Difference between revisions of "GltA"

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(Expression and regulation)
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* '''Regulatory mechanism:'''  Activator: [[GltC]] [http://www.ncbi.nlm.nih.gov/sites/entrez/2548995 PubMed]; Repressor: [[TnrA]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11029411 PubMed], pos. regulated by a mutant form of [[GltR]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+9023181 PubMed]
* '''Regulatory mechanism:'''  Activator: [[GltC]] [http://www.ncbi.nlm.nih.gov/sites/entrez/2548995 PubMed]; Repressor: [[TnrA]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11029411 PubMed], pos. regulated by a mutant form of [[GltR]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+9023181 PubMed]
* '''Additional information:'''
* '''Additional information:''' subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed]
=Biological materials =
=Biological materials =

Revision as of 19:27, 24 February 2009

  • Description: large subunit of glutamate synthase

Gene name gltA
Essential no
Product glutamate synthase (large subunit)
Function glutamate biosynthesis
MW, pI 168 kDa, 5.47
Gene length, protein length 4560 bp, 1520 amino acids
Immediate neighbours gltC, gltB
Gene sequence (+200bp) Protein sequence
Caution: The sequence for this gene in SubtiList contains errors
Genetic context
GltA context.gif

The gene

Basic information

  • Coordinates: 2009283 - 2013842

Phenotypes of a mutant

auxotrophic for glutamate

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 2 L-glutamate + NADP(+) <=> L-glutamine + 2-oxoglutarate + NADPH
  • Protein family: glutamate synthase family
  • Paralogous protein(s): YerD

Extended information on the protein

  • Kinetic information:
  • Domains:
    • Glutamine amidotransferase type-2 domain (22-415)
    • Nucleotide binding domain (1060-1112)
  • Modification:
  • Cofactor(s): 3Fe-4S, FAD, FMN
  • Effectors of protein activity:
  • Interactions:
  • Localization: membrane associated PubMed, cytoplasm

Database entries

  • Structure:
  • Swiss prot entry: [3]
  • KEGG entry: [4]
  • E.C. number: [5]

Additional information

subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Regulation: induced by sugar PubMed, repressed by arginine PubMed, ammonium required PubMed
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

  • Mutant: GP807 (del gltAB::tet), GP222 (gltA under the control of p-xyl), available in Stülke lab
  • Expression vector:
  • GFP fusion:
  • Antibody:

Labs working on this gene/protein

Linc Sonenshein, Tufts University, Boston, MA, USA Homepage

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks


  1. Yoshida K, et al. (2003) Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box. Mol Microbiol 49(1): 157-65. PubMed
  2. Belitsky, B. R., and Sonenshein, A. L. (1995) Mutations in GltC that increase Bacillus subtilis gltA expression. J Bacteriol 177: 5696-5700.PubMed
  3. Belitsky, B. R., and Sonenshein, A. L. (2004) Modulation of activity of Bacillus subtilis regulatory proteins GltC and TnrA by glutamate dehydrogenase. J Bacteriol 186: 3399-3407.PubMed
  4. Bohannon, D. E., and Sonenshein, A. L. (1989) Positive regulation of glutamate biosynthesis in Bacillus subtilis. J Bacteriol 171: 4718-4727.PubMed
  5. Commichau, F. M., Wacker, I., Schleider, J., Blencke, H.-M., Reif, I., Tripal, P., and Stülke, J. (2007) Characterization of Bacillus subtilis mutants with carbon source-independent glutamate biosynthesis. J Mol Microbiol Biotechnol 12: 106-113. PubMed
  6. Commichau, F. M., Herzberg, C., Tripal, P., Valerius, O., and Stülke, J. (2007) A regulatory protein-protein interaction governs glutamate biosynthesis in Bacillus subtilis: The glutamate dehydrogenase RocG moonlights in controlling the transcription factor GltC. Mol Microbiol 65: 642-654. PubMed
  7. Picossi, S., Belitsky, B. R., and Sonenshein, A. L. (2007) Molecular mechanism of the regulation of Bacillus subtilis gltAB expression by GltC. J Mol Biol 365: 1298-1313. PubMed
  8. Wacker, I., Ludwig, H., Reif, I., Blencke, H. M., Detsch, C., and Stülke, J. (2003) The regulatory link between carbon and nitrogen metabolism in Bacillus subtilis: regulation of the gltAB operon by the catabolite control protein CcpA. Microbiology 149: 3001-3009.PubMed
  9. Belitsky BR, Sonenshein AL (1997) Altered transcription activation specificity of a mutant form of Bacillus subtilis GltR, a LysR family member. J Bacteriol 179:1035-1043 PubMed
  10. Belitsky, B. R., Wray, L. V., Jr., Fisher, S. H., Bohannon, D. E. & Sonenshein, A. L. (2000). Role of TnrA in nitrogen source-dependent repression of Bacillus subtilis glutamate synthase gene expression. J Bacteriol 182, 5939-5947. PubMed
  11. Commichau, F. M., Gunka, K., Landmann, J. J. & Stülke, J. (2008) Glutamate metabolism in Bacillus subtilis: Gene expression and enzyme activities evolved to avoid futile cycles and to allow rapid responses to perturbations in the system. J. Bacteriol. 190: 3557-3564. PubMed
  12. Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
  13. Hahne et al. (2008) From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8:4123-4136 PubMed