DnaA

• Description: AAA+ ATPase, replication initiation protein
  
  

Gene name	dnaA
Synonyms	dnaH, dnaJ, dnaK
Essential	yes PubMed
Product	replication initiation protein
Function	DNA replication
Gene expression levels in SubtiExpress: dnaA
Interactions involving this protein in SubtInteract: DnaA
MW, pI	50 kDa, 6.035
Gene length, protein length	1338 bp, 446 aa
Immediate neighbours	rpmH, dnaN
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

DNA replication, essential genes

This gene is a member of the following regulons

Spo0A regulon

The gene

Basic information

• Locus tag: BSU00010

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • binds multiple regions in the oriC region, required for recruitment of proteins needed to load the replicative helicase DnaC

• Protein family: dnaA family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains: AAA+ domain

• Modification:

• Cofactor(s):

• Effectors of protein activity:
  • SirA displaces DnaA from the replication origin PubMed
  • YabA inhibits co-operative binding of DnaA to the oriC DNA PubMed
  • DnaA helix formation (and thus replication initiation) is inhibited by the interaction of either Soj, YabA or DnaN with the AAA+ domain of DnaA PubMed
  • interaction with DnaD inhibits the ability of DnaA to cooperatively bind to DNA PubMed

• Interactions:
  • DnaA assembles into a right-handed helical oligomer built upon interactions between neighbouring AAA+ domains PubMed
  • Soj-DnaA PubMed
  • DnaA-YabA PubMed
  • DnaA-YabA-DnaN PubMed
  • DnaA-DnaD PubMed
  • SirA-DnaA PubMed
  • YqaH-DnaA PubMed
  • part of the primosome: DnaA-DnaG-DnaC-DnaI-DnaD-DnaB PubMed

• Localization:
  • throughout the cytoplasm PubMed

Database entries

• Structure:

• UniProt: P05648

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: dnaA-dnaN PubMed

• Expression browser: dnaA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • negatively controlled by DnaA PubMed and Spo0A PubMed
  • repressed under conditions that trigger sporulation (Spo0A) PubMed

• Regulatory mechanism:
  • Spo0A: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

• Philippe Noirot, Jouy-en-Josas, France homepage
• Peter Graumann, Freiburg University, Germany homepage
• Alan Grossman, MIT, Cambridge, MA, USA
• Heath Murray, Centre for Bacterial Cell Biology, Newcastle, UK[4]

References

Reviews

Geoffrey S Briggs, Wiep Klaas Smits, Panos Soultanas
Chromosomal replication initiation machinery of low-G+C-content Firmicutes.
J Bacteriol: 2012, 194(19);5162-70
[PubMed:22797751] [WorldCat.org] [DOI] (I p)

An-Chun Chien, Norbert S Hill, Petra Anne Levin
Cell size control in bacteria.
Curr Biol: 2012, 22(9);R340-9
[PubMed:22575476] [WorldCat.org] [DOI] (I p)

Alan C Leonard, Julia E Grimwade
Regulation of DnaA assembly and activity: taking directions from the genome.
Annu Rev Microbiol: 2011, 65;19-35
[PubMed:21639790] [WorldCat.org] [DOI] (I p)

Alan C Leonard, Julia E Grimwade
Regulating DnaA complex assembly: it is time to fill the gaps.
Curr Opin Microbiol: 2010, 13(6);766-72
[PubMed:21035377] [WorldCat.org] [DOI] (I p)

Tsutomu Katayama, Shogo Ozaki, Kenji Keyamura, Kazuyuki Fujimitsu
Regulation of the replication cycle: conserved and diverse regulatory systems for DnaA and oriC.
Nat Rev Microbiol: 2010, 8(3);163-70
[PubMed:20157337] [WorldCat.org] [DOI] (I p)

The DnaA regulon

Alexi I Goranov, Luba Katz, Adam M Breier, Christopher B Burge, Alan D Grossman
A transcriptional response to replication status mediated by the conserved bacterial replication protein DnaA.
Proc Natl Acad Sci U S A: 2005, 102(36);12932-7
[PubMed:16120674] [WorldCat.org] [DOI] (P p)