Difference between revisions of "AspS"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 1584 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 1584 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 6801 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 6801 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1217 {{PubMed|21395229}}
 +
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 941 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 13:32, 17 April 2014

  • Description: aspartyl-tRNA synthetase

Gene name aspS
Synonyms
Essential yes PubMed
Product aspartyl-tRNA synthetase
Function translation
Gene expression levels in SubtiExpress: aspS
Metabolic function and regulation of this protein in SubtiPathways:
aspS
MW, pI 65 kDa, 4.654
Gene length, protein length 1776 bp, 592 aa
Immediate neighbours bsrA, hisS
Sequences Protein DNA DNA_with_flanks
Genetic context
AspS context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AspS expression.png















Categories containing this gene/protein

translation, essential genes, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

T-box

The gene

Basic information

  • Locus tag: BSU27550

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-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp) (according to Swiss-Prot)
  • Protein family: class-II aminoacyl-tRNA synthetase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification: phosphorylated on ser/ thr/ tyr PubMed
  • Effectors of protein activity:

Database entries

  • Structure: 1EQR (from Escherichia coli, 52% identity, 68% similarity) PubMed
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Regulation:
    • induced by histidine or aspartate limitation (T-box) PubMed
  • Additional information:
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 1584 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 6801 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1217 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 941 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)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P p)