GlpK

• Description: glycerol kinase
  
  

Gene name	glpK
Synonyms
Essential	no
Product	glycerol kinase
Function	glycerol utilization
MW, pI	54 kDa, 4.985
Gene length, protein length	1488 bp, 496 aa
Immediate neighbours	glpF, glpD
Gene sequence (+200bp)	Protein sequence
Caution: The sequence for this gene in SubtiList contains errors
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Coordinates:

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• Swiss prot entry:

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: glpF-glpK

• Sigma factor: SigA

• Regulation: expression activated by glucose (CcpA) PubMed, carbon catabolite repression, induction by glycerol

• Regulatory mechanism: 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

References

1. Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways. Metab Eng. 5: 133-149 PubMed
2. Beijer L, Rutberg L (1992) Utilisation of glycerol and glycerol-3-phosphate is differently affected by the phosphotransferase system in Bacillus subtilis. FEMS Microbiol Lett 100:217-220. PubMed
3. Charrier V, Buckley E, Parsonage D, Galinier A, Darbon E, Jaquinod M, Forest E, Deutscher J, Claiborne A (1997) 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 272:14166-14174. PubMed
4. Darbon E, Servant P, Poncet S, Deutscher J (2002) Antitermination by GlpP, catabolite repression via CcpA and inducer exclusion triggered by P~GlpK dephosphorylation control Bacillus subtilis glpFK expression. Mol Microbiol 43:1039-1052. PubMed
5. Wehtje C, Beijer L, Nilsson RP, Rutberg B (1995) Mutations in the glycerol kinase gene restore the ability of a ptsGHI mutant of Bacillus subtilis to grow on glycerol. Microbiology 141:1193-1198. PubMed
6. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed