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P0A6N4 (EFP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation factor P

Short name=EF-P
Gene names
Name:efp
Ordered Locus Names:b4147, JW4107
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in peptide bond synthesis, probably at an early stage of protein synthesis. 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. HAMAP MF_00141

Pathway

Protein biosynthesis; polypeptide chain elongation. HAMAP MF_00141

Subunit structure

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.

Subcellular location

Cytoplasm HAMAP MF_00141.

Post-translational modification

Has been seen to be partially modified on residues 32-34 by an unidentified entity with a mass difference of 143.77 Da. HAMAP MF_00141

Disruption phenotype

Lethality. Ref.7

Sequence similarities

Belongs to the elongation factor P family.

Caution

The ptm may be an artifact.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   Molecular functionElongation factor
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processpeptide biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from direct assay. Source: EcoCyc

   Molecular functionribosome binding

Inferred from direct assay Ref.9. Source: EcoCyc

translation elongation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.5
Chain2 – 188187Elongation factor P HAMAP MF_00141
PRO_0000094245

Sequences

Sequence LengthMass (Da)Tools
P0A6N4 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E36E136D4399460F

FASTA18820,591
        10         20         30         40         50         60 
MATYYSNDFR AGLKIMLDGE PYAVEASEFV KPGKGQAFAR VKLRRLLTGT RVEKTFKSTD 

        70         80         90        100        110        120 
SAEGADVVDM NLTYLYNDGE FWHFMNNETF EQLSADAKAI GDNAKWLLDQ AECIVTLWNG 

       130        140        150        160        170        180 
QPISVTPPNF VELEIVDTDP GLKGDTAGTG GKPATLSTGA VVKVPLFVQI GEVIKVDTRS 


GEYVSRVK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing and overexpression of the gene for prokaryotic factor EF-P involved in peptide bond synthesis."
Aoki H., Adams S.-L., Chung D.-G., Yaguchi M., Chuang S.-E., Ganoza M.C.
Nucleic Acids Res. 19:6215-6220(1991) [PubMed: 1956781] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-33; 71-80 AND 86-117.
[2]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed: 7610040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13.
Strain: K12 / EMG2.
[6]"Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reaction."
Aoki H., Adams S.-L., Turner M.A., Ganoza M.C.
Biochimie 79:7-11(1997) [PubMed: 9195040] [Abstract]
Cited for: CHARACTERIZATION.
[7]"The gene encoding the elongation factor P protein is essential for viability and is required for protein synthesis."
Aoki H., Dekany K., Adams S.L., Ganoza M.C.
J. Biol. Chem. 272:32254-32259(1997) [PubMed: 9405429] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[8]"Identification and quantitation of elongation factor EF-P in Escherichia coli cell-free extracts."
An G., Glick B.R., Friesen J.D., Ganoza M.C.
Can. J. Biochem. 58:1312-1314(1980) [PubMed: 7011506] [Abstract]
Cited for: COPY NUMBER.
[9]"Interactions of elongation factor EF-P with the Escherichia coli ribosome."
Aoki H., Xu J., Emili A., Chosay J.G., Golshani A., Ganoza M.C.
FEBS J. 275:671-681(2008) [PubMed: 18201202] [Abstract]
Cited for: PUTATIVE PTM, RIBOSOME-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61676 Genomic DNA. Translation: CAA43851.1.
U14003 Genomic DNA. Translation: AAA97046.1.
U00096 Genomic DNA. Translation: AAC77107.1.
AP009048 Genomic DNA. Translation: BAE78149.1.
PIRS34443.
RefSeqNP_418571.1. NC_000913.2.

3D structure databases

ProteinModelPortalP0A6N4.
SMRP0A6N4. Positions 3-187.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-31834N.
IntActP0A6N4. 1 interaction.

Proteomic databases

PRIDEP0A6N4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000001595; EBESCP00000001595; EBESCG00000001316.
EBESCT00000016420; EBESCP00000015711; EBESCG00000015480.
GeneID948661.
GenomeReviewsGene locus JW4107 in contig AP009048_GR.
Gene locus b4147 in contig U00096_GR.
KEGGecj:JW4107.
eco:b4147.
PATRIC32123863. VBIEscCol129921_4279.

Organism-specific databases

EchoBASEEB2023.
EcoGeneEG12099. efp.

Phylogenomic databases

eggNOGCOG0231.
GeneTreeEBGT00050000010829.
HOGENOMHBG303311.
OMAKDFTFLY.
PhylomeDBP0A6N4.
ProtClustDBPRK00529.

Enzyme and pathway databases

BioCycEcoCyc:EG12099-MONOMER.

Gene expression databases

GenevestigatorP0A6N4.

Family and domain databases

HAMAPMF_00141. EF-P.
[Tree]
InterProIPR015365. Elong-fact-P_C.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
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.
IPR014722. Transl_SH3-like_sub.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 2 hits.
G3DSA:2.30.30.30. Ribosomal_L2. 1 hit.
KOK02356.
PfamPF01132. EFP. 1 hit.
PF08207. EFP_N. 1 hit.
PF09285. Elong-fact-P_C. 1 hit.
[Graphical view]
PIRSFPIRSF005901. EF-P. 1 hit.
SMARTSM00841. Elong-fact-P_C. 1 hit.
[Graphical view]
SUPFAMSSF50249. Nucleic_acid_OB. 2 hits.
SSF50104. Transl_SH3_like. 1 hit.
TIGRFAMsTIGR00038. Efp. 1 hit.
PROSITEPS01275. EFP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEFP_ECOLI
AccessionPrimary (citable) accession number: P0A6N4
Secondary accession number(s): P33398, Q2M6F7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families