SubtiBank SubtiBank
cdaA
You are currently viewing an outdated version of SubtiWiki. Please use the newest version!

cdaA

diadenylate cyclase, synthesis of c-di-AMP in vegetative cells
Locus
BSU_01750
Isoelectric point
8.07
Molecular weight
30.42 kDa
Protein length
273 aa Sequence Blast
Gene length
822 bp Sequence Blast
Function
synthesis of c-di-AMP
Product
diadenylate cyclase
Essential
no
E.C.
2.7.7.85
Synonyms
ybbP,ybbQ

Genomic Context

      
Loading

Categories containing this gene/protein

Gene

Coordinates
196,213 → 197,034

Phenotypes of a mutant

  • inactivation of cdaA results in severe beta-lactam sensitivity PubMed
  • a cdaA disA double mutant or cdaA cdaS disA triple mutant is not viable on complex medium; however, the mutant grows at low potassium concentration (0.1 mM) PubMed
  • The protein

    Catalyzed reaction/ biological activity

  • synthesis of c-di-AMP from two molecules of ATP PubMed
  • 2 ATP --> c-di-AMP + 2 diphosphate (according to UniProt)
  • Protein family

  • adenylate cyclase family (with CdaS, according to UniProt)
  • Paralogous protein(s)

    Domains

  • contains a DAC domain involved in the synthesis of c-di-AMP PubMed
  • DAC domain (aa 82-242) (according to UniProt)
  • Cofactors

  • Mn2+ PubMed
  • Effectors of protein activity

  • the interaction with CdaR controls the diadenylate cyclase activity of CdaA PubMed
  • the interaction with CdaR inhibits the diadenylate cyclase activity of CdaA (shown in S. aureus) PubMed
  • the interaction with GlmM inhibits the diadenylate cyclase activity of CdaA under conditions of osmotic stress (shown in L. monocytogenes) PubMed
  • Structure

  • 6HUW
  • 4RV7 (the DAC domain and C-terminal domain of CdaA from Listeria monocytogenes (aa 101 - 273), 65% identity) PubMed
  • 6HVL (the DAC domain and C-terminal domain of CdaA from Listeria monocytogenes (aa 101 - 273) in complex with c-di-AMP, 65% identity) PubMed
  • Localization

  • cell membrane PubMed
  • Expression and Regulation

    Operons

    Description

    Sigma factors

  • SigA: sigma factor, PubMed, in SigA regulon
  • view in new tab

    Additional information

  • CdaA levels are increased at increased potassium concentrations PubMed
  • the mRNA is very stable (> 15 min) PubMed
  • Biological materials

    Mutant

  • GP94 ΔcdaA::spec, available in Jörg Stülke's lab PubMed
  • GP997 ΔcdaA::cat, available in Jörg Stülke's lab PubMed
  • GP2790 ΔcdaA::aphA3, available in Jörg Stülke's lab
  • GP985 (cdaA-cdaR::cat), available in Jörg Stülke's lab
  • GP2222 (cdaA::cat cdaS::ermC disA::tet), available in Jörg Stülke's lab, the mutant is only viable on minimal medium at low potassium concentration PubMed
  • BKE01750 (ΔcdaA::erm trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATTTCCTCGTCCTCCAAGA, downstream forward: _UP4_CGCTGGTATTGGAGGGGCAA
  • BKK01750 (ΔcdaA::kan trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATTTCCTCGTCCTCCAAGA, downstream forward: _UP4_CGCTGGTATTGGAGGGGCAA
  • Expression vectors

  • expression of native cdaA in B. subtilis: pGP1960 (in pBQ200), available in Jörg Stülke's lab
  • expression of cdaA-Strep in B. subtilis suitable for SPINE: pGP1986 (in pGP382), available in Jörg Stülke's lab
  • IPTG inducible expression of cdaA-Strep in E. coli: pGP2564 (in pGP574), available in Jörg Stülke's lab
  • LacZ fusion

  • GP1339 (cat) based on pAC6, available in Jörg Stülke's lab
  • Two-hybrid system

  • B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab. Respective plasmid: pGP1990.
  • FLAG-tag construct

  • GP1381 cdaA-3xFLAG ermC (based on pGP1087), available in Jörg Stülke's lab PubMed
  • Labs working on this gene/protein

  • Jörg Stülke, University of Göttingen, Germany Homepage
  • References

    Reviews

    Loading

    Original publications

    Loading