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5'-O-phosphonoadenylyl-(3'->5')-adenosine + H2O
2 AMP
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cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
cyclic di-3',5'-guanylate + H2O
5'-phosphoguanylyl-(3'->5')guanosine
additional information
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cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
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cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
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cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
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cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
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cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
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cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
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cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
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cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
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cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
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cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
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cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
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cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
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cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
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cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
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?
cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
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?
cyclic di-3',5'-adenylate + H2O
5'-O-phosphonoadenylyl-(3'->5')-adenosine
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-
?
cyclic di-3',5'-guanylate + H2O
5'-phosphoguanylyl-(3'->5')guanosine
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?
cyclic di-3',5'-guanylate + H2O
5'-phosphoguanylyl-(3'->5')guanosine
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cyclic di-3',5'-guanylate + H2O
5'-phosphoguanylyl-(3'->5')guanosine
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cyclic di-3',5'-guanylate + H2O
5'-phosphoguanylyl-(3'->5')guanosine
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additional information
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enzyme has c-di-AMP specific phosphodiesterase activity. It hydrolyzes c-di-AMP to 5'-AMP in two steps. First, it linearizes c-di-AMP into pApA , reaction of EC 3.1.4.59, which is further hydrolyzed to 5'-AMP, reaction of EC 3.1.4.60
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additional information
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enzyme has c-di-AMP specific phosphodiesterase activity. It hydrolyzes c-di-AMP to 5'-AMP in two steps. First, it linearizes c-di-AMP into pApA , reaction of EC 3.1.4.59, which is further hydrolyzed to 5'-AMP, reaction of EC 3.1.4.60
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additional information
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Pde is capable of converting c-di-AMP to pApA, i.e. 5'-O-phosphonoadenylyl-(3'->5')-adenosine and AMP, and hydrolyzing pApA to AMP
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additional information
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Pde is capable of converting c-di-AMP to pApA, i.e. 5'-O-phosphonoadenylyl-(3'->5')-adenosine and AMP, and hydrolyzing pApA to AMP
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additional information
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enzyme does not hydrolyze product 5'-O-phosphonoadenylyl-(3'->5')-adenosine
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additional information
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isoform Pde2 is capable of hydrolyzing c-di-AMP and Pde2 preferentially converts linear 5'-phosphonoadenylyl-adenosine (pApA) to AMP, reaction of EC 3.1.3.7. No substrate: ATP
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additional information
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isoform Pde2 is capable of hydrolyzing c-di-AMP and Pde2 preferentially converts linear 5'-phosphonoadenylyl-adenosine (pApA) to AMP, reaction of EC 3.1.3.7. No substrate: ATP
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additional information
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Pde2 directly hydrolyzes c-di-AMP into AMP. Additionally, Pde2 degrades 5'-O-phosphonoadenylyl-(3'->5')-adenosine into AMP. Pde2 prefers substrate 5'-O-phosphonoadenylyl-(3'->5')-adenosine
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additional information
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Pde2 directly hydrolyzes c-di-AMP into AMP. Additionally, Pde2 degrades 5'-O-phosphonoadenylyl-(3'->5')-adenosine into AMP. Pde2 prefers substrate 5'-O-phosphonoadenylyl-(3'->5')-adenosine
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physiological function
a Pde2 mutant strain displays a growth defect in the early growth phase. Mutation leads to an increase in cellular c-di-AMP and 5'-O-phosphonoadenylyl-(3'->5')-adenosine levels and increased resistance to oxacillin
physiological function
both phosphodiesterases, GdpP and PgpH, contribute to the degradation of cyclic di-AMP. Accumulation of cyclic di-AMP in a GdpP PgpH double mutant is toxic for the cells, and the cells respond to accumulation by inactivation of the diadenylate cyclase CdaA
physiological function
both phosphodiesterases, GdpP and PgpH, contribute to the degradation of cyclic di-AMP. Accumulation of cyclic di-AMP in a GdpP PgpH double mutant is toxic for the cells, and the cells respond to this accumulation by inactivation of the diadenylate cyclase CdaA
physiological function
deficiency of Pde significantly enhances intracellular C12-C20 fatty acid accumulation. Superfluous c-di-AMP in Mycobacterium smegmatis may lead to abnormal colonial morphology
physiological function
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
physiological function
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deletion of the GdpP gene impairs the processing of cysteine protease SpeB, decreases sensitivity to the antibiotic ampicillin, and attenuates virulence in a murine model of subcutaneous infection
physiological function
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
physiological function
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disruption of gdpP increases intracellular c-di-AMP level and affects growth and increases biofilm formation. The GdpP mutant strain exhibits a significant decrease in hemolytic activity and adherence to and invasion of HEp-2 cells compared with the parental strain. Virulence genes cps2,sly, fpbs, mrp, ef and gdh display reduced expression in the gdpP mutant. In murine infection models, the GdpP mutant strain is attenuated, and impaired bacterial growth is observed in specific organs
physiological function
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GdpP mutant bacteria contain extra-membranous material at the division sites and in the form of vesicles in the cytoplasm. Expression of superoxide dismutase SodM is 5fold downregulated in the mutant, while no significant differences in the susceptibility to H2O2 or in peroxide levels are observed
physiological function
inactivation of GdpP confers tolerance to inhibitors of peptidoglycan biosynthesis
physiological function
mutations in GdpP result in stable heat resistance and in some cases salt-hypersensitive phenotypes. Mutants display improved growth in response to sublethal concentrations of penicillin G. High-temperature incubation of a wild-type industrial Lactococcus lactis strain also results in spontaneous mutation GdpP and heat-resistant and salt-hypersensitive phenotypes. Acidification of milk by the GdpP-altered strain is inhibited by lower salt concentrations than the parent strain
physiological function
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mutations within the GdpP gene, allow both laboratory and clinical isolates of Staphylococcus aureus to grow without lipoteichoic acid. Intracellular c-di-AMP levels increase drastically in GdpP deletion strains and in an lipoteichoic acid-deficient suppressor strain. An increased amount of cross-linked peptidoglycan is observed in the GdpP mutant strain. GdpP mutant strains display a 13-22% reduction in the cell size due to increased c-di-AMP levels
physiological function
overexpression of PdeA leads to marked decreases in growth rates, both in vitro and in infected macrophages. Deletion of pdeA affects bacterial response to acid stress and leads to increased expression of resuscitation-promoting factors. Mutants with altered levels of c-di-AMP have different susceptibilities to peptidoglycan-targeting antibiotics
physiological function
the DHH/DHHA1 domain hydrolyzes c-di-AMP and c-di-GMP to generate the linear dinucleotides 5'-pApA and 5'-pGpG. The atypical GGDEF domain of YybT exhibits ATPase activity. YybT participates in DNA damage and acid resistance
physiological function
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inactivation of GdpP confers tolerance to inhibitors of peptidoglycan biosynthesis
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physiological function
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both phosphodiesterases, GdpP and PgpH, contribute to the degradation of cyclic di-AMP. Accumulation of cyclic di-AMP in a GdpP PgpH double mutant is toxic for the cells, and the cells respond to this accumulation by inactivation of the diadenylate cyclase CdaA
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physiological function
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the DHH/DHHA1 domain hydrolyzes c-di-AMP and c-di-GMP to generate the linear dinucleotides 5'-pApA and 5'-pGpG. The atypical GGDEF domain of YybT exhibits ATPase activity. YybT participates in DNA damage and acid resistance
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physiological function
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both phosphodiesterases, GdpP and PgpH, contribute to the degradation of cyclic di-AMP. Accumulation of cyclic di-AMP in a GdpP PgpH double mutant is toxic for the cells, and the cells respond to accumulation by inactivation of the diadenylate cyclase CdaA
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physiological function
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overexpression of PdeA leads to marked decreases in growth rates, both in vitro and in infected macrophages. Deletion of pdeA affects bacterial response to acid stress and leads to increased expression of resuscitation-promoting factors. Mutants with altered levels of c-di-AMP have different susceptibilities to peptidoglycan-targeting antibiotics
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physiological function
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mutations in GdpP result in stable heat resistance and in some cases salt-hypersensitive phenotypes. Mutants display improved growth in response to sublethal concentrations of penicillin G. High-temperature incubation of a wild-type industrial Lactococcus lactis strain also results in spontaneous mutation GdpP and heat-resistant and salt-hypersensitive phenotypes. Acidification of milk by the GdpP-altered strain is inhibited by lower salt concentrations than the parent strain
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physiological function
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a Pde2 mutant strain displays a growth defect in the early growth phase. Mutation leads to an increase in cellular c-di-AMP and 5'-O-phosphonoadenylyl-(3'->5')-adenosine levels and increased resistance to oxacillin
-
physiological function
-
deficiency of Pde significantly enhances intracellular C12-C20 fatty acid accumulation. Superfluous c-di-AMP in Mycobacterium smegmatis may lead to abnormal colonial morphology
-
physiological function
-
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
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physiological function
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disruption of gdpP increases intracellular c-di-AMP level and affects growth and increases biofilm formation. The GdpP mutant strain exhibits a significant decrease in hemolytic activity and adherence to and invasion of HEp-2 cells compared with the parental strain. Virulence genes cps2,sly, fpbs, mrp, ef and gdh display reduced expression in the gdpP mutant. In murine infection models, the GdpP mutant strain is attenuated, and impaired bacterial growth is observed in specific organs
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physiological function
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mutations within the GdpP gene, allow both laboratory and clinical isolates of Staphylococcus aureus to grow without lipoteichoic acid. Intracellular c-di-AMP levels increase drastically in GdpP deletion strains and in an lipoteichoic acid-deficient suppressor strain. An increased amount of cross-linked peptidoglycan is observed in the GdpP mutant strain. GdpP mutant strains display a 13-22% reduction in the cell size due to increased c-di-AMP levels
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Griffiths, J.; ONeill, A.
Loss of function of the GdpP protein leads to joint beta-lactam/ glycopeptide tolerance in Staphylococcus aureus
Antimicrob. Agents Chemother.
56
579-581
2012
Staphylococcus aureus (Q2G2T6), Staphylococcus aureus NCTC 8325 (Q2G2T6)
brenda
Smith, W.M.; Pham, T.H.; Lei, L.; Dou, J.; Soomro, A.H.; Beatson, S.A.; Dykes, G.A.; Turner, M.S.
Heat resistance and salt hypersensitivity in Lactococcus lactis due to spontaneous mutation of llmg_1816 (gdpP) induced by high-temperature growth
Appl. Environ. Microbiol.
78
7753-7759
2012
Lactococcus cremoris (A2RM60), Lactococcus cremoris MG1363 (A2RM60)
brenda
Wang, F.; He, Q.; Su, K.; Wei, T.; Xu, S.; Gu, L.
Structural and biochemical characterization of the catalytic domains of GdpP reveals a unified hydrolysis mechanism for the DHH/DHHA1 phosphodiesterase
Biochem. J.
475
191-205
2018
Staphylococcus aureus (A0A0U1MUE2)
brenda
Ye, M.; Zhang, J.J.; Fang, X.; Lawlis, G.B.; Troxell, B.; Zhou, Y.; Gomelsky, M.; Lou, Y.; Yang, X.F.
DhhP, a cyclic di-AMP phosphodiesterase of Borrelia burgdorferi, is essential for cell growth and virulence
Infect. Immun.
82
1840-1849
2014
Borreliella burgdorferi (O51564), Borreliella burgdorferi, Borreliella burgdorferi DSM 4680 (O51564)
brenda
Tang, Q.; Luo, Y.; Zheng, C.; Yin, K.; Ali, M.; Li, X.; He, J.
Functional analysis of a c-di-AMP-specific phosphodiesterase MsPDE from Mycobacterium smegmatis
Int. J. Biol. Sci.
11
813-824
2015
Mycolicibacterium smegmatis (A0QVM9), Mycolicibacterium smegmatis ATCC 700084 (A0QVM9)
brenda
Ba, X.; Kalmar, L.; Hadjirin, N.F.; Kerschner, H.; Apfalter, P.; Morgan, F.J.; Paterson, G.K.; Girvan, S.L.; Zhou, R.; Harrison, E.M.; Holmes, M.A.
Truncation of GdpP mediates beta-lactam resistance in clinical isolates of Staphylococcus aureus
J. Antimicrob. Chemother.
74
1182-1191
2019
Staphylococcus aureus
brenda
Bai, Y.; Yang, J.; Eisele, L.E.; Underwood, A.J.; Koestler, B.J.; Waters, C.M.; Metzger, D.W.; Bai, G.
Two DHH subfamily 1 proteins in Streptococcus pneumoniae possess cyclic di-AMP phosphodiesterase activity and affect bacterial growth and virulence
J. Bacteriol.
195
5123-5132
2013
Streptococcus pneumoniae D39 (A0A0H2ZNP2), Streptococcus pneumoniae D39 (A0A0H2ZQZ4)
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 (P37484), Bacillus subtilis (P46344), Bacillus subtilis 168 (P37484), Bacillus subtilis 168 (P46344)
brenda
Rao, F.; See, R.; Zhang, D.; Toh, D.; Ji, Q.; Liang, Z.
YybT is a signaling protein that contains a cyclic dinucleotide phosphodiesterase domain and a GGDEF domain with ATPase activity
J. Biol. Chem.
285
473-482
2010
Bacillus subtilis (P37484), Bacillus subtilis 168 (P37484)
brenda
Tan, E.; Rao, F.; Pasunooti, S.; Pham, T.H.; Soehano, I.; Turner, M.S.; Liew, C.W.; Lescar, J.; Pervushin, K.; Liang, Z.X.
Solution structure of the PAS domain of a thermophilic YybT protein homolog reveals a potential ligand-binding site
J. Biol. Chem.
288
11949-11959
2013
Geobacillus thermodenitrificans (A4ITV2), Geobacillus thermodenitrificans NG80-2 (A4ITV2)
brenda
Corrigan, R.M.; Bowman, L.; Willis, A.R.; Kaever, V.; Gruendling, A.
Cross-talk between two nucleotide-signaling pathways in Staphylococcus aureus
J. Biol. Chem.
290
5826-5839
2015
Staphylococcus aureus
brenda
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
J. Biol. Chem.
291
26970-26986
2016
Staphylococcus aureus (A0A0H2XFX6), Staphylococcus aureus USA300 (A0A0H2XFX6)
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
2013
Listeria monocytogenes (Q8YAR3), Listeria monocytogenes, Listeria monocytogenes ATCC BAA-679 (Q8YAR3)
brenda
Du, B.; Ji, W.; An, H.; Shi, Y.; Huang, Q.; Cheng, Y.; Fu, Q.; Wang, H.; Yan, Y.; Sun, J.
Functional analysis of c-di-AMP phosphodiesterase, GdpP, in Streptococcus suis serotype 2
Microbiol. Res.
169
749-758
2014
Streptococcus suis, Streptococcus suis serotype 2
brenda
Luo, Y.; Helmann, J.D.
A sigmaD-dependent antisense transcript modulates expression of the cyclic-di-AMP hydrolase GdpP in Bacillus subtilis
Microbiology
158
2732-2741
2012
Bacillus subtilis (P37484), Bacillus subtilis 168 (P37484)
brenda
Cho, K.; Kang, S.
Streptococcus pyogenes c-di-AMP phosphodiesterase, GdpP, influences SpeB processing and virulence
PLoS ONE
8
e69425
2013
Streptococcus pyogenes
brenda
Manikandan, K.; Sabareesh, V.; Singh, N.; Saigal, K.; Mechold, U.; Sinha, K.
Two-step synthesis and hydrolysis of cyclic di-AMP in Mycobacterium tuberculosis
PLoS ONE
9
e86096
2014
Mycobacterium tuberculosis (P71615), Mycobacterium tuberculosis H37Rv (P71615)
brenda
Corrigan, R.; Abbott, J.; Burhenne, H.; Kaever, V.; Gruendling, A.
C-di-amp is a new second messenger in staphylococcus aureus with a role in controlling cell size and envelope stress
PLoS Pathog.
7
e1002217
2011
Staphylococcus aureus, Staphylococcus aureus RN4220
brenda