Difference between revisions of "TsaB"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU05920&redirect=T BSU05920] | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU05920&redirect=T BSU05920] | ||
* '''Structure:''' | * '''Structure:''' |
Revision as of 13:05, 2 April 2014
- Description: required for threonyl carbamoyl adenosine (t6A) modification of tRNAs that pair with ANN codons in mRNA
Gene name | tsaB |
Synonyms | ydiC |
Essential | yes PubMed |
Product | tRNA modification enzyme |
Function | tRNA modification |
Gene expression levels in SubtiExpress: tsaB | |
Interactions involving this protein in SubtInteract: TsaB | |
MW, pI | 25 kDa, 5.762 |
Gene length, protein length | 687 bp, 229 aa |
Immediate neighbours | tsaE, ydiD |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU05920
Phenotypes of a mutant
essential PubMed
Database entries
- BsubCyc: BSU05920
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- BsubCyc: BSU05920
- Structure:
- UniProt: O05516
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Charles T Lauhon
Mechanism of N6-threonylcarbamoyladenonsine (t(6)A) biosynthesis: isolation and characterization of the intermediate threonylcarbamoyl-AMP.
Biochemistry: 2012, 51(44);8950-63
[PubMed:23072323]
[WorldCat.org]
[DOI]
(I p)
Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849]
[WorldCat.org]
[DOI]
(I p)
Basma El Yacoubi, Isabelle Hatin, Christopher Deutsch, Tamer Kahveci, Jean-Pierre Rousset, Dirk Iwata-Reuyl, Alexey G Murzin, Valérie de Crécy-Lagard
A role for the universal Kae1/Qri7/YgjD (COG0533) family in tRNA modification.
EMBO J: 2011, 30(5);882-93
[PubMed:21285948]
[WorldCat.org]
[DOI]
(I p)
Jennifer I Handford, Bérengère Ize, Grant Buchanan, Gareth P Butland, Jack Greenblatt, Andrew Emili, Tracy Palmer
Conserved network of proteins essential for bacterial viability.
J Bacteriol: 2009, 191(15);4732-49
[PubMed:19376873]
[WorldCat.org]
[DOI]
(I p)
Alison Hunt, Joy P Rawlins, Helena B Thomaides, Jeff Errington
Functional analysis of 11 putative essential genes in Bacillus subtilis.
Microbiology (Reading): 2006, 152(Pt 10);2895-2907
[PubMed:17005971]
[WorldCat.org]
[DOI]
(P p)