GlpP

• Description: transcriptional antiterminator of the glpT-glpQ and glpF-glpK-glpD operons
  
  

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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

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

The gene

Basic information

• Locus tag: BSU09270

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: P30300

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: yhxA-glpP PubMed

• Expression browser: glpP PubMed

• Sigma factor: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:
  • half-life of the mRNA: 3.7 min PubMed
  • the mRNA is stabilized in rppH and rnjA mutants PubMed
  • the mRNA is subject to degradation by RNase J1 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Josef Deutscher, Paris-Grignon, France

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)