Difference between revisions of "LicT"
(→Extended information on the protein: Added the domains and the phosphorylation sites) |
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* '''Domains:''' | * '''Domains:''' | ||
+ | ** N-terminal RNA binding domain [http://www.ncbi.nlm.nih.gov/pubmed/10610766?dopt=Abstract Pubmed] | ||
+ | ** 2xPRD (PTS regulation domains) [http://www.ncbi.nlm.nih.gov/pubmed/11447120?dopt=Abstract PubMed] | ||
− | * '''Modification:''' | + | * '''Modification:''' |
+ | ** phosphorylation at His-100 in PRD-1 by phosphorylated [[BglP]], inhibits LicT antitermination activity | ||
+ | ** phosphorylation at His-207 and/or His-269 in PRD-2 by His-P-[[ptsH|HPr]] | ||
* '''Cofactor(s):''' | * '''Cofactor(s):''' |
Revision as of 13:07, 3 June 2009
- Description: transcriptional antiterminator of the bglPH operon
Gene name | licT |
Synonyms | |
Essential | no |
Product | transcriptional antiterminator (BglG family) |
Function | required for substrate-dependent induction of bglPH |
MW, pI | 32 kDa, 5.944 |
Gene length, protein length | 831 bp, 277 aa |
Immediate neighbours | bglS, yxiP |
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: BSU39080
Phenotypes of a mutant
no expression of the bglP-bglH operon
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: binding to the mRNAs of bglS and the bglP-bglH operon, causes transcription antitermination (in presence of salicin and absence of glucose)
- Protein family: transcriptional antiterminator bglG family (according to Swiss-Prot) BglG family of antiterminators
Extended information on the protein
- Kinetic information:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- Swiss prot entry: P39805
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Stephane Aymerich, Microbiology and Molecular Genetics, INRA Paris-Grignon, France
Josef Deutscher, Microbiology and Molecular Genetics, INRA Paris-Grignon, France
Michael Hecker, Greifswald, Germany Homepage
Your additional remarks
References
Original description
K Schnetz, J Stülke, S Gertz, S Krüger, M Krieg, M Hecker, B Rak
LicT, a Bacillus subtilis transcriptional antiterminator protein of the BglG family.
J Bacteriol: 1996, 178(7);1971-9
[PubMed:8606172]
[WorldCat.org]
[DOI]
(P p)
Control of LicT activity
Cordula Lindner, Michael Hecker, Dominique Le Coq, Josef Deutscher
Bacillus subtilis mutant LicT antiterminators exhibiting enzyme I- and HPr-independent antitermination affect catabolite repression of the bglPH operon.
J Bacteriol: 2002, 184(17);4819-28
[PubMed:12169607]
[WorldCat.org]
[DOI]
(P p)
P Tortosa, N Declerck, H Dutartre, C Lindner, J Deutscher, D Le Coq
Sites of positive and negative regulation in the Bacillus subtilis antiterminators LicT and SacY.
Mol Microbiol: 2001, 41(6);1381-93
[PubMed:11580842]
[WorldCat.org]
[DOI]
(P p)
C Lindner, A Galinier, M Hecker, J Deutscher
Regulation of the activity of the Bacillus subtilis antiterminator LicT by multiple PEP-dependent, enzyme I- and HPr-catalysed phosphorylation.
Mol Microbiol: 1999, 31(3);995-1006
[PubMed:10048041]
[WorldCat.org]
[DOI]
(P p)
S Krüger, S Gertz, M Hecker
Transcriptional analysis of bglPH expression in Bacillus subtilis: evidence for two distinct pathways mediating carbon catabolite repression.
J Bacteriol: 1996, 178(9);2637-44
[PubMed:8626332]
[WorldCat.org]
[DOI]
(P p)
Structural analysis of LicT
Hélène Déméné, Thierry Ducat, Karine De Guillen, Catherine Birck, Stéphane Aymerich, Michel Kochoyan, Nathalie Declerck
Structural mechanism of signal transduction between the RNA-binding domain and the phosphotransferase system regulation domain of the LicT antiterminator.
J Biol Chem: 2008, 283(45);30838-49
[PubMed:18682383]
[WorldCat.org]
[DOI]
(P p)
Marc Graille, Cong-Zhao Zhou, Véronique Receveur-Bréchot, Bruno Collinet, Nathalie Declerck, Herman van Tilbeurgh
Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes.
J Biol Chem: 2005, 280(15);14780-9
[PubMed:15699035]
[WorldCat.org]
[DOI]
(P p)
N Declerck, H Dutartre, V Receveur, V Dubois, C Royer, S Aymerich, H van Tilbeurgh
Dimer stabilization upon activation of the transcriptional antiterminator LicT.
J Mol Biol: 2001, 314(4);671-81
[PubMed:11733988]
[WorldCat.org]
[DOI]
(P p)
H van Tilbeurgh, D Le Coq, N Declerck
Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator.
EMBO J: 2001, 20(14);3789-99
[PubMed:11447120]
[WorldCat.org]
[DOI]
(P p)
LicT-RNA interaction
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed