TsaC
- Description: L-threonylcarbamoyl-AMP synthase, biosynthesis of the hypermodified base threonylcarbamoyladenosine (t(6)A) (together with TsaB-TsaD-TsaE)
| Gene name | tsaC |
| Synonyms | ipc-29d, ywlC |
| Essential | no |
| Product | L-threonylcarbamoyl-AMP synthase |
| Function | tRNA modification |
| Gene expression levels in SubtiExpress: tsaC | |
| MW, pI | 36 kDa, 5.82 |
| Gene length, protein length | 1038 bp, 346 aa |
| Immediate neighbours | ywlD, ywlB |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
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Expression at a glance PubMed
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Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU36950
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- conversion of L-threonine, bicarbonate/CO2 and ATP to give the intermediate L-threonylcarbamoyl-AMP (TC-AMP) and pyrophosphate as products PubMed
- biosynthesis of the hypermodified base threonylcarbamoyladenosine (t(6)A), a universal modification found at position 37 of ANN decoding tRNAs, which imparts a unique structure to the anticodon loop enhancing its binding to ribosomes in vitro (shown for the corresponding E. coli protein YrdC) PubMed
- Protein family: SUA5 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- UniProt: P39153
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- Regulation:
- 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, Benjamin Lyons, Yulien Cruz, Robert Reddy, Brian Nordin, Fabio Agnelli, James R Williamson, Paul Schimmel, Manal A Swairjo, Valérie de Crécy-Lagard
The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA.
Nucleic Acids Res: 2009, 37(9);2894-909
[PubMed:19287007]
[WorldCat.org]
[DOI]
(I p)
Shu Ishikawa, Yoshitoshi Ogura, Mika Yoshimura, Hajime Okumura, Eunha Cho, Yoshikazu Kawai, Ken Kurokawa, Taku Oshima, Naotake Ogasawara
Distribution of stable DnaA-binding sites on the Bacillus subtilis genome detected using a modified ChIP-chip method.
DNA Res: 2007, 14(4);155-68
[PubMed:17932079]
[WorldCat.org]
[DOI]
(P 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)
