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Revision as of 18:04, 8 November 2010 by Jourde (talk | contribs) (immediate neighbours "antE" and "yqxD" changed to "sigA" and "antE" respectivly)
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  • Description: DNA primase, part of the replisome

Gene name dnaG
Synonyms dnaE
Essential yes PubMed
Product DNA primase
Function DNA replication
MW, pI 68 kDa, 6.706
Gene length, protein length 1809 bp, 603 aa
Immediate neighbours sigA, antE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
DnaG context.gif
This image was kindly provided by SubtiList

The gene

Basic information

  • Locus tag: BSU25210

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: DNA primase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity: the enzymatic activity is inhibited by (p)ppGpp during the ´stringent response´ PubMed
  • Localization: Cytoplasm (Homogeneous) PubMed

Database entries

  • Structure: 1D0Q (zinc binding domain, Geobacillus stearothermophilus), 1Z8S (DnaB binding domain, AA 452-597, Geobacillus stearothermophilus)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • repressed under conditions that trigger sporulation (Spo0A) PubMed
    • enzymatic activity is inhibited by (p)ppGpp during the ´stringent response´
  • Regulatory mechanism:
  • Additional information:
    • enzymatic activity is inhibited by (p)ppGpp during the ´stringent response´ PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks


Glenn M Sanders, H Garry Dallmann, Charles S McHenry
Reconstitution of the B. subtilis replisome with 13 proteins including two distinct replicases.
Mol. Cell: 2010, 37(2);273-81
[PubMed:20122408] [WorldCat.org] [DOI] (I p)

Kiran Chintakayala, Cristina Machón, Anna Haroniti, Marilyn A Larson, Steven H Hinrichs, Mark A Griep, Panos Soultanas
Allosteric regulation of the primase (DnaG) activity by the clamp-loader (tau) in vitro.
Mol. Microbiol.: 2009, 72(2);537-49
[PubMed:19415803] [WorldCat.org] [DOI] (I p)

Jue D Wang, Glenn M Sanders, Alan D Grossman
Nutritional control of elongation of DNA replication by (p)ppGpp.
Cell: 2007, 128(5);865-75
[PubMed:17350574] [WorldCat.org] [DOI] (P p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol. Microbiol.: 2003, 50(5);1683-701
[PubMed:14651647] [WorldCat.org] [DOI] (P p)

L F Wang, C W Price, R H Doi
Bacillus subtilis dnaE encodes a protein homologous to DNA primase of Escherichia coli.
J. Biol. Chem.: 1985, 260(6);3368-72
[PubMed:3919021] [WorldCat.org] (P p)