LicT
- Description: transcriptional antiterminator of the bglP-bglH-yxiE operon and the bglS gene
| Gene name | licT |
| Synonyms | |
| Essential | no |
| Product | transcriptional antiterminator (BglG family) |
| Function | control of beta-glucan and beta-glucoside utilization |
| Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism | |
| 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
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Contents
Categories containing this gene/protein
utilization of specific carbon sources, transcription factors and their control, RNA binding regulators, phosphoproteins
This gene is a member of the following regulons
The LicT regulon: bglP-bglH-yxiE, bglS
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 of antiterminators (according to Swiss-Prot)
Extended information on the protein
- Kinetic information:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- UniProt: P39805
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP427 (licTS, erm), available in the Stülke lab
- Expression vector:
- for expression, purification of both PRDs in E. coli with N-terminal His-tag, in pWH844: pGP165, available in Stülke lab
- for expression, purification of the RNA-binding domain in E. coli with N-terminal His-tag, in pWH844: pGP315, available in Stülke lab
- for expression, purification of the RNA-binding domain in E. coli with N-terminal His-tag and thrombin cleavage site, in pGP570: pGP572, available in Stülke lab
- 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
Control of LicT activity
Thomas Bahr, Denise Lüttmann, Walter März, Bodo Rak, Boris Görke
Insight into bacterial phosphotransferase system-mediated signaling by interspecies transplantation of a transcriptional regulator.
J Bacteriol: 2011, 193(8);2013-26
[PubMed:21335451]
[WorldCat.org]
[DOI]
(I p)
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
LicT-RNA interaction
