GlpQ
- 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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
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
- BsubCyc: BSU02130
- 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:
- Localization:
- extracellular (signal peptide) PubMed
Database entries
- BsubCyc: BSU02130
- UniProt: P37965
- KEGG entry: [3]
- E.C. number: 3.1.4.46
Additional information
Expression and regulation
- 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)