The enzyme, characterized from the Gram-positive bacterium Staphylococcus aureus, is a cytoplasmic protein that contains a DHH/DHHA1 domain. It can act on cyclic di-3',5'-adenylate with a much lower activity (cf. EC 3.1.4.59, cyclic-di-AMP phosphodiesterase). Activity requires Mn2+ and is inhibited by ppGpp.
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The enzyme appears in viruses and cellular organisms
The enzyme, characterized from the Gram-positive bacterium Staphylococcus aureus, is a cytoplasmic protein that contains a DHH/DHHA1 domain. It can act on cyclic di-3',5'-adenylate with a much lower activity (cf. EC 3.1.4.59, cyclic-di-AMP phosphodiesterase). Activity requires Mn2+ and is inhibited by ppGpp.
DhhP is essential for Borrelia burgdorferi growth both in vitro and in the mammalian host. The conditional DhhP mutant has a dramatic increase in intracellular c-di-AMP level in comparison to the isogenic wild-type strain. Elevated cellular c-di-AMP in Borrelia burgdorferi does not result in an increased resistance to beta-lactamase antibiotics. The DhhP mutant is defective in induction of the sigmaS factor, RpoS, and the RpoS-dependent outer membrane virulence factor OspC
deficiency of Pde significantly enhances intracellular C12-C20 fatty acid accumulation. Superfluous c-di-AMP in Mycobacterium smegmatis may lead to abnormal colonial morphology
deletion of either isoform Pde1 or Pde2 results in a moderate increase of the c-di-AMP levels compared with the parental strain. Deletion of both genes results in an up to 4fold increase in c-di-AMP levels compared to that of the parental strain. Both Pde1 and Pde2 play a role in pneumococcal growth. Deletion of either isoform Pde1 or Pde2 reduces the growth rate slightly, and the double mutant synergizes the reduction
a Pde2 mutant strain displays a growth defect in the early growth phase. The mutant displays an increase in cellular c-di-AMP and 5'-O-phosphonoadenylyl-(3'->5')-adenosine levels and increased oxacillin resistance. A strain producing a high level of c-di-AMP has increased and a stain producing low levels has decreased acid resistance
DhhP is essential for Borrelia burgdorferi growth both in vitro and in the mammalian host. The conditional DhhP mutant has a dramatic increase in intracellular c-di-AMP level in comparison to the isogenic wild-type strain. Elevated cellular c-di-AMP in Borrelia burgdorferi does not result in an increased resistance to beta-lactamase antibiotics. The DhhP mutant is defective in induction of the sigmaS factor, RpoS, and the RpoS-dependent outer membrane virulence factor OspC
deficiency of Pde significantly enhances intracellular C12-C20 fatty acid accumulation. Superfluous c-di-AMP in Mycobacterium smegmatis may lead to abnormal colonial morphology
a Pde2 mutant strain displays a growth defect in the early growth phase. The mutant displays an increase in cellular c-di-AMP and 5'-O-phosphonoadenylyl-(3'->5')-adenosine levels and increased oxacillin resistance. A strain producing a high level of c-di-AMP has increased and a stain producing low levels has decreased acid resistance
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physiological function
Streptococcus pneumoniae serotype 2 D39
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deletion of either isoform Pde1 or Pde2 results in a moderate increase of the c-di-AMP levels compared with the parental strain. Deletion of both genes results in an up to 4fold increase in c-di-AMP levels compared to that of the parental strain. Both Pde1 and Pde2 play a role in pneumococcal growth. Deletion of either isoform Pde1 or Pde2 reduces the growth rate slightly, and the double mutant synergizes the reduction
Bowman, L.; Zeden, M.S.; Schuster, C.F.; Kaever, V.; Gruendling, A.
New insights into the cyclic di-adenosine monophosphate (c-di-AMP) degradation pathway and the requirement of the cyclic dinucleotide for acid stress resistance in Staphylococcus aureus
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3.1.4.60 pApA phosphodiesterase
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