Difference between revisions of "GlcT"
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=== Additional information=== | === Additional information=== | ||
+ | |||
+ | = Categories containing this gene/protein = | ||
+ | {{SubtiWiki category|[[carbon core metabolism]]}}, | ||
+ | {{SubtiWiki category|[[transcription factors and their control]]}}, | ||
+ | {{SubtiWiki category|[[RNA binding regulators]]}}, | ||
+ | {{SubtiWiki category|[[phosphoproteins]]}} | ||
=The protein= | =The protein= | ||
Revision as of 17:00, 30 November 2010
- 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 |
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
|
Contents
The gene
Basic information
- Locus tag: BSU13880
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
Categories containing this gene/protein
carbon core metabolism, transcription factors and their control, RNA binding regulators, phosphoproteins
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
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:
- Localization:
Database entries
- UniProt: O31691
- KEGG entry: [2]
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: available in Stülke lab:
- 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
Original publications
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