Part:BBa_K1045003:Design

Diadenylate cyclase domain of Listeria monocytogenes cdaA (DacA)

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  COMPATIBLE WITH RFC[1000]

Design Notes

The genomic sequence of BBa_K1045003 contained a SpeI restriction site on position 456 of the DNA sequence. The restriction site was deleted without altering the amino acid sequence of the protein.

Source

The part was amplified using PCR from L. monocytogenes genomic DNA.

References

Corrigan RM and Gründling A. Cyclic di-AMP: another second messenger enters the fray. Nat Rev Microbiol. 2013; 11(8):513-524

Luo Y and Helmann JD. Analysis of the role of Bacillus subtilis σ(M) in β-lactam resistance reveals an essential role for c-di-AMP in peptidoglycan homeostasis. Mol Microbiol. 2012; 83(3):623-639

Mehne FM, Gunka K, Eilers H, Herzberg C, Kaever V, Stülke 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. 2013; 288(3):2004-2017

Oppenheimer-Shaanan Y, Wexselblatt E, Katzenhendler J, Yavin E, Ben-Yehuda S. c-di-AMP reports DNA integrity during sporulation in Bacillus subtilis. EMBO Rep. 2011; 12(6):594-601

Witte G, Hartung S, Büttner K, Hopfner KP. Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates. Mol Cell. 2008; 30(2):167-178

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. 2013; 52(6-7):319-324 </p>

Acknowledgements: In order to obtain the crystals and the protein structure we would like to thank Dr. Achim Dichmanns and Dr. Piotr Neumann for their great support.