Difference between revisions of "GlnA"

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* '''Operon:''' ''[[glnR]]-[[glnA]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/8636055 PubMed]
 
* '''Operon:''' ''[[glnR]]-[[glnA]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/8636055 PubMed]
  
* '''Sigma factor:''' [[SigA]]
+
* '''[[Sigma factor]]:''' [[SigA]]
  
 
* '''Regulation:''' expressed in the absence of glutamine [http://www.ncbi.nlm.nih.gov/sites/entrez/8636055 PubMed]
 
* '''Regulation:''' expressed in the absence of glutamine [http://www.ncbi.nlm.nih.gov/sites/entrez/8636055 PubMed]

Revision as of 09:09, 8 April 2009

  • Description: glutamine synthetase

Gene name glnA
Synonyms
Essential no
Product trigger enzyme: glutamine synthetase
Function glutamine biosynthesis, control of TnrA and GlnR activity
MW, pI 50 kDa, 4.874
Gene length, protein length 1332 bp, 444 aa
Immediate neighbours glnR, ynxB
Gene sequence (+200bp) Protein sequence
Genetic context
GlnA context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

auxotrophic for glutamine

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: K(M) for: Glu: 27 mM, ATP: 2.4 mM, ammonium: 0.18 mM; v(max): 3.7 µmol/min/mg
  • Domains: glutamate binding flap (aa 300 ... 306: protects unstable intermediates from abberant hydrolysis)
  • Modification: phosphorylated on ser/ thr/ tyr PubMed
  • Cofactor(s): Mg(2+)
  • Effectors of protein activity: feedback inhibition by glutamine, glutamine binds thhe entrance site for glutamate
  • Localization:

Database entries

  • Structure:
  • Swiss prot entry:
  • KEGG entry: [3]
  • E.C. number: 6.3.1.2


Additional information

GlnA is a homooligomer of 12 subunits

Expression and regulation

  • Regulation: expressed in the absence of glutamine PubMed
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Susan Fisher, Boston, USA homepage

Your additional remarks

References

  1. 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
  2. Brown, S. W., and A. L. Sonenshein. 1996. Autogenous regulation of the Bacillus subtilis glnRA operon. J. Bacteriol. 178: 2450-2454. PubMed
  3. Wray LV Jr, Zalieckas JM, Fisher SH. (2001) Bacillus subtilis glutamine synthetase controls gene expression through protein-protein interaction with transcription factor TnrA. Cell 107:427-435. PubMed
  4. Fisher, S. H., and Wray, L. V., Jr. (2006) Feedback-resistant mutations in Bacillus subtilis glutamine synthetase are clustered in the active site. J Bacteriol 188: 5966-5974. PubMed
  5. Fisher SH, Sonenshein AL (1984) Bacillus subtilis glutamine synthetase mutants pleiotropically altered in catabolite repression. J Bacteriol 157:612-621. PubMed
  6. Fisher, S. H., Brandenburg, J. L. & Wray, L. V. (2002). Mutations in Bacillus subtilis glutamine synthetase that block its interaction with transcription factor TnrA. Mol Microbiol 45, 627-635. PubMed
  7. Schreier, H. J., Brown, S. W., Hirschi, K. D., Nomellini, J. F. & Sonenshein, A. L. (1989). Regulation of Bacillus subtilis glutamine synthetase gene expression by the product of the glnR gene. J Mol Biol 210, 51-63. PubMed
  8. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed