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
Control of LicT activity
Structural analysis of LicT
LicT-RNA interaction
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)
Yinshan Yang, Nathalie Declerck, Xavier Manival, Stéphane Aymerich, Michel Kochoyan
Solution structure of the LicT-RNA antitermination complex: CAT clamping RAT.
EMBO J: 2002, 21(8);1987-97
[PubMed:11953318]
[WorldCat.org]
[DOI]
(P p)
N Declerck, F Vincent, F Hoh, S Aymerich, H van Tilbeurgh
RNA recognition by transcriptional antiterminators of the BglG/SacY family: functional and structural comparison of the CAT domain from SacY and LicT.
J Mol Biol: 1999, 294(2);389-402
[PubMed:10610766]
[WorldCat.org]
[DOI]
(P p)
S Aymerich, M Steinmetz
Specificity determinants and structural features in the RNA target of the bacterial antiterminator proteins of the BglG/SacY family.
Proc Natl Acad Sci U S A: 1992, 89(21);10410-4
[PubMed:1279678]
[WorldCat.org]
[DOI]
(P p)
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed