Difference between revisions of "GlpK"

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Revision as of 12:51, 16 May 2013

  • Description: glycerol kinase

Gene name glpK
Synonyms
Essential no
Product glycerol kinase
Function glycerol utilization
Gene expression levels in SubtiExpress: glpK
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
Sequences Protein DNA DNA_with_flanks
Genetic context
GlpK context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
GlpK expression.png




























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)