|PROSITE documentation PDOC51794 [for PROSITE entry PS51794]|
Cyclic di-AMP (c-di-AMP) is a bacterial secondary messenger molecule, which is associated with various physiological functions. It is involved in several important cellular processes, such as cell wall metabolism, maintenance of DNA integrity, ion transport, transcription regulation, and allosteric regulation of enzyme function. The 120-amino acid-long diadenylate cyclase (DAC) domain converts two ATP or ADP molecules into one c-di-AMP molecule. The majority of DAC domain-containing proteins are found in bacterial species, but a small number are also present in archaea of the phylum Euryarchaeota. In bacteria, DAC domain proteins are most frequently found in Gram-positive bacteria belonging to the phyla Firmicutes and Actinobacteria, including pathogenic bacteria such as Listeria monocytogenes or Staphylococcus aureus. Compared with the majority of bacterial species which encode only one DAC enzyme, members of the genus bacillus generally encode three DAC domain-containing proteins: DisA, CdaA (previously named YbbP in the genus Bacillus or DacA in other genera) and CdaS (previously named YojJ in the genus Bacillus or DacB in others) [1,2,3,4,5].
The DAC domain exhibits an overall globular α/β fold with the long N-terminally located helix (α1) flanking the core (see <PDB:4RV7>). A slightly twisted central β-sheet, made up of seven mixed-parallel and antiparallel β-strands, forms the core globular part. Both sides of the β-sheets are flanked by a total of five α-helices (α1-α5), resulting in the observed globular shape [1,2].
The profile we developed covers the entire DAC domain.Last update:
March 2016 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Witte G. Hartung S. Buettner K. Hopfner K.-P.|
|Title||Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates.|
|Source||Mol. Cell 30:167-178(2008).|
|2||Authors||Rosenberg J. Dickmanns A. Neumann P. Gunka K. Arens J. Kaever V. Stuelke J. Ficner R. Commichau F.M.|
|Title||Structural and biochemical analysis of the essential diadenylate cyclase CdaA from Listeria monocytogenes.|
|Source||J. Biol. Chem. 290:6596-6606(2015).|
|3||Authors||Zheng C. Ma Y. Wang X. Xie Y. Ali M.K. He J.|
|Title||Functional analysis of the sporulation-specific diadenylate cyclase CdaS in Bacillus thuringiensis.|
|Source||Front. Microbiol. 6:908-908(2015).|
|4||Authors||Mueller M. Deimling T. Hopfner K.-P. Witte G.|
|Title||Structural analysis of the diadenylate cyclase reaction of DNA-integrity scanning protein A (DisA) and its inhibition by 3'-dATP.|
|Source||Biochem. J. 469:367-374(2015).|
|5||Authors||Corrigan R.M. Gruendling A.|
|Title||Cyclic di-AMP: another second messenger enters the fray.|
|Source||Nat. Rev. Microbiol. 11:513-524(2013).|