GlpP

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Gene name glpP
Synonyms
Essential no
Product transcriptional antiterminator
Function regulation of glycerol and glycerol-3-phosphate utilization
Gene expression levels in SubtiExpress: glpP
Metabolic function and regulation of this protein in SubtiPathways:
Sugar catabolism
MW, pI 21 kDa, 8.104
Gene length, protein length 576 bp, 192 aa
Immediate neighbours yhxA, glpF
Sequences Protein DNA DNA_with_flanks
Genetic context
GlpP context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
GlpP expression.png




























Categories containing this gene/protein

utilization of specific carbon sources, utilization of lipids, transcription factors and their control, RNA binding regulators

This gene is a member of the following regulons

The GlpP regulon: glpF-glpK-glpD, glpT-glpQ

The gene

Basic information

  • Locus tag: BSU09270

Phenotypes of a mutant

Database entries

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

Additional information

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:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • 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

Your additional remarks

References

Jamie Richards, Quansheng Liu, Olivier Pellegrini, Helena Celesnik, Shiyi Yao, David H Bechhofer, Ciarán Condon, Joel G Belasco
An RNA pyrophosphohydrolase triggers 5'-exonucleolytic degradation of mRNA in Bacillus subtilis.
Mol Cell: 2011, 43(6);940-9
[PubMed:21925382] [WorldCat.org] [DOI] (I p)

Emmanuelle Darbon, Pascale Servant, Sandrine Poncet, Josef Deutscher
Antitermination by GlpP, catabolite repression via CcpA and inducer exclusion triggered by P-GlpK dephosphorylation control Bacillus subtilis glpFK expression.
Mol Microbiol: 2002, 43(4);1039-52
[PubMed:11929549] [WorldCat.org] [DOI] (P p)

E Glatz, A Farewell, B Rutberg
The Bacillus subtilis glpD leader and antiterminator protein GlpP provide a target for glucose repression in Escherichia coli.
FEMS Microbiol Lett: 1998, 162(1);93-6
[PubMed:9595668] [WorldCat.org] [DOI] (P p)

Elisabeth Glatz, Martin Persson, Blanka Rutberg
Antiterminator protein GlpP of Bacillus subtilis binds to glpD leader mRNA.
Microbiology (Reading): 1998, 144 ( Pt 2);449-456
[PubMed:9493382] [WorldCat.org] [DOI] (P p)

E Glatz, R P Nilsson, L Rutberg, B Rutberg
A dual role for the Bacillus subtilis glpD leader and the GlpP protein in the regulated expression of glpD: antitermination and control of mRNA stability.
Mol Microbiol: 1996, 19(2);319-28
[PubMed:8825777] [WorldCat.org] [DOI] (P p)

L Beijer, R P Nilsson, C Holmberg, L Rutberg
The glpP and glpF genes of the glycerol regulon in Bacillus subtilis.
J Gen Microbiol: 1993, 139(2);349-59
[PubMed:8436953] [WorldCat.org] [DOI] (P p)

C Holmberg, L Rutberg
An inverted repeat preceding the Bacillus subtilis glpD gene is a conditional terminator of transcription.
Mol Microbiol: 1992, 6(20);2931-8
[PubMed:1479885] [WorldCat.org] [DOI] (P p)

C Holmberg, B Rutberg
Expression of the gene encoding glycerol-3-phosphate dehydrogenase (glpD) in Bacillus subtilis is controlled by antitermination.
Mol Microbiol: 1991, 5(12);2891-900
[PubMed:1809833] [WorldCat.org] [DOI] (P p)

V Lindgren, L Rutberg
Genetic control of the glp system in Bacillus subtilis.
J Bacteriol: 1976, 127(3);1047-57
[PubMed:182672] [WorldCat.org] [DOI] (P p)