Difference between revisions of "TsaE"
| Line 15: | Line 15: | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU05910 ydiB] | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU05910 ydiB] | ||
|- | |- | ||
| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/ | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/TsaE TsaE] |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 17 kDa, 4.597 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 17 kDa, 4.597 | ||
| Line 21: | Line 21: | ||
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 474 bp, 158 aa | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 474 bp, 158 aa | ||
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[thiL]]'', ''[[ | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[thiL]]'', ''[[tsaB]]'' |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB12410]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' | |colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB12410]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' | ||
| Line 94: | Line 94: | ||
* '''[[Localization]]:''' | * '''[[Localization]]:''' | ||
| − | ** cytoplasm with the | + | ** cytoplasm with the exception of the nucleoid region [http://www.ncbi.nlm.nih.gov/sites/entrez/19246765 PubMed] |
=== Database entries === | === Database entries === | ||
| Line 112: | Line 112: | ||
=Expression and regulation= | =Expression and regulation= | ||
| − | * '''Operon:''' | + | * '''Operon:''' ''[[thiL]]-[[tsaE]]-[[tsaB]]-[[ydiD]]-[[tsaD]]'' {{PubMed|22383849}} |
| − | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ydiB_641654_642130_1 | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ydiB_641654_642130_1 tsaE] {{PubMed|22383849}} |
* '''Sigma factor:''' | * '''Sigma factor:''' | ||
| Line 146: | Line 146: | ||
=References= | =References= | ||
| − | <pubmed> 17005971, 19246765 23072323</pubmed> | + | <pubmed> 17005971, 19246765 23072323 22383849</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 11:24, 18 October 2012
- Description: P-loop ATPase, required for threonyl carbamoyl adenosine (t6A) modification of tRNAs that pair with ANN codons in mRNA
| Gene name | ydiB |
| Synonyms | |
| Essential | no |
| Product | tRNA modification enzyme |
| Function | tRNA modification |
| Gene expression levels in SubtiExpress: ydiB | |
| 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
| |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU05910
Phenotypes of a mutant
reduced growth rate PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- 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:
- 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
- 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)
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)
