P0A6N4 · EFP_ECOLI

Function

function

Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Beta-lysylation at Lys-34 is required for alleviation. The Pro codons and their context do not affect activity; only consecutive Pro residues (not another amino acid) are affected by EF-P. Has stimulatory effects on peptide bond formation between ribosome-bound initiator tRNA(fMet) and puromycin, and N-acetyl-Phe tRNA(Phe)-primed poly(U)-directed poly(Phe) synthesis.

Caution

The modification on Lys-34 was initially thought to be a spermidine residue.

Pathway

Protein biosynthesis; polypeptide chain elongation.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Molecular Functionribosome binding
Molecular Functiontranslation elongation factor activity
Biological Processnegative regulation of translational frameshifting
Biological Processpeptide biosynthetic process
Biological Processrescue of stalled ribosome
Biological Processtranslational elongation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Elongation factor P
  • Short names
    EF-P

Gene names

    • Name
      efp
    • Ordered locus names
      b4147, JW4107

Organism names

  • Taxonomic identifier
  • Strains
    • K12 / MG1655 / ATCC 47076
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / EMG2
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P0A6N4
  • Secondary accessions
    • P33398
    • Q2M6F7

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Disruption of this gene leads to lethality (PubMed:9405429) or to a very slow growth phenotype (PubMed:20729861).
Required for the expression of poly-Pro-containing proteins

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis31No lysylation.
Mutagenesis33No lysylation. Loss of in vivo EF-P function for cell growth.
Mutagenesis34No lysylation and loss of EF-P activity. No facilitation of translation of poly-Pro stretches.

PTM/Processing

Features

Showing features for initiator methionine, chain, modified residue.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00000942452-188Elongation factor P
Modified residue34N6-(3,6-diaminohexanoyl)-5-hydroxylysine

Post-translational modification

Is beta-lysylated on the epsilon-amino group of Lys-34 by the combined action of EpmA and EpmB, and then hydroxylated on the C5 position of the same residue by EpmC. Lysylation is critical for the stimulatory effect of EF-P on peptide-bond formation. The lysylation moiety would extend toward the peptidyltransferase center and stabilize the terminal 3-CCA end of the tRNA. The hydroxylation of the C5 position on Lys-34 would allow additional potential stabilizing hydrogen-bond interactions with the P-tRNA (PubMed:20729861, PubMed:21841797, PubMed:22128152, PubMed:22706199).

Keywords

Proteomic databases

Interaction

Subunit

Binds 30S, 50S and 70S ribosomes, possibly near the A site, note that T.thermophilus structures show binding between the P and E sites (PDB 3HUW and 3HUY). Proportionally less EF-P binds to larger polysomes, suggesting it has a role early in translation. It is present in 1 copy per 10 ribosomes.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the elongation factor P family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    188
  • Mass (Da)
    20,591
  • Last updated
    2007-01-23 v2
  • Checksum
    E36E136D4399460F
MATYYSNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVVDMNLTYLYNDGEFWHFMNNETFEQLSADAKAIGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEIVDTDPGLKGDTAGTGGKPATLSTGAVVKVPLFVQIGEVIKVDTRSGEYVSRVK

Mass Spectrometry

Molecular mass is 20,591.6 Da. Determined by Electrospray. With N6-(3,6-diaminohexanoyl)-5-hydroxy-Lys-34.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X61676
EMBL· GenBank· DDBJ
CAA43851.1
EMBL· GenBank· DDBJ
Genomic DNA
U14003
EMBL· GenBank· DDBJ
AAA97046.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC77107.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE78149.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp