GltC

• Description: Transcriptional activator of the gltA-gltB operon. Activates expression of the operon in the absence of arginine.
  
  

Gene name	gltC
Synonyms
Essential	No
Product	transcriptional regulator (LysR family)
Function	positive regulation of the glutamate synthase operon (gltAB)
Interactions involving this protein in SubtInteract: GltC
Metabolic function and regulation of this protein in SubtiPathways: Ammonium/ glutamate
MW, pI	33.9 kDa, 5.62
Gene length, protein length	900 bp, 300 amino acids
Immediate neighbours	gltA, proJ
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, transcription factors and their control

The GltC regulon:

• gltA-gltB

The gene

Basic information

• Locus tag: BSU18460

Phenotypes of a mutant

gltC mutants are auxotrophic for glutamate.

Database entries

• DBTBS entry: [1]

• SubtiList entry:[2]

Additional information

Expression

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: transcription activation of the gltA-gltB operon PubMed

• Protein family: LysR family PubMed

• Paralogous protein(s): none, but there are 19 members of the LysR family in B. subtilis

Extended information on the protein

• Kinetic information:

• Domains: DNA-binding helix-turn-helix motif: AA 18 ... 37

• Modification:

• Cofactor(s):

• Effectors of protein activity: 2-oxoglutarate stimulates transcription activation, glutamate inhibits transcription activation PubMed

• Interactions:
  • active as dimer
  • GltC-RocG, This interaction takes place in the presence of glutamate. It prevents the transcription activation of the gltA-gltB operon. Note that RocG expression is strongly regulated by carbon and nitrogen sources, respectively. PubMed

• Localization:

Database entries

• Structure:

• UniProt: P20668

• KEGG entry: [3]

Expression and regulation

• Operon: gltC (according to DBTBS)

• Expression browser: gltC PubMed

• Sigma factor: SigA PubMed

• Regulation: autoregulation by GltC PubMed

• Regulatory mechanism: autorepression PubMed

• Database entries: DBTBS

• Additional information:

Biological materials

• Mutant: GP344 (erm), GP738 (spc) (available in Stülke lab)

• Expression vector:
  • for expression, purification in E. coli with N-terminal His-tag, in pWH844: pGP903, available in Stülke lab
  • for expression, purification in E. coli with C-terminal Strep-tag, in pET3C: pGP951, available in Stülke lab

• lacZ fusion:

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab

• Antibody: available in Stülke lab

Labs working on this gene/protein

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

Jörg Stülke, University of Göttingen, Germany Homepage

Fabian Commichau University of Göttingen, Germany Homepage

References

Reviews

Katrin Gunka, Fabian M Commichau
Control of glutamate homeostasis in Bacillus subtilis: a complex interplay between ammonium assimilation, glutamate biosynthesis and degradation.
Mol Microbiol: 2012, 85(2);213-24
[PubMed:22625175] [WorldCat.org] [DOI] (I p)

Sabine Brantl, Andreas Licht
Characterisation of Bacillus subtilis transcriptional regulators involved in metabolic processes.
Curr Protein Pept Sci: 2010, 11(4);274-91
[PubMed:20408793] [WorldCat.org] [DOI] (I p)

Original Publications

Katrin Gunka, Joseph A Newman, Fabian M Commichau, Christina Herzberg, Cecilia Rodrigues, Lorraine Hewitt, Richard J Lewis, Jörg Stülke
Functional dissection of a trigger enzyme: mutations of the bacillus subtilis glutamate dehydrogenase RocG that affect differentially its catalytic activity and regulatory properties.
J Mol Biol: 2010, 400(4);815-27
[PubMed:20630473] [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)

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)