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Protein

Elongation factor P

Gene

efp

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: -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. Modification of Lys-34 is required for alleviation.UniRule annotation

Pathwayi: polypeptide chain elongation

This protein is involved in the pathway polypeptide chain elongation, which is part of Protein biosynthesis.UniRule annotation
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

Keywordsi

Molecular functionElongation factor
Biological processProtein biosynthesis

Enzyme and pathway databases

BioCyciSENT99287:G1FZD-4378-MONOMER
UniPathwayiUPA00345

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor PUniRule annotation
Short name:
EF-PUniRule annotation
Gene namesi
Name:efpUniRule annotation
Ordered Locus Names:STM4334
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells lacking EF-P display highly pleiotropic phenotypes similar to those lacking EmpA or EmpB. They exhibit reduced growth rates, and they display increased susceptibility to hypoosmotic conditions, antibiotics, and detergents and enhanced resistance to the compound S-nitrosoglutathione. The susceptibility phenotypes are largely explained by the enhanced membrane permeability of the efp mutant. Analysis of the membrane proteomes of wild-type and efp mutant strains reveals few changes, including the prominent overexpression of a single porin, KdgM (STM1131), in the efp mutant outer membrane.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000943232 – 188Elongation factor PAdd BLAST187

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei34N6-(3,6-diaminohexanoyl)-5-hydroxylysineUniRule annotation1 Publication1

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 (Probable) (PubMed:20670890).1 Publication

Keywords - PTMi

Hydroxylation

Proteomic databases

PaxDbiP64036
PRIDEiP64036

Interactioni

Protein-protein interaction databases

STRINGi99287.STM4334

Structurei

3D structure databases

ProteinModelPortaliP64036
SMRiP64036
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the elongation factor P family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DRH Bacteria
COG0231 LUCA
HOGENOMiHOG000010047
KOiK02356
OMAiNTFSAGH
PhylomeDBiP64036

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
InterProiView 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
PANTHERiPTHR30053 PTHR30053, 1 hit
PfamiView protein in Pfam
PF01132 EFP, 1 hit
PF08207 EFP_N, 1 hit
PF09285 Elong-fact-P_C, 1 hit
PIRSFiPIRSF005901 EF-P, 1 hit
SMARTiView protein in SMART
SM01185 EFP, 1 hit
SM00841 Elong-fact-P_C, 1 hit
SUPFAMiSSF50104 SSF50104, 1 hit
SSF50249 SSF50249, 2 hits
TIGRFAMsiTIGR00038 efp, 1 hit
PROSITEiView protein in PROSITE
PS01275 EFP, 1 hit

Sequencei

Sequence statusi: Complete.

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

P64036-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATYYSNDFR SGLKIMLDGE PYAVESSEFV 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):20,623
Last modified:January 23, 2007 - v2
Checksum:i76D5264BF296C790
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA Translation: AAL23157.1
RefSeqiNP_463198.1, NC_003197.2
WP_000257282.1, NC_003197.2

Genome annotation databases

EnsemblBacteriaiAAL23157; AAL23157; STM4334
GeneIDi1255860
KEGGistm:STM4334
PATRICifig|99287.12.peg.4560

Similar proteinsi

Entry informationi

Entry nameiEFP_SALTY
AccessioniPrimary (citable) accession number: P64036
Secondary accession number(s): Q8XFX2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 86 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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