand bound to the active site
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the CdaA-CdaA dimer interface buries about 605 A2 of the accessible surface area (7.3%) and is stabilized by six hydrogen bonds and two salt bridges. Additional interactions between the monomers are mediated by the ligand bound to the active site
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
homodimer
-
the dimer-forming CdaA contains three transmembrane domains with the DAC domain (Dis_N Pfam PF02457) located intracellularly, while CdaR contains one transmembrane domain and several YbbR domains (Pfam PF07949) predicted to be located extracellularly
-
monomer
1 * 23000, calculated, plus hexamer and dimer
monomer
-
1 * 23000, calculated, plus hexamer and dimer
-
octamer
8 * 42900
octamer
8 * 42000, calculated
octamer
-
8 * 42000, calculated
-
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
enzyme CdaA contains three transmembrane domains (TM) and a diadenylate cyclase domain (DAC) that is surrounded by coiled-coil (CC) domains
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
enzyme CdaA contains three transmembrane domains (TM) and a diadenylate cyclase domain (DAC) that is surrounded by coiled-coil (CC) domains
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
-
additional information
-
the DAC enzyme is organized in the CdaA-CdaR-GlmM protein complex
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Zheng, C.; Wang, J.; Luo, Y.; Fu, Y.; Su, J.; He, J.
Highly efficient enzymatic preparation of c-di-AMP using the diadenylate cyclase DisA from Bacillus thuringiensis
Enzyme Microb. Technol.
52
319-324
2013
Bacillus thuringiensis (D5TM67), Bacillus thuringiensis, Bacillus thuringiensis BMB171 (D5TM67)
brenda
Mehne, F.M.; Gunka, K.; Eilers, H.; Herzberg, C.; Kaever, V.; Stuelke, J.
Cyclic di-AMP homeostasis in Bacillus subtilis: both lack and high level accumulation of the nucleotide are detrimental for cell growth
J. Biol. Chem.
288
2004-2017
2013
Bacillus subtilis, Bacillus subtilis 168
brenda
Witte, C.E.; Whiteley, A.T.; Burke, T.P.; Sauer, J.D.; Portnoy, D.A.; Woodward, J.J.
Cyclic di-AMP is critical for Listeria monocytogenes growth, cell wall homeostasis, and establishment of infection
mBio
4
e00282-13
2013
Listeria monocytogenes
brenda
Witte, G.; Hartung, S.; Buettner, K.; Hopfner, K.P.
Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates
Mol. Cell
30
167-178
2008
Bacillus subtilis (P37573), Bacillus subtilis, Thermotoga maritima (Q9WY43)
brenda
Woodward, J.; Lavarone, A.; Portnoy, D.
C-di-AMP secreted by intracellular Listeria monocytogenes activates a host type I interferon response
Science
328
1703-1705
2010
Listeria monocytogenes (Q8Y5E4)
brenda
Mueller, M.; Deimling, T.; Hopfner, K.P.; Witte, G.
Structural analysis of the diadenylate cyclase reaction of DNA-integrity scanning protein A (DisA) and its inhibition by 3-dATP
Biochem. J.
469
367-374
2015
Thermotoga maritima (Q9WY43), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9WY43)
brenda
Cheng, X.; Zheng, X.; Zhou, X.; Zeng, J.; Ren, Z.; Xu, X.; Cheng, L.; Li, M.; Li, J.; Li, Y.
Regulation of oxidative response and extracellular polysaccharide synthesis by a diadenylate cyclase in Streptococcus mutans
Environ. Microbiol.
18
904-922
2016
Streptococcus mutans (Q8DTC4), Streptococcus mutans, Streptococcus mutans UA159 (Q8DTC4)
brenda
Zheng, C.; Ma, Y.; Wang, X.; Xie, Y.; Ali, M.K.; He, J.
Functional analysis of the sporulation-specific diadenylate cyclase CdaS in Bacillus thuringiensis
Front. Microbiol.
6
908
2015
Bacillus thuringiensis (D5TM67), Bacillus thuringiensis, Bacillus thuringiensis BMB171 (D5TM67)
brenda
Gundlach, J.; Mehne, F.M.; Herzberg, C.; Kampf, J.; Valerius, O.; Kaever, V.; Stuelke, J.
An essential poison: synthesis and degradation of cyclic di-AMP in Bacillus subtilis
J. Bacteriol.
197
3265-3274
2015
Bacillus subtilis (Q45589), Bacillus subtilis, Bacillus subtilis 168 (Q45589)
brenda
Rismondo, J.; Gibhardt, J.; Rosenberg, J.; Kaever, V.; Halbedel, S.; Commichau, F.M.
Phenotypes associated with the essential diadenylate cyclase CdaA and its potential regulator CdaR in the human pathogen Listeria monocytogenes
J. Bacteriol.
198
416-426
2016
Listeria monocytogenes (Q8Y5E4), Listeria monocytogenes, Listeria monocytogenes ATCC BAA-679 (Q8Y5E4)
brenda
Mehne, F.M.; Schroeder-Tittmann, K.; Eijlander, R.T.; Herzberg, C.; Hewitt, L.; Kaever, V.; Lewis, R.J.; Kuipers, O.P.; Tittmann, K.; Stuelke, J.
Control of the diadenylate cyclase CdaS in Bacillus subtilis: an autoinhibitory domain limits cyclic di-AMP production
J. Biol. Chem.
289
21098-21107
2014
Bacillus subtilis (O31854), Bacillus subtilis, Bacillus subtilis 168 (O31854)
brenda
Rosenberg, J.; Dickmanns, A.; Neumann, P.; Gunka, K.; Arens, J.; Kaever, V.; Stuelke, J.; Ficner, R.; Commichau, F.M.
Structural and biochemical analysis of the essential diadenylate cyclase CdaA from Listeria monocytogenes
J. Biol. Chem.
290
6596-6606
2015
Listeria monocytogenes (Q8Y5E4), Listeria monocytogenes, Listeria monocytogenes ATCC BAA-679 (Q8Y5E4)
brenda
Zhu, Y.; Pham, T.H.; Nhiep, T.H.; Vu, N.M.; Marcellin, E.; Chakrabortti, A.; Wang, Y.; Waanders, J.; Lo, R.; Huston, W.M.; Bansal, N.; Nielsen, L.K.; Liang, Z.X.; Turner, M.S.
Cyclic-di-AMP synthesis by the diadenylate cyclase CdaA is modulated by the peptidoglycan biosynthesis enzyme GlmM in Lactococcus lactis
Mol. Microbiol.
99
1015-1027
2016
Lactococcus lactis
brenda
Dengler, V.; McCallum, N.; Kiefer, P.; Christen, P.; Patrignani, A.; Vorholt, J.A.; Berger-Baechi, B.; Senn, M.M.
Mutation in the C-di-AMP cyclase dacA affects fitness and resistance of methicillin resistant Staphylococcus aureus
PLoS ONE
8
e73512
2013
Staphylococcus aureus (Q2FW92), Staphylococcus aureus, Staphylococcus aureus NCTC 8325 (Q2FW92)
brenda
Opoku-Temeng, C.; Sintim, H.O.
Inhibition of cyclic diadenylate cyclase, DisA, by polyphenols
Sci. Rep.
6
25445
2016
Bacillus subtilis
brenda
Pham, T.H.; Liang, Z.X.; Marcellin, E.; Turner, M.S.
Replenishing the cyclic-di-AMP pool regulation of diadenylate cyclase activity in bacteria
Curr. Genet.
62
731-738
2016
Streptococcus pneumoniae (A0A0B7L730), Clostridium botulinum (A0A0C2N691), Bacillus amyloliquefaciens (A0A0D7XMK3), Clostridium perfringens (A0A0H2YU52), Lacticaseibacillus rhamnosus (A0A2A5L6R6), Bacillus anthracis (A0A2A8KZ47), Streptococcus equi subsp. zooepidemicus (A0A2X3T317), Enterococcus faecalis (A0A2Z6BU13), Clostridium novyi (A0PXZ3), Lactococcus cremoris (A2RIF7), Lactococcus cremoris (Q031P4), Clostridium ljungdahlii (D8GIJ7), Tetragenococcus halophilus (G4L7W3), Streptococcus pyogenes serotype M2 (Q1JH51), Staphylococcus aureus (Q2FW92), Bacillus subtilis (Q45589), Lactobacillus acidophilus (Q5FL37), Bacillus licheniformis (Q65P49), Geobacter sulfurreducens (Q74EU1), Streptococcus mutans serotype c (Q8DTC4), Listeria monocytogenes EGD (Q8Y5E4), Tetragenococcus halophilus JCM 20259 (G4L7W3), Listeria monocytogenes EGD EGD-e (Q8Y5E4), Lactococcus cremoris Sk11 (Q031P4), Staphylococcus aureus NCTC 8325 (Q2FW92), Bacillus subtilis 168 (Q45589), Tetragenococcus halophilus DSM 20338 (G4L7W3), Tetragenococcus halophilus NCIMB 9735 (G4L7W3), Clostridium ljungdahlii DSM 13528 (D8GIJ7), Bacillus licheniformis NCIMB 9375 (Q65P49), Enterococcus faecalis ERV62 (A0A2Z6BU13), Bacillus licheniformis Gibson 46 (Q65P49), Clostridium novyi NT (A0PXZ3), Clostridium perfringens NCIMB 6125 (A0A0H2YU52), Clostridium perfringens NCTC 8237 (A0A0H2YU52), Clostridium perfringens JCM 1290 (A0A0H2YU52), Bacillus licheniformis JCM 2505 (Q65P49), Streptococcus mutans serotype c ATCC 700610 (Q8DTC4), Tetragenococcus halophilus NBRC 12172 (G4L7W3), Lactococcus cremoris MG1363 (A2RIF7), Lactobacillus acidophilus NCFM (Q5FL37), Streptococcus pyogenes serotype M2 MGAS10270 (Q1JH51), Bacillus licheniformis NRRL NRS-1264 (Q65P49), Clostridium perfringens type A (A0A0H2YU52), Lacticaseibacillus rhamnosus ATCC 8530 (A0A2A5L6R6), Geobacter sulfurreducens PCA (Q74EU1), Clostridium ljungdahlii PETC (D8GIJ7), Streptococcus pneumoniae ATCC 700669 (A0A0B7L730), Listeria monocytogenes EGD ATCC BAA-679 (Q8Y5E4), Lactobacillus acidophilus ATCC 700396 (Q5FL37), Geobacter sulfurreducens ATCC 51573 (Q74EU1), Lactobacillus acidophilus NCK56 (Q5FL37), Clostridium perfringens DSM 756 (A0A0H2YU52), Bacillus licheniformis NBRC 12200 (Q65P49), Staphylococcus aureus PS 47 (Q2FW92), Bacillus licheniformis ATCC 14580 (Q65P49), Lactobacillus acidophilus N2 (Q5FL37), Streptococcus mutans serotype c UA159 (Q8DTC4), Bacillus licheniformis DSM 13 (Q65P49), Clostridium ljungdahlii ATCC 55383 (D8GIJ7), Geobacter sulfurreducens DSM 12127 (Q74EU1)
brenda
Gibhardt, J.; Heidemann, J.L.; Bremenkamp, R.; Rosenberg, J.; Seifert, R.; Kaever, V.; Ficner, R.; Commichau, F.M.
An extracytoplasmic protein and a moonlighting enzyme modulate synthesis of c-di-AMP in Listeria monocytogenes
Environ. Microbiol.
22
2771-2791
2020
Listeria monocytogenes EGD (Q8Y5E4), Listeria monocytogenes EGD ATCC BAA-679 (Q8Y5E4)
brenda
Commichau, F.M.; Heidemann, J.L.; Ficner, R.; Stuelke, J.
Making and breaking of an essential poison the cyclases and phosphodiesterases that produce and degrade the essential second messenger cyclic di-AMP in bacteria
J. Bacteriol.
201
e00462-18
2019
Streptococcus pneumoniae (A0A0B7L730), Bacillus subtilis (A0A6M3Z9Z6), Bacillus subtilis (O31854), Bacillus subtilis (P37573), Mycoplasma pneumoniae (P75528), Listeria monocytogenes EGD (Q8Y5E4), Staphylococcus aureus (Q9RL70), Listeria monocytogenes EGD EGD-e (Q8Y5E4), Bacillus subtilis 168 (A0A6M3Z9Z6), Bacillus subtilis 168 (O31854), Bacillus subtilis 168 (P37573), Mycoplasma pneumoniae M129 (P75528), Listeria monocytogenes EGD ATCC BAA-679 (Q8Y5E4), Mycoplasma pneumoniae ATCC 29342 (P75528)
brenda
Zarrella, T.M.; Yang, J.; Metzger, D.W.; Bai, G.
Bacterial second messenger cyclic di-AMP modulates the competence state in Streptococcus pneumoniae
J. Bacteriol.
202
e00691-19
2020
Streptococcus pneumoniae serotype 2 D39 (A0A0H2ZPG9), Streptococcus pneumoniae serotype 2 D39 NCTC 7466 (A0A0H2ZPG9)
brenda
Heidemann, J.L.; Neumann, P.; Dickmanns, A.; Ficner, R.
Crystal structures of the c-di-AMP-synthesizing enzyme CdaA
J. Biol. Chem.
294
10463-10470
2019
Listeria monocytogenes EGD (Q8Y5E4), Listeria monocytogenes EGD ATCC BAA-679 (Q8Y5E4)
brenda
Braun, F.; Thomalla, L.; van der Does, C.; Quax, T.E.F.; Allers, T.; Kaever, V.; Albers, S.V.
Cyclic nucleotides in archaea cyclic di-AMP in the archaeon Haloferax volcanii and its putative role
MicrobiologyOpen
8
e00829
2019
Haloferax volcanii (D4GZM5), Haloferax volcanii, Haloferax volcanii NCIMB 2012 (D4GZM5), Haloferax volcanii JCM 8879 (D4GZM5), Haloferax volcanii DS2 (D4GZM5), Haloferax volcanii DSM 3757 (D4GZM5), Haloferax volcanii ATCC 29605 (D4GZM5), Haloferax volcanii NBRC 14742 (D4GZM5), Haloferax volcanii VKM B-1768 (D4GZM5)
brenda