StoA

• Description: thiol-disulfide oxidoreductase, with thioredoxin-like domain, required for the synthesis of the endospore peptidoglycan cortex
  
  

Gene name	stoA
Synonyms	spoIVH, ykvV
Essential	no
Product	thiol-disulfide oxidoreductase
Function	spore cortex formation
Gene expression levels in SubtiExpress: stoA
Interactions involving this protein in SubtInteract: StoA
MW, pI	18 kDa, 5.297
Gene length, protein length	495 bp, 165 aa
Immediate neighbours	ykvU, zosA
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

sporulation proteins

This gene is a member of the following regulons

SigE regulon, SigG regulon

The gene

Basic information

• Locus tag: BSU13840

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: reduction of intramolecular disulfide bonds in SpoVD PubMed

• Protein family: thioredoxin domain (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:
  • forespore envelope PubMed

Database entries

• Structure: 3ERW

• UniProt: O31687

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • ykvU-stoA PubMed
  • stoA PubMed

• Expression browser: stoA PubMed

• Sigma factor:
  • ykvU: SigE PubMed
  • stoA: SigG PubMed

• Regulation:
  • expressed during sporulation (SigE, SigG) PubMed

• Regulatory mechanism:

• Additional information:
  • A ncRNA is predicted between stoA and zosA PubMed

Biological materials

• Mutant:
  • 1S130 ( stoA::cat), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Lars Hederstedt, University of Lund, Sweden Homepage

References

Reviews

Patrick Eichenberger
The red-ox status of a penicillin-binding protein is an on/off switch for spore peptidoglycan synthesis in Bacillus subtilis.
Mol Microbiol: 2010, 75(1);10-2
[PubMed:19919674] [WorldCat.org] [DOI] (I p)