Difference between revisions of "Efp"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 649 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 649 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 2275 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 2275 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 5117 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1779 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1876 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 14:05, 17 April 2014

Gene name efp
Synonyms yqhU, yqgF
Essential no
Product elongation factor P
Function translation
Gene expression levels in SubtiExpress: efp
MW, pI 20 kDa, 4.845
Gene length, protein length 555 bp, 185 aa
Immediate neighbours yqhV, papA
Sequences Protein DNA DNA_with_flanks
Genetic context
Efp context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Efp expression.png















Categories containing this gene/protein

translation, membrane proteins

This gene is a member of the following regulons

Efp-dependent proteins

The gene

Basic information

  • Locus tag: BSU24450

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: transpeptidase family (according to Swiss-Prot) elongation factor P family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cell membrane (according to Swiss-Prot), cell membrane (according to Swiss-Prot)

Database entries

  • Structure: 1YBY (Efp from Clostridium thermocellum)
  • KEGG entry: [2]
  • E.C. number:

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 649 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 2275 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 5117 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1779 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1876 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Lili K Doerfel, Ingo Wohlgemuth, Christina Kothe, Frank Peske, Henning Urlaub, Marina V Rodnina
EF-P is essential for rapid synthesis of proteins containing consecutive proline residues.
Science: 2013, 339(6115);85-8
[PubMed:23239624] [WorldCat.org] [DOI] (I p)

Susanne Ude, Jürgen Lassak, Agata L Starosta, Tobias Kraxenberger, Daniel N Wilson, Kirsten Jung
Translation elongation factor EF-P alleviates ribosome stalling at polyproline stretches.
Science: 2013, 339(6115);82-5
[PubMed:23239623] [WorldCat.org] [DOI] (I 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)

Daniel B Kearns, Frances Chu, Rivka Rudner, Richard Losick
Genes governing swarming in Bacillus subtilis and evidence for a phase variation mechanism controlling surface motility.
Mol Microbiol: 2004, 52(2);357-69
[PubMed:15066026] [WorldCat.org] [DOI] (P p)