SpoIIAA

• Description: anti-anti-SigF
  
  

Gene name	spoIIAA
Synonyms
Essential	no
Product	anti-anti-SigF
Function	control of SigF activity
Metabolic function and regulation of this protein in SubtiPathways: Stress
MW, pI	12 kDa, 5.855
Gene length, protein length	351 bp, 117 aa
Immediate neighbours	spoIIAB, dacF
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: BSU23470

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: anti-sigma-factor antagonist family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylation on (Ser-58 OR Ser-59) by SpoIIABPubMed, PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions: SpoIIAB-SpoIIAA

• Localization:

Database entries

• Structure: 1TIL (complex with SpoIIAB, Geobacillus stearothermophilus), 1AUZ (NMR)

• Swiss prot entry: P10727

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: dacF-spoIIAA-spoIIAB-sigF

spoIIAA-spoIIAB-sigF

• Sigma factor: dacF: SigF, SigG

spoIIA: SigH

• Regulation: repressed by glucose (5.2-fold) PubMed, dacF: expressed during sporulation, spoIIAA: expressed early during sporulation
  • expressed under conditions that trigger sporulation (Spo0A) PubMed

• Regulatory mechanism: spoIIAA: activated by Spo0A and repressed by SinR
  • Spo0A: transcription activation 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
• Charles Moran, Emory University, NC, USA homepage

References

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

1. Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways. Metab Eng. 5: 133-149 PubMed
2. Lévine et al. (2006) Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes. Proteomics 6: 2157-2173 PubMed
3. Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6: 697-707 PubMed
4. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed