Difference between revisions of "GlcT"

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(Original publications)
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|style="background:#ABCDEF;" align="center"|'''Function''' || control of glucose uptake
 
|style="background:#ABCDEF;" align="center"|'''Function''' || control of glucose uptake
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU13880 glcT]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/GlcT GlcT]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/GlcT GlcT]

Revision as of 08:59, 7 August 2012

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





























Categories containing this gene/protein

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

This gene is a member of the following regulons

The GlcT regulon: ptsG-ptsH-ptsI

The gene

Basic information

  • Locus tag: BSU13880

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

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:

Database entries

  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • 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

Your additional remarks

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