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
Sequences	Protein DNA DNA_with_flanks
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)