Spo0A

• Description: phosphorelay regulator, initiation of sporulation, coordinates DNA replication and initiation of sporulation by binding to sites close to the oriC
  
  

Gene name	spo0A
Synonyms	spo0C, spo0G, spoIIL, sof-1
Essential	no
Product	phosphorelay response regulator
Function	initiation of sporulation
Gene expression levels in SubtiExpress: spo0A
Interactions involving this protein in SubtInteract: Spo0A
Metabolic function and regulation of this protein in SubtiPathways: Biofilm, Nucleotides (regulation), Ammonium/ glutamate, Central C-metabolism,Sugar catabolism, Phosphorelay, Stress, tRNA charging,Lipid synthesis, Protein secretion
MW, pI	29 kDa, 5.989
Gene length, protein length	801 bp, 267 aa
Immediate neighbours	yqiG, spoIVB
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

transcription factors and their control, phosphorelay, biofilm formation, phosphoproteins

This gene is a member of the following regulons

SigH regulon, Spo0A regulon

The gene

Basic information

• Locus tag: BSU24220

Phenotypes of a mutant

• inactivation of spo0A restores beta-lactam resistance in a sigM mutant PubMed
• altered cell death pattern in colonies PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • activation of gene expression at the onset of sporulation (Spo0A regulon)
  • coordination between DNA replication and initiation of sporulation by binding to sites close to the oriC (this limits re-initiation of replication) PubMed

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: receives phosphorylation from Spo0B, dephosphorylation by Spo0E, direct phosphorylation by KinC upon potassium leakage PubMed

• Cofactor(s):

• Effectors of protein activity:
  • the phosphorylation state affects DNA binding activity
  • interaction with MecA inhibits the transcriptional activity of Spo0A∼P PubMed

• Interactions:
  • KinC-Spo0A PubMed
  • Spo0A-Spo0E PubMed
  • Spo0A-SigA PubMed
  • Spo0A-Spo0B
  • SinI-Spo0A PubMed
  • MecA-Spo0A PubMed

• Localization:

Database entries

• Structure: 1QMP (with phosphorylated aspartate, Geobacillus stearothermophilus), 1FC3 (trans-activation domain, Geobacillus stearothermophilus), 1LQ1 (complex with DNA)

• UniProt: P06534

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: spo0A PubMed

• Expression browser: spo0A PubMed

• Sigma factor: SigA PubMed, SigH PubMed

• Regulation:
  • repressed under conditions that trigger sporulation (Spo0A) PubMed
  • repressed by casamino acids PubMed
  • repressed by SinR overexpression PubMed
  • repressed by soj PubMed
  • expression increases when drowth rate declines PubMed

• Regulatory mechanism:
  • Spo0A: transcription repression PubMed
  • Spo0A synthesis is subject to a post-transcriptional control mechanism such that translation of mRNAs originating from the SigA-dependent promoter is impeded due to RNA secondary structure PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

• Tony Wilkinson, York University, U.K. homepage
• Imrich Barak, Slovak Academy of Science, Bratislava, Slovakia homepage
• Charles Moran, Emory University, NC, USA homepage

References

Other original Publications

Additional publications: PubMed

TTTTT

ÜÜÜ

Mirjam Boonstra, Imke G de Jong, Graham Scholefield, Heath Murray, Oscar P Kuipers, Jan-Willem Veening
Spo0A regulates chromosome copy number during sporulation by directly binding to the origin of replication in Bacillus subtilis.
Mol Microbiol: 2013, 87(4);925-38
[PubMed:23301687] [WorldCat.org] [DOI] (I p)

Munehiro Asally, Mark Kittisopikul, Pau Rué, Yingjie Du, Zhenxing Hu, Tolga Çağatay, Andra B Robinson, Hongbing Lu, Jordi Garcia-Ojalvo, Gürol M Süel
Localized cell death focuses mechanical forces during 3D patterning in a biofilm.
Proc Natl Acad Sci U S A: 2012, 109(46);18891-6
[PubMed:23012477] [WorldCat.org] [DOI] (I p)

Fordyce A Davidson, Chung Seon-Yi, Nicola R Stanley-Wall
Selective heterogeneity in exoprotease production by Bacillus subtilis.
PLoS One: 2012, 7(6);e38574
[PubMed:22745669] [WorldCat.org] [DOI] (I p)