GlpQ

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  • Description: glycerolphosphate diester phosphodiesterase

Gene name glpQ
Synonyms ybeD
Essential no
Product glycerolphosphate diester phosphodiesterase
Function glycerol-3-phosphate utilization
Gene expression levels in SubtiExpress: glpQ
MW, pI 32 kDa, 9.263
Gene length, protein length 879 bp, 293 aa
Immediate neighbours ybeC, glpT
Sequences Protein DNA DNA_with_flanks
Genetic context
GlpQ context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
GlpQ expression.png















Categories containing this gene/protein

utilization of specific carbon sources, utilization of lipids

This gene is a member of the following regulons

CcpA regulon, GlpP regulon, PhoP regulon

The gene

Basic information

  • Locus tag: BSU02130

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: A glycerophosphodiester + H2O = an alcohol + sn-glycerol 3-phosphate (according to Swiss-Prot)
  • Protein family: glycerophosphoryl diester phosphodiesterase family (according to Swiss-Prot)

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure: 2PZ0 (the enzyme from Thermoanaerobacter tengcongensis) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulatory mechanism:
    • CcpA: transcription repression
    • GlpP: transcriptional antitermination via a protein-dependent RNA switch
    • PhoP: transcription activation PubMed
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original publications

Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862] [WorldCat.org] [DOI] (I p)

Liang Shi, Jun-Feng Liu, Xiao-Min An, Dong-Cai Liang
Crystal structure of glycerophosphodiester phosphodiesterase (GDPD) from Thermoanaerobacter tengcongensis, a metal ion-dependent enzyme: insight into the catalytic mechanism.
Proteins: 2008, 72(1);280-8
[PubMed:18214974] [WorldCat.org] [DOI] (I p)

H Antelmann, C Scharf, M Hecker
Phosphate starvation-inducible proteins of Bacillus subtilis: proteomics and transcriptional analysis.
J Bacteriol: 2000, 182(16);4478-90
[PubMed:10913081] [WorldCat.org] [DOI] (P p)

R P Nilsson, L Beijer, B Rutberg
The glpT and glpQ genes of the glycerol regulon in Bacillus subtilis.
Microbiology (Reading): 1994, 140 ( Pt 4);723-30
[PubMed:8012593] [WorldCat.org] [DOI] (P p)