GlcT

• Description: transcriptional antiterminator , controls expression of the ptsG-ptsH-ptsI operon
  
  

Gene name	glcT
Synonyms	ykwA
Essential	no
Product	transcriptional antiterminator of the ptsG-ptsH-ptsI operon
Function	control of glucose uptake
Interactions involving this protein in SubtInteract: GlcT
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	33,0 kDa, 7.01
Gene length, protein length	855 bp, 285 amino acids
Immediate neighbours	ykvZ, ptsG
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

carbon core metabolism, transcription factors and their control, RNA binding regulators, phosphoproteins

The gene

Basic information

• Locus tag: BSU13880

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: transcription antiterminator , RNA-binding protein, binds the ptsG RAT sequence

• Protein family: transcription antiterminator of the BglG/ SacY family

• Paralogous protein(s): LicT, SacT, SacY

Extended information on the protein

• Kinetic information:

• Domains:
  • RNA-binding domain (N-terminal, constitutive antiterminator)
  • 2x PTS regulation domains (PRDs) (C-terminal, neg. regulated by PtsG)

• Modification: phosphorylation (His104)

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • PtsH-GlcT

• Localization:

Database entries

• Structure: 3GWH (PRD-II) PubMed

• UniProt: O31691

• KEGG entry: [2]

Expression and regulation

• Operon:

• Expression browser: glcT PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant: available in Stülke lab:
  • GP109 (in frame deletion)
  • GP778 (replacement of glcT and the ptsG-ptsH-ptsI operon by a spc cassette)
  • GP926 (substitution of glcT and ptsG by a tet cassette)

• Expression vector:
  • pGP124 (full length, in pWH844), available in Stülke lab
  • pGP114 (amino acids 1-60, RNA-binding domain, in pWH844), available in Stülke lab
  • pGP230 (amino acids 1-60, RNA-binding domain with thrombin cleavage site, in pWH844), available in Stülke lab
  • pGP164 (both PRDs, in pWH844), in addition diverse expression vectors for phosphorylation site mutants and for RBD mutants (all in pWH844), available in Stülke lab
  • pGP424 (PRDI, in pWH844), available in Stülke lab
  • pGP425 (PRDII, in pWH844), available in Stülke lab
  • pGP442 (PRDI, in pGP570, with thrombin cleavage site), available in Stülke lab
  • pGP443 (PRDII, in pGP570, with thrombin cleavage site), available in Stülke lab
  • pGP575 (amino acids 1-60, RNA-binding domain with Strep-tag, in pGP574), available in Stülke lab

• lacZ fusion:

• GFP fusion:

• Antibody:

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

References

Reviews

Fabian M Commichau, Jörg Stülke
Trigger enzymes: bifunctional proteins active in metabolism and in controlling gene expression.
Mol Microbiol: 2008, 67(4);692-702
[PubMed:18086213] [WorldCat.org] [DOI] (P p)

J Stülke, M Arnaud, G Rapoport, I Martin-Verstraete
PRD--a protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria.
Mol Microbiol: 1998, 28(5);865-74
[PubMed:9663674] [WorldCat.org] [DOI] (P p)

Original publications

Sebastian Himmel, Christopher P Zschiedrich, Stefan Becker, He-Hsuan Hsiao, Sebastian Wolff, Christine Diethmaier, Henning Urlaub, Donghan Lee, Christian Griesinger, Jörg Stülke
Determinants of interaction specificity of the Bacillus subtilis GlcT antitermination protein: functionality and phosphorylation specificity depend on the arrangement of the regulatory domains.
J Biol Chem: 2012, 287(33);27731-42
[PubMed:22722928] [WorldCat.org] [DOI] (I p)

Dayté D Rodríguez, Christian Grosse, Sebastian Himmel, César González, Iñaki M de Ilarduya, Stefan Becker, George M Sheldrick, Isabel Usón
Crystallographic ab initio protein structure solution below atomic resolution.
Nat Methods: 2009, 6(9);651-3
[PubMed:19684596] [WorldCat.org] [DOI] (I p)

Oliver Schilling, Christina Herzberg, Tina Hertrich, Hanna Vörsmann, Dirk Jessen, Sebastian Hübner, Fritz Titgemeyer, Jörg Stülke
Keeping signals straight in transcription regulation: specificity determinants for the interaction of a family of conserved bacterial RNA-protein couples.
Nucleic Acids Res: 2006, 34(21);6102-15
[PubMed:17074746] [WorldCat.org] [DOI] (I p)

Oliver Schilling, Ines Langbein, Michael Müller, Matthias H Schmalisch, Jörg Stülke
A protein-dependent riboswitch controlling ptsGHI operon expression in Bacillus subtilis: RNA structure rather than sequence provides interaction specificity.
Nucleic Acids Res: 2004, 32(9);2853-64
[PubMed:15155854] [WorldCat.org] [DOI] (I e)

Matthias H Schmalisch, Steffi Bachem, Jörg Stülke
Control of the Bacillus subtilis antiterminator protein GlcT by phosphorylation. Elucidation of the phosphorylation chain leading to inactivation of GlcT.
J Biol Chem: 2003, 278(51);51108-15
[PubMed:14527945] [WorldCat.org] [DOI] (P p)

David B Greenberg, Jorg Stülke, Milton H Saier
Domain analysis of transcriptional regulators bearing PTS regulatory domains.
Res Microbiol: 2002, 153(8);519-26
[PubMed:12437213] [WorldCat.org] [DOI] (P p)

I Langbein, S Bachem, J Stülke
Specific interaction of the RNA-binding domain of the bacillus subtilis transcriptional antiterminator GlcT with its RNA target, RAT.
J Mol Biol: 1999, 293(4);795-805
[PubMed:10543968] [WorldCat.org] [DOI] (P p)

S Bachem, J Stülke
Regulation of the Bacillus subtilis GlcT antiterminator protein by components of the phosphotransferase system.
J Bacteriol: 1998, 180(20);5319-26
[PubMed:9765562] [WorldCat.org] [DOI] (P p)

J Stülke, I Martin-Verstraete, M Zagorec, M Rose, A Klier, G Rapoport
Induction of the Bacillus subtilis ptsGHI operon by glucose is controlled by a novel antiterminator, GlcT.
Mol Microbiol: 1997, 25(1);65-78
[PubMed:11902727] [WorldCat.org] [DOI] (P p)

Complete list of publications: PubMed