GlpK

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  • Description: glycerol kinase

Gene name glpK
Synonyms
Essential no
Product glycerol kinase
Function glycerol utilization
Interactions involving this protein in SubtInteract: GlpK
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
GlpK context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

utilization of specific carbon sources, phosphoproteins

This gene is a member of the following regulons

AbrB regulon, CcpA regulon, GlpP regulon

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:

Database entries

  • Structure: 3H46 (from Enterococcus casseliflavus, complex with glycerol) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • 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

Additional publications: PubMed

Joanne I Yeh, Regina Kettering, Ruth Saxl, Alexa Bourand, Emmanuelle Darbon, Nathalie Joly, Pierre Briozzo, Josef Deutscher
Structural characterizations of glycerol kinase: unraveling phosphorylation-induced long-range activation.
Biochemistry: 2009, 48(2);346-56
[PubMed:19102629] [WorldCat.org] [DOI] (I p)

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)