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
Sequences	Protein DNA DNA_with_flanks
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
  • 1S131 ( stoA::tet), 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)