GlpK

• 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 Advanced_DNA
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

• Expression browser: 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)