Difference between revisions of "GlcT"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ykvZ]]'', ''[[ptsG]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ykvZ]]'', ''[[ptsG]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU13880 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU13880 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU13880 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU13880 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU13880 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU13880 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:glcT_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:glcT_context.gif]]

Revision as of 10:03, 14 May 2013

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 DNA_with_flanks
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: 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

Your additional remarks

References

Reviews

Original publications

Additional publications: PubMed