UniProtKB - P0A6N4 (EFP_ECOLI)
Elongation factor P
efp
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 PublicationsCaution
: polypeptide chain elongation Pathwayi
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
- negative regulation of translational frameshifting Source: EcoCyc
- rescue of stalled ribosome Source: EcoCyc
- translational elongation Source: EcoCyc
Keywordsi
Molecular function | Elongation factor |
Biological process | Protein biosynthesis |
Enzyme and pathway databases
BioCyci | EcoCyc:EG12099-MONOMER |
UniPathwayi | UPA00345 |
Names & Taxonomyi
Protein namesi | Recommended name: Elongation factor PShort name: EF-P |
Gene namesi | Name:efp Ordered Locus Names:b4147, JW4107 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 31 | K → A: No lysylation. 1 Publication | 1 | |
Mutagenesisi | 33 | G → K: No lysylation. Loss of in vivo EF-P function for cell growth. 1 Publication | 1 | |
Mutagenesisi | 34 | K → A: No lysylation and loss of EF-P activity. No facilitation of translation of poly-Pro stretches. 3 Publications | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000094245 | 2 – 188 | Elongation factor PAdd BLAST | 187 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 34 | N6-(3,6-diaminohexanoyl)-5-hydroxylysine3 Publications | 1 |
Post-translational modificationi
Keywords - PTMi
HydroxylationProteomic databases
jPOSTi | P0A6N4 |
PaxDbi | P0A6N4 |
PRIDEi | P0A6N4 |
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 PublicationProtein-protein interaction databases
BioGRIDi | 4260776, 791 interactors |
DIPi | DIP-31834N |
IntActi | P0A6N4, 51 interactors |
STRINGi | 511145.b4147 |
Structurei
Secondary structure
3D structure databases
SMRi | P0A6N4 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0231, Bacteria |
HOGENOMi | CLU_074944_0_0_6 |
InParanoidi | P0A6N4 |
PhylomeDBi | P0A6N4 |
Family and domain databases
CDDi | cd04470, S1_EF-P_repeat_1, 1 hit cd05794, S1_EF-P_repeat_2, 1 hit |
Gene3Di | 2.30.30.30, 1 hit |
HAMAPi | MF_00141, EF_P, 1 hit |
InterProi | View protein in InterPro IPR015365, 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_sf |
PANTHERi | PTHR30053, PTHR30053, 1 hit |
Pfami | View protein in Pfam PF01132, EFP, 1 hit PF08207, EFP_N, 1 hit PF09285, Elong-fact-P_C, 1 hit |
PIRSFi | PIRSF005901, EF-P, 1 hit |
SMARTi | View protein in SMART SM01185, EFP, 1 hit SM00841, Elong-fact-P_C, 1 hit |
SUPFAMi | SSF50104, SSF50104, 1 hit SSF50249, SSF50249, 2 hits |
TIGRFAMsi | TIGR00038, efp, 1 hit |
PROSITEi | View protein in PROSITE PS01275, EFP, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Mass spectrometryi
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 |
PIRi | S34443 |
RefSeqi | NP_418571.1, NC_000913.3 WP_000257278.1, NZ_STEB01000014.1 |
Genome annotation databases
EnsemblBacteriai | AAC77107; AAC77107; b4147 BAE78149; BAE78149; BAE78149 |
GeneIDi | 67414765 948661 |
KEGGi | ecj:JW4107 eco:b4147 |
PATRICi | fig|1411691.4.peg.2553 |
Similar proteinsi
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 |
PIRi | S34443 |
RefSeqi | NP_418571.1, NC_000913.3 WP_000257278.1, NZ_STEB01000014.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3A5Z | X-ray | 2.50 | B/D/F/H | 1-188 | [»] | |
6ENJ | electron microscopy | 3.70 | w | 1-188 | [»] | |
6ENU | electron microscopy | 3.10 | w | 1-188 | [»] | |
SMRi | P0A6N4 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260776, 791 interactors |
DIPi | DIP-31834N |
IntActi | P0A6N4, 51 interactors |
STRINGi | 511145.b4147 |
Proteomic databases
jPOSTi | P0A6N4 |
PaxDbi | P0A6N4 |
PRIDEi | P0A6N4 |
Genome annotation databases
EnsemblBacteriai | AAC77107; AAC77107; b4147 BAE78149; BAE78149; BAE78149 |
GeneIDi | 67414765 948661 |
KEGGi | ecj:JW4107 eco:b4147 |
PATRICi | fig|1411691.4.peg.2553 |
Organism-specific databases
EchoBASEi | EB2023 |
Phylogenomic databases
eggNOGi | COG0231, Bacteria |
HOGENOMi | CLU_074944_0_0_6 |
InParanoidi | P0A6N4 |
PhylomeDBi | P0A6N4 |
Enzyme and pathway databases
UniPathwayi | UPA00345 |
BioCyci | EcoCyc:EG12099-MONOMER |
Miscellaneous databases
PROi | PR:P0A6N4 |
Family and domain databases
CDDi | cd04470, S1_EF-P_repeat_1, 1 hit cd05794, S1_EF-P_repeat_2, 1 hit |
Gene3Di | 2.30.30.30, 1 hit |
HAMAPi | MF_00141, EF_P, 1 hit |
InterProi | View protein in InterPro IPR015365, 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_sf |
PANTHERi | PTHR30053, PTHR30053, 1 hit |
Pfami | View protein in Pfam PF01132, EFP, 1 hit PF08207, EFP_N, 1 hit PF09285, Elong-fact-P_C, 1 hit |
PIRSFi | PIRSF005901, EF-P, 1 hit |
SMARTi | View protein in SMART SM01185, EFP, 1 hit SM00841, Elong-fact-P_C, 1 hit |
SUPFAMi | SSF50104, SSF50104, 1 hit SSF50249, SSF50249, 2 hits |
TIGRFAMsi | TIGR00038, efp, 1 hit |
PROSITEi | View protein in PROSITE PS01275, EFP, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | EFP_ECOLI | |
Accessioni | P0A6N4Primary (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: | February 23, 2022 | |
This is version 129 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families