Efp

• Description: elongation factor P, important for the translation of proteins containing three or more consecutive proline residues
  
  

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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

translation, membrane proteins

The gene

Basic information

• Locus tag: BSU24450

Database entries

• BsubCyc: BSU24450

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions:

• Localization: cell membrane (according to Swiss-Prot), cell membrane (according to Swiss-Prot)

Database entries

• BsubCyc: BSU24450

• Structure: 1YBY (Efp from Clostridium thermocellum)

• UniProt: P49778

• KEGG entry: [2]

• E.C. number:

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

• Operon:

• Expression browser: efp PubMed

• Sigma factor:

• 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:

References

Agata L Starosta, Jürgen Lassak, Lauri Peil, Gemma C Atkinson, Christopher J Woolstenhulme, Kai Virumäe, Allen Buskirk, Tanel Tenson, Jaanus Remme, Kirsten Jung, Daniel N Wilson
A conserved proline triplet in Val-tRNA synthetase and the origin of elongation factor P.
Cell Rep: 2014, 9(2);476-83
[PubMed:25310979] [WorldCat.org] [DOI] (I p)

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)