GltA

• Description: large subunit of glutamate synthase
  
  

Gene name	gltA
Synonyms
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 This image was kindly provided by SubtiList

The gene

Basic information

• Coordinates: 2009283 - 2013842

Phenotypes of a mutant

auxotrophic for glutamate

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• Operon: gltA-gltB

• Sigma factor: SigA

• Regulation: expression activated by glucose (11.21) PubMed, induced by sugar PubMed, repressed by arginine PubMed, ammonium required PubMed

• Regulatory mechanism: Activator: GltC PubMed; Repressor: TnrA PubMed, pos. regulated by a mutant form of GltR 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:

• lacZ fusion: pGP526 (in pAC7), pGP919 (in pAC5), available in Stülke lab

• GFP fusion:

• Antibody:

Labs working on this gene/protein

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

Jörg Stülke, University of Göttingen, Germany Homepage

References

1. Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways. Metab Eng. 5: 133-149 PubMed
2. 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
3. Belitsky, B. R., and Sonenshein, A. L. (1995) Mutations in GltC that increase Bacillus subtilis gltA expression. J Bacteriol 177: 5696-5700.PubMed
4. 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
5. Bohannon, D. E., and Sonenshein, A. L. (1989) Positive regulation of glutamate biosynthesis in Bacillus subtilis. J Bacteriol 171: 4718-4727.PubMed
6. 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
7. 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
8. 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
9. 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
10. 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
11. 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
12. 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
13. Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
14. Hahne et al. (2008) From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8:4123-4136 PubMed