{PDOC51794}
{PS51794; DAC}
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* Diadenylate cyclase (DAC) domain profile *
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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 alpha/beta fold with the long N-
terminally located  helix  (alpha1)  flanking  the  core  (see  <PDB:4RV7>). A
slightly twisted  central  beta-sheet,  made  up  of  seven mixed-parallel and
antiparallel beta-strands,  forms  the  core  globular part. Both sides of the
beta-sheets are  flanked  by  a  total  of five alpha-helices (alpha1-alpha5),
resulting in the observed globular shape [1,2].

The profile we developed covers the entire DAC domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: March 2016 / First entry.

[ 1] Witte G., Hartung S., Buettner K., Hopfner K.-P.
     "Structural biochemistry of a bacterial checkpoint protein reveals
     diadenylate cyclase activity regulated by DNA recombination
     intermediates."
     Mol. Cell 30:167-178(2008).
     PubMed=18439896; DOI=10.1016/j.molcel.2008.02.020
[ 2] Rosenberg J., Dickmanns A., Neumann P., Gunka K., Arens J., Kaever V.,
     Stuelke J., Ficner R., Commichau F.M.
     "Structural and biochemical analysis of the essential diadenylate
     cyclase CdaA from Listeria monocytogenes."
     J. Biol. Chem. 290:6596-6606(2015).
     PubMed=25605729; DOI=10.1074/jbc.M114.630418
[ 3] Zheng C., Ma Y., Wang X., Xie Y., Ali M.K., He J.
     "Functional analysis of the sporulation-specific diadenylate cyclase
     CdaS in Bacillus thuringiensis."
     Front. Microbiol. 6:908-908(2015).
     PubMed=26441857; DOI=10.3389/fmicb.2015.00908
[ 4] Mueller M., Deimling T., Hopfner K.-P., Witte G.
     "Structural analysis of the diadenylate cyclase reaction of
     DNA-integrity scanning protein A (DisA) and its inhibition by
     3'-dATP."
     Biochem. J. 469:367-374(2015).
     PubMed=26014055; DOI=10.1042/BJ20150373
[ 5] Corrigan R.M., Gruendling A.
     "Cyclic di-AMP: another second messenger enters the fray."
     Nat. Rev. Microbiol. 11:513-524(2013).
     PubMed=23812326; DOI=10.1038/nrmicro3069

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