GlnA

• 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
Gene sequence (+200bp)	Protein sequence
Genetic context 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]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• 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

• Interactions: GlnR-GlnA, GlnA-TnrA (only the feedback-inhibited enzyme interacts with TnrA and GlnR)

• Localization:

Database entries

• Structure:

• Swiss prot entry:

• KEGG entry: [3]

• E.C. number: 6.3.1.2

Additional information

GlnA is a homooligomer of 12 subunits

Expression and regulation

• Operon: glnR-glnA PubMed

• Sigma factor: SigA

• Regulation: expressed in the absence of glutamine PubMed

• Regulatory mechanism: repressed by GlnR-GlnA complex PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody: available in Karl Forchhammer lab

Labs working on this gene/protein

Susan Fisher, Boston, USA homepage

References

1. 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 PubMed
2. Brown, S. W., and A. L. Sonenshein. 1996. Autogenous regulation of the Bacillus subtilis glnRA operon. J. Bacteriol. 178: 2450-2454. PubMed
3. 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. PubMed
4. 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. PubMed
5. Fisher SH, Sonenshein AL (1984) Bacillus subtilis glutamine synthetase mutants pleiotropically altered in catabolite repression. J Bacteriol 157:612-621. PubMed
6. 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. PubMed
7. 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. PubMed
8. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed