Difference between revisions of "GlnA"

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=References=
 
=References=
  
# 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 [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed]
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<pubmed> 2573733, 8636055, 19233925, 16493705, 11719184, 16885465, 6141156, 12139611 </pubmed>
# Brown, S. W., and A. L. Sonenshein. 1996. Autogenous regulation of the ''Bacillus subtilis glnRA'' operon. J. Bacteriol. 178: 2450-2454. [http://www.ncbi.nlm.nih.gov/sites/entrez/8636055 PubMed]
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# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/11719184 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/16885465 PubMed]
 
# Fisher SH, Sonenshein AL (1984) ''Bacillus subtilis'' glutamine synthetase mutants pleiotropically altered in catabolite repression. J Bacteriol 157:612-621. [http://www.ncbi.nlm.nih.gov/sites/entrez/6141156 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12139611 PubMed]
 
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/2573733 PubMed]
 
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]

Revision as of 18:05, 22 May 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
Get the DNA and protein sequences
(Barbe et al., 2009)
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: glutamine synthetase family (according to Swiss-Prot)
  • 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: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure:


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. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed