Difference between revisions of "GlcT"
Line 12: | Line 12: | ||
|style="background:#ABCDEF;" align="center"| '''Product''' || transcriptional antiterminator of the ''[[ptsG]]-[[ptsH]]-[[ptsI]]'' operon | |style="background:#ABCDEF;" align="center"| '''Product''' || transcriptional antiterminator of the ''[[ptsG]]-[[ptsH]]-[[ptsI]]'' operon | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || transcriptional antiterminator | + | |style="background:#ABCDEF;" align="center"|'''Function''' || [[transcriptional antiterminator|transcription antiterminators]] |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]''' |
Revision as of 19:48, 20 September 2009
Gene name | glcT |
Synonyms | ykwA |
Essential | no |
Product | transcriptional antiterminator of the ptsG-ptsH-ptsI operon |
Function | transcription antiterminators |
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
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: transcriptional antiterminator, RNA-binding protein, binds the ptsG RAT sequence
- Protein family: 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
- Structure:
- UniProt: O31691
- KEGG entry: [2]
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP109 (in frame deletion), 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
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, 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)
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)