Difference between revisions of "AroA"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 20630 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 20630 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 13334 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 13334 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 9514 {{PubMed|21395229}}
 +
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 9162 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 13:32, 17 April 2014

  • Description: 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase / chorismate mutase-isozyme 3

Gene name aroA
Synonyms aroG
Essential no
Product 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase /

chorismate mutase-isozyme 3

Function biosynthesis of aromatic amino acids
Gene expression levels in SubtiExpress: aroA
Metabolic function and regulation of this protein in SubtiPathways:
aroA
MW, pI 39 kDa, 5.341
Gene length, protein length 1074 bp, 358 aa
Immediate neighbours ccpA, ytxJ
Sequences Protein DNA DNA_with_flanks
Genetic context
AroA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AroA expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU29750

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate (according to Swiss-Prot)
  • Protein family: class-I DAHP synthetase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
    • phosphorylation on Ser-2 PubMed
    • phosphorylation on Thr-4 PubMed
    • phosphorylated on Arg-45 and Arg-301 PubMed
    • Cys126 is S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species PubMed


  • Effectors of protein activity: subject to feedback inhibition PubMed

Database entries

  • Structure: 1VR6 (from Thermotoga maritima, 51% identity, 68% similarity)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • subject to feedback inhibition PubMed
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 20630 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 13334 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 9514 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 9162 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Bui Khanh Chi, Alexandra A Roberts, Tran Thi Thanh Huyen, Katrin Bäsell, Dörte Becher, Dirk Albrecht, Chris J Hamilton, Haike Antelmann
S-bacillithiolation protects conserved and essential proteins against hypochlorite stress in firmicutes bacteria.
Antioxid Redox Signal: 2013, 18(11);1273-95
[PubMed:22938038] [WorldCat.org] [DOI] (I p)

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

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)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [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)

Alia Lapidus, Nathalie Galleron, Alexei Sorokin, S Dusko Ehrlich
Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region.
Microbiology (Reading): 1997, 143 ( Pt 11);3431-3441
[PubMed:9387221] [WorldCat.org] [DOI] (P p)