TsaE

• Description: P-loop ATPase, required for threonyl carbamoyl adenosine (t6A) modification of tRNAs that pair with ANN codons in mRNA
  
  

Gene name	tsaE
Synonyms	ydiB
Essential	no
Product	tRNA modification enzyme
Function	tRNA modification
Gene expression levels in SubtiExpress: tsaE
Interactions involving this protein in SubtInteract: TsaE
MW, pI	17 kDa, 4.597
Gene length, protein length	474 bp, 158 aa
Immediate neighbours	thiL, tsaB
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

translation

The gene

Basic information

• Locus tag: BSU05910

Phenotypes of a mutant

reduced growth rate PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • biosynthesis of the threonylcarbamoyladenosine (t6A) residue at position 37 of ANN-decoding tRNAs using L-threonylcarbamoyl-AMP (TsaB-TsaD-TsaE) PubMed

• Protein family: UPF0079 family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information: K(M) for ATP: 60 myM, V(max) 10 nmol/min PubMed

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • dimerizes and oligomerizes PubMed
  • TsaB-TsaE PubMed
  • TsaD-TsaE PubMed

• Localization:
  • cytoplasm with the exception of the nucleoid region PubMed

Database entries

• Structure:

• UniProt: O05515

• KEGG entry: [2]

• E.C. number:

Additional information

ATPase activity is required for in vivo function of the protein PubMed

Expression and regulation

• Operon: thiL-tsaE-tsaB-ydiD-tsaD PubMed

• Expression browser: tsaE PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:
  • for expression/ purification from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP833, available in Stülke lab
  • for expression/ purification from E. coli with N-terminal His-tag, in pWH844: pGP841, available in Stülke lab

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)

Johanna C Karst, Anne-Emmanuelle Foucher, Tracey L Campbell, Anne-Marie Di Guilmi, David Stroebel, Chand S Mangat, Eric D Brown, Jean-Michel Jault
The ATPase activity of an 'essential' Bacillus subtilis enzyme, YdiB, is required for its cellular function and is modulated by oligomerization.
Microbiology (Reading): 2009, 155(Pt 3);944-956
[PubMed:19246765] [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)