Difference between revisions of "GlpK"

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|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/glpK_nucleotide.txt    Gene sequence      (+200bp)  ]'''  
 
|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/glpK_nucleotide.txt    Gene sequence      (+200bp)  ]'''  
 
|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/glpK_protein.txt Protein sequence]'''
 
|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/glpK_protein.txt Protein sequence]'''
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|-
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|colspan="2" style="background:#FAF8CC;color:#FF0000" align="center" | '''Caution: The sequence for this gene in SubtiList contains errors
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:glpK_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:glpK_context.gif]]

Revision as of 14:00, 23 February 2009

  • Description: write here

Gene name glpK
Synonyms
Essential no
Product glycerol kinase (EC 2.7.1.30)
Function
MW, pI 54 kDa, 4.985
Gene length, protein length 1488 bp, 496 aa
Immediate neighbours glpF, glpD
Gene sequence (+200bp) Protein sequence
Caution: The sequence for this gene in SubtiList contains errors
Genetic context
GlpK context.gif



The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

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:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization:

Database entries

  • Structure:
  • Swiss prot entry:
  • KEGG entry:
  • E.C. number:

Additional information

Expression and regulation

  • Regulation: carbon catabolite repression, induction by glycerol
  • Regulatory mechanism: catabolite repression: repression by CcpA, induction: GlpP-dependent RNA switch (transcriptional antitermination)
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Josef Deutscher, Paris-Grignon, France

Your additional remarks

References

  1. Beijer L, Rutberg L (1992) Utilisation of glycerol and glycerol-3-phosphate is differently affected by the phosphotransferase system in Bacillus subtilis. FEMS Microbiol Lett 100:217-220. PubMed
  2. Charrier V, Buckley E, Parsonage D, Galinier A, Darbon E, Jaquinod M, Forest E, Deutscher J, Claiborne A (1997) Cloning and sequencing of two enterococcal glpK genes and regulation of the encoded glycerol kinases by phosphoenolpyruvate-dependent, phosphotransferase system-catalyzed phosphorylation of a single histidyl residue. J Biol Chem 272:14166-14174. PubMed
  3. Darbon E, Servant P, Poncet S, Deutscher J (2002) Antitermination by GlpP, catabolite repression via CcpA and inducer exclusion triggered by P~GlpK dephosphorylation control Bacillus subtilis glpFK expression. Mol Microbiol 43:1039-1052. PubMed
  4. Wehtje C, Beijer L, Nilsson RP, Rutberg B (1995) Mutations in the glycerol kinase gene restore the ability of a ptsGHI mutant of Bacillus subtilis to grow on glycerol. Microbiology 141:1193-1198. PubMed
  5. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed