Difference between revisions of "GlpQ"

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Revision as of 13:24, 18 April 2012

  • Description: glycerolphosphate diester phosphodiesterase

Gene name glpQ
Synonyms ybeD
Essential no
Product glycerolphosphate diester phosphodiesterase
Function glycerol-3-phosphate utilization
MW, pI 32 kDa, 9.263
Gene length, protein length 879 bp, 293 aa
Immediate neighbours ybeC, glpT
Get the DNA and protein sequences
(Barbe et al., 2009)
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:
  • Domains:
  • Modification:
  • Cofactor(s):
  • 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

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)