GlpQ

• 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 This image was kindly provided by SubtiList

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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)

• Paralogous protein(s): YhdW, YqiK

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:
  • extracellular (signal peptide) PubMed

Database entries

• Structure: 2PZ0 (the enzyme from Thermoanaerobacter tengcongensis) PubMed

• UniProt: P37965

• KEGG entry: [3]

• E.C. number: 3.1.4.46

Expression and regulation

• Operon:
  • glpT-glpQ PubMed
  • glpQ

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by glucose (6.2-fold) (CcpA) PubMed
  • induced by glycerol (GlpP) PubMed
  • glpQ: induced by phosphate limitation (PhoP) PubMed

• 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:

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)