Difference between revisions of "OppA"

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* '''Regulation:'''  
 
* '''Regulation:'''  
 +
** expressed in the absence of good nitrogen sources (glutamine or ammonium) ([[TnrA]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/12823818 PubMed]
 
** repressed during exponential growth ([[ScoC]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/10383984 PubMed]
 
** repressed during exponential growth ([[ScoC]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/10383984 PubMed]
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
 +
** [[TnrA]]: transcription activation [http://www.ncbi.nlm.nih.gov/sites/entrez/12823818 PubMed]
 
** [[ScoC]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/10383984 PubMed]
 
** [[ScoC]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/10383984 PubMed]
  

Revision as of 17:41, 11 June 2009

  • Description: oligopeptide ABC transporter (binding protein)

Gene name oppA
Synonyms spo0KA
Essential no
Product oligopeptide ABC transporter (binding protein)
Function initiation of sporulation, competence development
MW, pI 61 kDa, 5.722
Gene length, protein length 1635 bp, 545 aa
Immediate neighbours trpS, oppB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
OppA context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU11430

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: bacterial solute-binding protein 5 family (according to Swiss-Prot)
  • Paralogous protein(s): DppE

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on (Tyr-301 OR Tyr-303) AND Thr-470 PubMed
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cell membrane (according to Swiss-Prot), extracellular (signal peptide) PubMed, membrane PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
    • expressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed
    • repressed during exponential growth (ScoC) PubMed
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

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)

  1. Voigt et al. (2009) Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis. J Mol Microbiol Biotechnol. 16: 53-68 PubMed
  2. Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 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