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
Gene expression levels in SubtiExpress: glcT
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
Sequences	Protein DNA Advanced_DNA
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
  • 3RIO (RBD-PRD-I) 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: GP1224 (spc, based on pGP1870), available in the Stülke lab

• YFP fusion: GP1228 (spc, based on pGP1871), available in the Stülke lab

• FLAG-tag construct: GP1220 (spc, based on pGP1331), available in the Stülke lab

• 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

Additional publications: PubMed

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)

Sebastian Himmel, Sebastian Wolff, Stefan Becker, Donghan Lee, Christian Griesinger
Detection and identification of protein-phosphorylation sites in histidines through HNP correlation patterns.
Angew Chem Int Ed Engl: 2010, 49(47);8971-4
[PubMed:20939030] [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)