DnaB

• Description: initiation of chromosome replication/ membrane attachment protein
  
  

Gene name	dnaB
Synonyms
Essential	yes PubMed
Product	initiation of chromosome replication/ membrane attachment protein
Function	DNA replication
MW, pI	54 kDa, 5.278
Gene length, protein length	1416 bp, 472 aa
Immediate neighbours	dnaI, ytcG
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU28990

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: DnaB-PriA, DnaB-DnaI, DnaB-DnaC PubMed, DnaD-DnaB PubMed, DnaB-DnaX PubMed

• Localization: Membrane-proximal (Spotty) PubMed forms foci, close to oriC PubMed

Database entries

• Structure:

• UniProt: P07908

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Sigma factor: SigE PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

William H Grainger, Cristina Machón, David J Scott, Panos Soultanas
DnaB proteolysis in vivo regulates oligomerization and its localization at oriC in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(9);2851-64
[PubMed:20071750] [WorldCat.org] [DOI] (I p)

Wiep Klaas Smits, Alexi I Goranov, Alan D Grossman
Ordered association of helicase loader proteins with the Bacillus subtilis origin of replication in vivo.
Mol Microbiol: 2010, 75(2);452-61
[PubMed:19968790] [WorldCat.org] [DOI] (I p)

Megan E Rokop, Alan D Grossman
Intragenic and extragenic suppressors of temperature sensitive mutations in the replication initiation genes dnaD and dnaB of Bacillus subtilis.
PLoS One: 2009, 4(8);e6774
[PubMed:19707554] [WorldCat.org] [DOI] (I e)

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)

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)

Claude Bruand, Marion Velten, Stephen McGovern, Stéphanie Marsin, Céline Sérèna, S Dusko Ehrlich, Patrice Polard
Functional interplay between the Bacillus subtilis DnaD and DnaB proteins essential for initiation and re-initiation of DNA replication.
Mol Microbiol: 2005, 55(4);1138-50
[PubMed:15686560] [WorldCat.org] [DOI] (P p)

Megan E Rokop, Jennifer M Auchtung, Alan D Grossman
Control of DNA replication initiation by recruitment of an essential initiation protein to the membrane of Bacillus subtilis.
Mol Microbiol: 2004, 52(6);1757-67
[PubMed:15186423] [WorldCat.org] [DOI] (P p)

Anna Haroniti, Christopher Anderson, Zara Doddridge, Laurence Gardiner, Clive J Roberts, Stephanie Allen, Panos Soultanas
The clamp-loader-helicase interaction in Bacillus. Atomic force microscopy reveals the structural organisation of the DnaB-tau complex in Bacillus.
J Mol Biol: 2004, 336(2);381-93
[PubMed:14757052] [WorldCat.org] [DOI] (P p)

A Haroniti, R Till, M C M Smith, P Soultanas
Clamp-loader-helicase interaction in Bacillus. Leucine 381 is critical for pentamerization and helicase binding of the Bacillus tau protein.
Biochemistry: 2003, 42(37);10955-64
[PubMed:12974630] [WorldCat.org] [DOI] (P p)

Marion Velten, Stephen McGovern, Stéphanie Marsin, S Dusko Ehrlich, Philippe Noirot, Patrice Polard
A two-protein strategy for the functional loading of a cellular replicative DNA helicase.
Mol Cell: 2003, 11(4);1009-20
[PubMed:12718886] [WorldCat.org] [DOI] (P p)

P Soultanas
A functional interaction between the putative primosomal protein DnaI and the main replicative DNA helicase DnaB in Bacillus.
Nucleic Acids Res: 2002, 30(4);966-74
[PubMed:11842108] [WorldCat.org] [DOI] (I p)

C Bruand, M Farache, S McGovern, S D Ehrlich, P Polard
DnaB, DnaD and DnaI proteins are components of the Bacillus subtilis replication restart primosome.
Mol Microbiol: 2001, 42(1);245-55
[PubMed:11679082] [WorldCat.org] [DOI] (P p)

S Marsin, S McGovern, S D Ehrlich, C Bruand, P Polard
Early steps of Bacillus subtilis primosome assembly.
J Biol Chem: 2001, 276(49);45818-25
[PubMed:11585815] [WorldCat.org] [DOI] (P p)

M Bárcena, T Ruiz, L E Donate, S E Brown, N E Dixon, M Radermacher, J M Carazo
The DnaB.DnaC complex: a structure based on dimers assembled around an occluded channel.
EMBO J: 2001, 20(6);1462-8
[PubMed:11250911] [WorldCat.org] [DOI] (P p)

Y Imai, N Ogasawara, D Ishigo-Oka, R Kadoya, T Daito, S Moriya
Subcellular localization of Dna-initiation proteins of Bacillus subtilis: evidence that chromosome replication begins at either edge of the nucleoids.
Mol Microbiol: 2000, 36(5);1037-48
[PubMed:10844689] [WorldCat.org] [DOI] (P p)

G Henckes, F Harper, A Levine, F Vannier, S J Séror
Overreplication of the origin region in the dnaB37 mutant of Bacillus subtilis: postinitiation control of chromosomal replication.
Proc Natl Acad Sci U S A: 1989, 86(22);8660-4
[PubMed:2554322] [WorldCat.org] [DOI] (P p)