2019-07-22 08:57:202025-05-13 22:53:27
The protein
Catalyzed reaction/ biological activity
synthesis of c-di-AMP from two molecules of ATP [Pubmed|23192352]
synthesis of c-di-AMP from two molecules of ATP [Pubmed|23192352]
2 ATP --> c-di-AMP + 2 diphosphate (according to UniProt)
The protein
[SW|Domains]
contains a [SW|DAC domain] involved in the synthesis of c-di-AMP [Pubmed|21566650]
contains a [SW|DAC domain] involved in the synthesis of c-di-AMP [Pubmed|21566650]
[SW|DAC domain] (aa 82-242) (according to UniProt)
The protein
Effectors of protein activity
the interaction with [[protein|CdaR]] controls the diadenylate cyclase activity of [[protein|CdaA]] [Pubmed|23192352]
the interaction with [[protein|CdaR]] inhibits the diadenylate cyclase activity of [[protein|CdaA]] (shown in S. aureus) [pubmed|30668586]
the interaction with [[protein|CdaR]] controls the diadenylate cyclase activity of [[protein|CdaA]] [Pubmed|23192352]
the interaction with [[protein|CdaR]] inhibits the diadenylate cyclase activity of [[protein|CdaA]] (shown in S. aureus) [pubmed|30668586]
the interaction with [[protein|GlmM]] inhibits the diadenylate cyclase activity of [[protein|CdaA]] under conditions of osmotic stress (shown in L. monocytogenes) [pubmed|32250026]
The protein
Structure
[PDB|4RV7] (the [SW|DAC domain] and C-terminal domain of CdaA from ''Listeria monocytogenes'' (aa 101 - 273), 65% identity) [Pubmed|25605729]
[PDB|6HVL] (the [SW|DAC domain] and C-terminal domain of CdaA from ''Listeria monocytogenes'' (aa 101 - 273) in complex with c-di-AMP, 65% identity) [Pubmed|31118276]
[PDB|6HUW]
[PDB|4RV7] (the [SW|DAC domain] and C-terminal domain of CdaA from ''Listeria monocytogenes'' (aa 101 - 273), 65% identity) [Pubmed|25605729]
[PDB|6HVL] (the [SW|DAC domain] and C-terminal domain of CdaA from ''Listeria monocytogenes'' (aa 101 - 273) in complex with c-di-AMP, 65% identity) [Pubmed|31118276]
References
Reviews
References
Original publications
labs
[SW|Jörg Stülke], University of Göttingen, Germany [http://genmibio.uni-goettingen.de Homepage]