Difference between revisions of "GlpK"
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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P18157 P18157] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P18157 P18157] | ||
− | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU09290] |
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.1.30 2.7.1.30] | * '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.1.30 2.7.1.30] |
Revision as of 02:30, 25 June 2009
- Description: glycerol kinase
Gene name | glpK |
Synonyms | |
Essential | no |
Product | glycerol kinase |
Function | glycerol utilization |
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism | |
MW, pI | 54 kDa, 4.985 |
Gene length, protein length | 1488 bp, 496 aa |
Immediate neighbours | glpF, glpD |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU09290
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + glycerol = ADP + sn-glycerol 3-phosphate (according to Swiss-Prot)
- Protein family: FGGY kinase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- Structure:
- Swiss prot entry: P18157
- KEGG entry: [3]
- E.C. number: 2.7.1.30
Additional information
Expression and regulation
- 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
Emmanuelle Darbon, Pascale Servant, Sandrine Poncet, Josef Deutscher
Antitermination by GlpP, catabolite repression via CcpA and inducer exclusion triggered by P-GlpK dephosphorylation control Bacillus subtilis glpFK expression.
Mol Microbiol: 2002, 43(4);1039-52
[PubMed:11929549]
[WorldCat.org]
[DOI]
(P p)
V Charrier, E Buckley, D Parsonage, A Galinier, E Darbon, M Jaquinod, E Forest, J Deutscher, A Claiborne
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: 1997, 272(22);14166-74
[PubMed:9162046]
[WorldCat.org]
[DOI]
(P p)
Christina Wehtje, Lena Beijer, Rune-Pär Nilsson, Blanka Rutberg
Mutations in the glycerol kinase gene restore the ability of a ptsGHI mutant of Bacillus subtilis to grow on glycerol.
Microbiology (Reading): 1995, 141 ( Pt 5);1193-1198
[PubMed:7773413]
[WorldCat.org]
[DOI]
(P p)
L Beijer, L Rutberg
Utilisation of glycerol and glycerol 3-phosphate is differently affected by the phosphotransferase system in Bacillus subtilis.
FEMS Microbiol Lett: 1992, 100(1-3);217-20
[PubMed:1335945]
[WorldCat.org]
[DOI]
(P p)