Difference between revisions of "ProJ"

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=References=
'''Additional publications:''' {{PubMed|21784929}}
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<pubmed>,21296969</pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:53, 27 October 2014

  • Description: glutamate 5-kinase

Gene name proJ
Synonyms yohA
Essential no
Product glutamate 5-kinase
Function osmoadaptive de novo production of proline
Gene expression levels in SubtiExpress: proJ
Metabolic function and regulation of this protein in SubtiPathways:
proJ
MW, pI 40 kDa, 5.296
Gene length, protein length 1113 bp, 371 aa
Immediate neighbours gltC, proH
Sequences Protein DNA DNA_with_flanks
Genetic context
ProJ context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ProJ expression.png




























Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, coping with hyper-osmotic stress

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU18470

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + L-glutamate = ADP + L-glutamate 5-phosphate (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s): ProB

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Regulation:
    • expressed under conditions of osmotic stress PubMed
    • induced by cold stress PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP817 (spc) available in the Stülke lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Adrienne Zaprasis, Monika Bleisteiner, Anne Kerres, Tamara Hoffmann, Erhard Bremer
Uptake of amino acids and their metabolic conversion into the compatible solute proline confers osmoprotection to Bacillus subtilis.
Appl Environ Microbiol: 2015, 81(1);250-9
[PubMed:25344233] [WorldCat.org] [DOI] (I p)

Jeanette Brill, Tamara Hoffmann, Monika Bleisteiner, Erhard Bremer
Osmotically controlled synthesis of the compatible solute proline is critical for cellular defense of Bacillus subtilis against high osmolarity.
J Bacteriol: 2011, 193(19);5335-46
[PubMed:21784929] [WorldCat.org] [DOI] (I p)

Tamara Hoffmann, Erhard Bremer
Protection of Bacillus subtilis against cold stress via compatible-solute acquisition.
J Bacteriol: 2011, 193(7);1552-62
[PubMed:21296969] [WorldCat.org] [DOI] (I p)