Difference between revisions of "GlpK"
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# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/1335945 PubMed] | # 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/1335945 PubMed] | ||
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/9162046 PubMed] | # 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/9162046 PubMed] |
Revision as of 00:48, 3 April 2009
- Description: glycerol kinase
Gene name | glpK |
Synonyms | |
Essential | no |
Product | glycerol kinase |
Function | glycerol utilization |
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 This image was kindly provided by SubtiList
|
Contents
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: [3]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor: SigA
- Regulation: repressed by glucose (CcpA) , carbon catabolite repression, induction by glycerol
- Regulatory mechanism: CcpA: transcription repression, 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
- 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
- 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
- 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
- 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
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed