GltA

• Description: large subunit of glutamate synthase
  
  

Gene name	gltA
Synonyms
Essential	no
Product	glutamate synthase (large subunit)
Function	glutamate biosynthesis
Metabolic function and regulation of this protein in SubtiPathways: Ammonium/ glutamate
MW, pI	168 kDa, 5.47
Gene length, protein length	4560 bp, 1520 amino acids
Immediate neighbours	gltC, gltB
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU18450

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 (according to Swiss-Prot) 2 L-glutamate + NADP(+) <=> L-glutamine + 2-oxoglutarate + NADPH

• Protein family: glutamate synthase family (according to Swiss-Prot) 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:

• UniProt: P39812

• KEGG entry: [3]

• E.C. number: 1.4.1.13 3 1.4.1.13]

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 fold) PubMed, induced by sugar PubMed, repressed by arginine PubMed, ammonium required PubMed
  • repressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed

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

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)

Fabian M Commichau, Katrin Gunka, Jens J Landmann, Jörg Stülke
Glutamate metabolism in Bacillus subtilis: gene expression and enzyme activities evolved to avoid futile cycles and to allow rapid responses to perturbations of the system.
J Bacteriol: 2008, 190(10);3557-64
[PubMed:18326565] [WorldCat.org] [DOI] (I p)

Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik, Robert L Switzer, Michael Hecker
Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.
J Bacteriol: 2008, 190(1);321-31
[PubMed:17981983] [WorldCat.org] [DOI] (I p)

Fabian M Commichau, Christina Herzberg, Philipp Tripal, Oliver Valerius, Jörg Stülke
A regulatory protein-protein interaction governs glutamate biosynthesis in Bacillus subtilis: the glutamate dehydrogenase RocG moonlights in controlling the transcription factor GltC.
Mol Microbiol: 2007, 65(3);642-54
[PubMed:17608797] [WorldCat.org] [DOI] (P p)

Fabian M Commichau, Ingrid Wacker, Jan Schleider, Hans-Matti Blencke, Irene Reif, Philipp Tripal, Jörg Stülke
Characterization of Bacillus subtilis mutants with carbon source-independent glutamate biosynthesis.
J Mol Microbiol Biotechnol: 2007, 12(1-2);106-13
[PubMed:17183217] [WorldCat.org] [DOI] (P p)

Silvia Picossi, Boris R Belitsky, Abraham L Sonenshein
Molecular mechanism of the regulation of Bacillus subtilis gltAB expression by GltC.
J Mol Biol: 2007, 365(5);1298-313
[PubMed:17134717] [WorldCat.org] [DOI] (P p)

Boris R Belitsky, Abraham L Sonenshein
Modulation of activity of Bacillus subtilis regulatory proteins GltC and TnrA by glutamate dehydrogenase.
J Bacteriol: 2004, 186(11);3399-407
[PubMed:15150225] [WorldCat.org] [DOI] (P p)

Ingrid Wacker, Holger Ludwig, Irene Reif, Hans-Matti Blencke, Christian Detsch, Jörg Stülke
The regulatory link between carbon and nitrogen metabolism in Bacillus subtilis: regulation of the gltAB operon by the catabolite control protein CcpA.
Microbiology (Reading): 2003, 149(Pt 10);3001-3009
[PubMed:14523131] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

Ken-ichi Yoshida, Hirotake Yamaguchi, Masaki Kinehara, Yo-hei Ohki, Yoshiko Nakaura, Yasutaro Fujita
Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box.
Mol Microbiol: 2003, 49(1);157-65
[PubMed:12823818] [WorldCat.org] [DOI] (P p)

B R Belitsky, L V Wray, S H Fisher, D E Bohannon, A L Sonenshein
Role of TnrA in nitrogen source-dependent repression of Bacillus subtilis glutamate synthase gene expression.
J Bacteriol: 2000, 182(21);5939-47
[PubMed:11029411] [WorldCat.org] [DOI] (P p)

B R Belitsky, A L Sonenshein
Mutations in GltC that increase Bacillus subtilis gltA expression.
J Bacteriol: 1995, 177(19);5696-700
[PubMed:7559360] [WorldCat.org] [DOI] (P p)

D E Bohannon, A L Sonenshein
Positive regulation of glutamate biosynthesis in Bacillus subtilis.
J Bacteriol: 1989, 171(9);4718-27
[PubMed:2548995] [WorldCat.org] [DOI] (P p)