Difference between revisions of "IleS"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU15430&redirect=T BSU15430]
  
 
* '''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=BSU15430&redirect=T BSU15430]
  
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=1qu2 1QU2] (from ''Staphylococcus aureus'', 61% identity) {{PubMed|10446055}}
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=1qu2 1QU2] (from ''Staphylococcus aureus'', 61% identity) {{PubMed|10446055}}

Revision as of 13:40, 2 April 2014

  • Description: isoleucyl-tRNA synthetase

Gene name ileS
Synonyms
Essential yes PubMed
Product isoleucyl-tRNA synthetase
Function translation
Gene expression levels in SubtiExpress: ileS
Metabolic function and regulation of this protein in SubtiPathways:
ileS
MW, pI 104 kDa, 5.191
Gene length, protein length 2763 bp, 921 aa
Immediate neighbours divIVA, ylyA
Sequences Protein DNA DNA_with_flanks
Genetic context
IleS context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
IleS expression.png















Categories containing this gene/protein

translation, essential genes

This gene is a member of the following regulons

T-box

The gene

Basic information

  • Locus tag: BSU15430

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile) (according to Swiss-Prot)
  • Protein family: IleS type 1 subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1QU2 (from Staphylococcus aureus, 61% identity) PubMed
  • KEGG entry: [2]

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Operon:
  • Regulation:
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Ana Gutiérrez-Preciado, Tina M Henkin, Frank J Grundy, Charles Yanofsky, Enrique Merino
Biochemical features and functional implications of the RNA-based T-box regulatory mechanism.
Microbiol Mol Biol Rev: 2009, 73(1);36-61
[PubMed:19258532] [WorldCat.org] [DOI] (I p)

Scott P Salowe, Judyann Wiltsie, Julio C Hawkins, Lisa M Sonatore
The catalytic flexibility of tRNAIle-lysidine synthetase can generate alternative tRNA substrates for isoleucyl-tRNA synthetase.
J Biol Chem: 2009, 284(15);9656-62
[PubMed:19233850] [WorldCat.org] [DOI] (P p)

Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik, Robert L Switzer, Michael Hecker
Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.
J Bacteriol: 2008, 190(1);321-31
[PubMed:17981983] [WorldCat.org] [DOI] (I p)

L F Silvian, J Wang, T A Steitz
Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin.
Science: 1999, 285(5430);1074-7
[PubMed:10446055] [WorldCat.org] (P p)