GlpK

• 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

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions: PtsH-GlpK

• Localization:

Database entries

• Structure: 3H46 (from Enterococcus casseliflavus, complex with glycerol) PubMed

• UniProt: P18157

• KEGG entry: [3]

• E.C. number: 2.7.1.30

Expression and regulation

• Operon: glpF-glpK PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by glucose (8-fold) (CcpA) PubMed
  • induction by glycerol (GlpP) PubMed

• Regulatory mechanism:
  • CcpA: transcription repression PubMed
  • GlpP-dependent RNA switch (transcriptional antitermination) PubMed
  • AbrB: transcription activation PubMed

• 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

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)