Difference between revisions of "StoA"

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=== Additional information===
 
=== Additional information===
 
 
  
  
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* '''Additional information:'''
 
* '''Additional information:'''
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** A [[ncRNA]] is predicted between ''[[stoA]]'' and ''[[zosA]]'' {{PubMed|20525796}}
  
 
=Biological materials =
 
=Biological materials =
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<pubmed> 19919674 </pubmed>
 
<pubmed> 19919674 </pubmed>
 
==Original Publications==
 
==Original Publications==
<pubmed>,12662922,15292147,15342593, 19144642 19919673 </pubmed>
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<pubmed>,12662922,15292147,15342593, 19144642 19919673 20525796</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 18:31, 4 May 2011

  • 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
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
YkvV context.gif
This image was kindly provided by SubtiList



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

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

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

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Lars Hederstedt, University of Lund, Sweden Homepage

Your additional remarks

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)

Original Publications