Difference between revisions of "Eno"

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* '''Additional information:'''
 
* '''Additional information:'''
 
** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
 
** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium): 10563 {{PubMed|24696501}}
 +
** number of protein molecules per cell (complex medium with amino acids, without glucose): 9957 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =

Revision as of 09:26, 17 April 2014

Gene name eno
Synonyms
Essential Yes (PubMed)
Product enolase
Function enzyme in glycolysis/ gluconeogenesis
Gene expression levels in SubtiExpress: eno
Interactions involving this protein in SubtInteract: Eno
Metabolic function and regulation of this protein in SubtiPathways:
Eno
MW, pI 46,4 kDa, 4.49
Gene length, protein length 1290 bp, 430 amino acids
Immediate neighbours yvbK, pgm
Sequences Protein DNA DNA_with_flanks
Genetic context
Eno context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Eno expression.png
















Categories containing this gene/protein

carbon core metabolism, essential genes, membrane proteins, phosphoproteins, universally conserved proteins, most abundant proteins

This gene is a member of the following regulons

CggR regulon

The gene

Basic information

  • Locus tag: BSU33900

Phenotypes of a mutant

  • no growth on LB, requires glucose and malate
  • essential according to Kobayashi et al. on LB PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O (according to Swiss-Prot) 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O
  • Protein family: enolase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: reversible Michaelis-Menten PubMed
  • Domains:
    • substrate binding domain (366–369)
  • Modification: phosphorylation on Thr-141 AND Ser-259 AND Tyr-281 AND Ser-325 PubMed, PubMed, PubMed
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulatory mechanism: transcription repression by CggR PubMed
  • Additional information:
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 10563 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 9957 PubMed

Biological materials

  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References

Reviews

Subcellular localization of enolase

Chun-Kai Yang, Xiao-Zhou Zhang, Chung-Dar Lu, Phang C Tai
An internal hydrophobic helical domain of Bacillus subtilis enolase is essential but not sufficient as a non-cleavable signal for its secretion.
Biochem Biophys Res Commun: 2014, 446(4);901-5
[PubMed:24642254] [WorldCat.org] [DOI] (I p)

Chun-Kai Yang, Hosam E Ewis, XiaoZhou Zhang, Chung-Dar Lu, Hae-Jin Hu, Yi Pan, Ahmed T Abdelal, Phang C Tai
Nonclassical protein secretion by Bacillus subtilis in the stationary phase is not due to cell lysis.
J Bacteriol: 2011, 193(20);5607-15
[PubMed:21856851] [WorldCat.org] [DOI] (I p)

Carsten Jers, Malene Mejer Pedersen, Dafni Katerina Paspaliari, Wolfgang Schütz, Christina Johnsson, Boumediene Soufi, Boris Macek, Peter Ruhdal Jensen, Ivan Mijakovic
Bacillus subtilis BY-kinase PtkA controls enzyme activity and localization of its protein substrates.
Mol Microbiol: 2010, 77(2);287-99
[PubMed:20497499] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Grégory Boël, Vianney Pichereau, Ivan Mijakovic, Alain Mazé, Sandrine Poncet, Sylvie Gillet, Jean-Christophe Giard, Axel Hartke, Yanick Auffray, Josef Deutscher
Is 2-phosphoglycerate-dependent automodification of bacterial enolases implicated in their export?
J Mol Biol: 2004, 337(2);485-96
[PubMed:15003462] [WorldCat.org] [DOI] (P p)


Other original publications