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Protein

Elongation factor P

Gene

efp

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Pathwayi: polypeptide chain elongation

This protein is involved in the pathway polypeptide chain elongation, which is part of Protein biosynthesis.
View all proteins of this organism that are known to be involved in the pathway polypeptide chain elongation and in Protein biosynthesis.

GO - Molecular functioni

  • ribosome binding Source: EcoCyc
  • translation elongation factor activity Source: EcoCyc

GO - Biological processi

  • translational elongation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG12099-MONOMER.
ECOL316407:JW4107-MONOMER.
MetaCyc:EG12099-MONOMER.
UniPathwayiUPA00345.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor P
Short name:
EF-P
Gene namesi
Name:efp
Ordered Locus Names:b4147, JW4107
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12099. efp.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoCyc
  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

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.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi31K → A: No lysylation. 1 Publication1
Mutagenesisi33G → K: No lysylation. Loss of in vivo EF-P function for cell growth. 1 Publication1
Mutagenesisi34K → A: No lysylation and loss of EF-P activity. No facilitation of translation of poly-Pro stretches. 3 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000942452 – 188Elongation factor PAdd BLAST187

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei34N6-(3,6-diaminohexanoyl)-5-hydroxylysine3 Publications1

Post-translational modificationi

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:21841797 PubMed:22128152 PubMed:22706199 and PubMed:20729861).3 Publications

Keywords - PTMi

Hydroxylation

Proteomic databases

EPDiP0A6N4.
PaxDbiP0A6N4.
PRIDEiP0A6N4.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi4260776. 698 interactors.
DIPiDIP-31834N.
IntActiP0A6N4. 1 interactor.
STRINGi511145.b4147.

Structurei

Secondary structure

1188
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Beta strandi14 – 17Combined sources4
Beta strandi20 – 30Combined sources11
Beta strandi38 – 45Combined sources8
Helixi46 – 48Combined sources3
Beta strandi51 – 57Combined sources7
Beta strandi61 – 64Combined sources4
Beta strandi67 – 70Combined sources4
Beta strandi73 – 77Combined sources5
Beta strandi82 – 85Combined sources4
Turni87 – 89Combined sources3
Beta strandi92 – 95Combined sources4
Helixi97 – 100Combined sources4
Turni102 – 106Combined sources5
Beta strandi109 – 112Combined sources4
Beta strandi114 – 118Combined sources5
Beta strandi121 – 126Combined sources6
Beta strandi152 – 156Combined sources5
Beta strandi161 – 164Combined sources4
Beta strandi173 – 177Combined sources5
Turni178 – 181Combined sources4
Beta strandi182 – 186Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3A5ZX-ray2.50B/D/F/H1-188[»]
ProteinModelPortaliP0A6N4.
SMRiP0A6N4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the elongation factor P family.Curated

Phylogenomic databases

eggNOGiENOG4105DRH. Bacteria.
COG0231. LUCA.
HOGENOMiHOG000010047.
InParanoidiP0A6N4.
KOiK02356.
OMAiDYVFMDM.
PhylomeDBiP0A6N4.

Family and domain databases

CDDicd04470. S1_EF-P_repeat_1. 1 hit.
cd05794. S1_EF-P_repeat_2. 1 hit.
Gene3Di2.30.30.30. 1 hit.
HAMAPiMF_00141. EF_P. 1 hit.
InterProiIPR015365. Elong-fact-P_C.
IPR012340. NA-bd_OB-fold.
IPR014722. Rib_L2_dom2.
IPR020599. Transl_elong_fac_P/YeiP.
IPR013185. Transl_elong_KOW-like.
IPR001059. Transl_elong_P/YeiP_cen.
IPR013852. Transl_elong_P/YeiP_CS.
IPR011768. Transl_elongation_fac_P.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamiPF01132. EFP. 1 hit.
PF08207. EFP_N. 1 hit.
PF09285. Elong-fact-P_C. 1 hit.
[Graphical view]
PIRSFiPIRSF005901. EF-P. 1 hit.
SMARTiSM01185. EFP. 1 hit.
SM00841. Elong-fact-P_C. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 2 hits.
TIGRFAMsiTIGR00038. efp. 1 hit.
PROSITEiPS01275. EFP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6N4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATYYSNDFR AGLKIMLDGE PYAVEASEFV KPGKGQAFAR VKLRRLLTGT
60 70 80 90 100
RVEKTFKSTD SAEGADVVDM NLTYLYNDGE FWHFMNNETF EQLSADAKAI
110 120 130 140 150
GDNAKWLLDQ AECIVTLWNG QPISVTPPNF VELEIVDTDP GLKGDTAGTG
160 170 180
GKPATLSTGA VVKVPLFVQI GEVIKVDTRS GEYVSRVK
Length:188
Mass (Da):20,591
Last modified:January 23, 2007 - v2
Checksum:iE36E136D4399460F
GO

Mass spectrometryi

Molecular mass is 20591.6 Da from positions 2 - 188. Determined by ESI. With N6-(3,6-diaminohexanoyl)-5-hydroxy-Lys-34.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61676 Genomic DNA. Translation: CAA43851.1.
U14003 Genomic DNA. Translation: AAA97046.1.
U00096 Genomic DNA. Translation: AAC77107.1.
AP009048 Genomic DNA. Translation: BAE78149.1.
PIRiS34443.
RefSeqiNP_418571.1. NC_000913.3.
WP_000257278.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77107; AAC77107; b4147.
BAE78149; BAE78149; BAE78149.
GeneIDi948661.
KEGGiecj:JW4107.
eco:b4147.
PATRICi32123863. VBIEscCol129921_4279.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61676 Genomic DNA. Translation: CAA43851.1.
U14003 Genomic DNA. Translation: AAA97046.1.
U00096 Genomic DNA. Translation: AAC77107.1.
AP009048 Genomic DNA. Translation: BAE78149.1.
PIRiS34443.
RefSeqiNP_418571.1. NC_000913.3.
WP_000257278.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3A5ZX-ray2.50B/D/F/H1-188[»]
ProteinModelPortaliP0A6N4.
SMRiP0A6N4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260776. 698 interactors.
DIPiDIP-31834N.
IntActiP0A6N4. 1 interactor.
STRINGi511145.b4147.

Proteomic databases

EPDiP0A6N4.
PaxDbiP0A6N4.
PRIDEiP0A6N4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77107; AAC77107; b4147.
BAE78149; BAE78149; BAE78149.
GeneIDi948661.
KEGGiecj:JW4107.
eco:b4147.
PATRICi32123863. VBIEscCol129921_4279.

Organism-specific databases

EchoBASEiEB2023.
EcoGeneiEG12099. efp.

Phylogenomic databases

eggNOGiENOG4105DRH. Bacteria.
COG0231. LUCA.
HOGENOMiHOG000010047.
InParanoidiP0A6N4.
KOiK02356.
OMAiDYVFMDM.
PhylomeDBiP0A6N4.

Enzyme and pathway databases

UniPathwayiUPA00345.
BioCyciEcoCyc:EG12099-MONOMER.
ECOL316407:JW4107-MONOMER.
MetaCyc:EG12099-MONOMER.

Miscellaneous databases

PROiP0A6N4.

Family and domain databases

CDDicd04470. S1_EF-P_repeat_1. 1 hit.
cd05794. S1_EF-P_repeat_2. 1 hit.
Gene3Di2.30.30.30. 1 hit.
HAMAPiMF_00141. EF_P. 1 hit.
InterProiIPR015365. Elong-fact-P_C.
IPR012340. NA-bd_OB-fold.
IPR014722. Rib_L2_dom2.
IPR020599. Transl_elong_fac_P/YeiP.
IPR013185. Transl_elong_KOW-like.
IPR001059. Transl_elong_P/YeiP_cen.
IPR013852. Transl_elong_P/YeiP_CS.
IPR011768. Transl_elongation_fac_P.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamiPF01132. EFP. 1 hit.
PF08207. EFP_N. 1 hit.
PF09285. Elong-fact-P_C. 1 hit.
[Graphical view]
PIRSFiPIRSF005901. EF-P. 1 hit.
SMARTiSM01185. EFP. 1 hit.
SM00841. Elong-fact-P_C. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 2 hits.
TIGRFAMsiTIGR00038. efp. 1 hit.
PROSITEiPS01275. EFP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEFP_ECOLI
AccessioniPrimary (citable) accession number: P0A6N4
Secondary accession number(s): P33398, Q2M6F7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The modification on Lys-34 was initially thought to be a spermidine residue.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.