Difference between revisions of "Sandbox"

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−
* '''Description:''' unknown <br/><br/>
+
* '''Description:''' glutamine synthetase <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
−
|''ymcB''
+
|''glnA''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''
 
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Product''' || unknown
+
|style="background:#ABCDEF;" align="center"| '''Product''' || trigger enzyme: glutamine synthetase
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"|'''Function''' || unknown
+
|style="background:#ABCDEF;" align="center"|'''Function''' || glutamine biosynthesis, control of TnrA and GlnR activity
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 57 kDa, 6.873  
+
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 50 kDa, 4.874  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1527 bp, 509 aa  
+
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1332 bp, 444 aa  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[kbl]]'', ''[[ymcA]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[glnR]]'', ''[[ynxB]]''
 
|-
 
|-
−
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB13574&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
+
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB13630&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
 
|-
 
|-
−
|colspan="2" | '''Genetic context''' <br/> [[Image:YmcB_context.png]]
+
|colspan="2" | '''Genetic context''' <br/> [[Image:glnA_context.gif]]
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
|-
 
|-
Line 38: Line 38:
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
 +
 +
auxotrophic for glutamine
  
 
=== Database entries ===
 
=== Database entries ===
  
−
* '''DBTBS entry:''' no entry
+
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/glnRA.html]
  
−
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG13418]
+
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10425]
  
 
=== Additional information===
 
=== Additional information===
Line 60: Line 62:
 
=== Extended information on the protein ===
 
=== Extended information on the protein ===
  
−
* '''Kinetic information:'''
+
* '''Kinetic information:''' K(M) for: Glu: 27 mM, ATP: 2.4 mM, ammonium: 0.18 mM; v(max): 3.7 µmol/min/mg
  
−
* '''Domains:'''  
+
* '''Domains:''' glutamate binding flap (aa 300 ... 306: protects unstable intermediates from abberant hydrolysis)
  
−
* '''Modification:'''
+
* '''Modification:''' phosphorylated on ser/ thr/ tyr [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed]
  
−
* '''Cofactor(s):'''
+
* '''Cofactor(s):''' Mg(2+)
  
−
* '''Effectors of protein activity:'''
+
* '''Effectors of protein activity:''' feedback inhibition by glutamine, glutamine binds thhe entrance site for glutamate
  
−
* '''Interactions:'''
+
* '''Interactions:''' [[TnrA]]-[[GlnA]],  [[GlnR]]-[[GlnA]], (only the feedback-inhibited enzyme interacts with [[TnrA]] and [[GlnR]])
  
 
* '''Localization:''' Cytoplasm
 
* '''Localization:''' Cytoplasm
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* '''Swiss prot entry:'''
 
* '''Swiss prot entry:'''
  
−
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU17010]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU17460]
 +
 
 +
* '''E.C. number:''' 6.3.1.2
  
−
* '''E.C. number:'''
 
  
 
=== Additional information===
 
=== Additional information===
 +
 +
GlnA is a homooligomer of 12 subunits
  
 
=Expression and regulation=
 
=Expression and regulation=
  
−
* '''Operon:'''  
+
* '''Operon:''' ''[[glnR]]-[[glnA]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/8636055 PubMed]
  
−
* '''[[Sigma factor]]:'''  
+
* '''[[Sigma factor]]:''' [[SigA]]
  
−
* '''Regulation:'''  
+
* '''Regulation:''' expressed in the absence of glutamine [http://www.ncbi.nlm.nih.gov/sites/entrez/8636055 PubMed]
  
−
* '''Regulatory mechanism:'''  
+
* '''Regulatory mechanism:''' repressed by [[GlnR]]-[[GlnA]] complex [http://www.ncbi.nlm.nih.gov/sites/entrez/8636055 PubMed]
  
 
* '''Additional information:'''
 
* '''Additional information:'''
Line 100: Line 105:
 
=Biological materials =
 
=Biological materials =
  
−
* '''Mutant:''' GP1109 (spc), available in [[Stülke]] lab
+
* '''Mutant:'''
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''
Line 110: Line 115:
 
* '''two-hybrid system:'''  
 
* '''two-hybrid system:'''  
  
−
* '''Antibody:'''
+
* '''Antibody:''' available in [[Karl Forchhammer]] lab
  
 
=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
 +
 +
[[Susan Fisher]], Boston, USA [http://www.bumc.bu.edu/microbiology/research/susan-h-fisher-phd/ homepage]
  
 
=Your additional remarks=
 
=Your additional remarks=
Line 118: Line 125:
 
=References=
 
=References=
  
 +
# L&#233;vine 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 [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed]
 +
# Brown, S. W., and A. L. Sonenshein. 1996. Autogenous regulation of the ''Bacillus subtilis glnRA'' operon. J. Bacteriol. 178: 2450-2454. [http://www.ncbi.nlm.nih.gov/sites/entrez/8636055 PubMed]
 +
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/11719184 PubMed]
 +
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/16885465 PubMed]
 +
# Fisher SH, Sonenshein AL (1984) ''Bacillus subtilis'' glutamine synthetase mutants pleiotropically altered in catabolite repression. J Bacteriol 157:612-621. [http://www.ncbi.nlm.nih.gov/sites/entrez/6141156 PubMed]
 +
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12139611 PubMed]
 +
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/2573733 PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]

Revision as of 02:23, 30 April 2009

  • 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
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
GlnA context.gif
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]

Additional information

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
  • Localization: Cytoplasm

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

  • Regulation: expressed in the absence of glutamine PubMed
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:

Labs working on this gene/protein

Susan Fisher, Boston, USA homepage

Your additional remarks

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
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