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P0A6M8 (EFG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 88. 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 G

Short name=EF-G
Gene names
Name:fusA
Synonyms:far, fus
Ordered Locus Names:b3340, JW3302
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length704 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. HAMAP-Rule MF_00054_B

Subcellular location

Cytoplasm HAMAP-Rule MF_00054_B.

Sequence similarities

Belongs to the GTP-binding elongation factor family. EF-G/EF-2 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Nucleotide-binding
   Molecular functionElongation factor
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from direct assay PubMed 16858726. Source: UniProtKB

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

GTPase activity

Inferred from electronic annotation. Source: InterPro

translation elongation factor activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.8
Chain2 – 704703Elongation factor G HAMAP-Rule MF_00054_B
PRO_0000091119

Regions

Nucleotide binding17 – 248GTP By similarity
Nucleotide binding88 – 925GTP By similarity
Nucleotide binding142 – 1454GTP By similarity

Amino acid modifications

Modified residue5041N6-acetyllysine Ref.12
Modified residue6431N6-acetyllysine Ref.12

Experimental info

Sequence conflict296 – 2972NG → DC AA sequence Ref.5
Sequence conflict300 – 3023Missing AA sequence Ref.5
Sequence conflict3961T → C AA sequence Ref.5
Sequence conflict5761I → V AA sequence Ref.5
Sequence conflict5761I → V AA sequence Ref.9
Sequence conflict5841H → K AA sequence Ref.5
Sequence conflict5841H → K AA sequence Ref.9
Sequence conflict5941K → H AA sequence Ref.5
Sequence conflict5941K → H AA sequence Ref.9
Sequence conflict6261E → Q AA sequence Ref.5
Sequence conflict6261E → Q AA sequence Ref.9
Sequence conflict6461E → Q AA sequence Ref.5
Sequence conflict6461E → Q AA sequence Ref.9
Sequence conflict6571E → Q AA sequence Ref.5
Sequence conflict6571E → Q AA sequence Ref.9
Sequence conflict6621E → EQ AA sequence Ref.5
Sequence conflict6621E → EQ AA sequence Ref.9

Secondary structure

.............................................................................................................................. 704
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6M8 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8C72B9F87253BC7B

FASTA70477,581
        10         20         30         40         50         60 
MARTTPIARY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHDGAATM DWMEQEQERG 

        70         80         90        100        110        120 
ITITSAATTA FWSGMAKQYE PHRINIIDTP GHVDFTIEVE RSMRVLDGAV MVYCAVGGVQ 

       130        140        150        160        170        180 
PQSETVWRQA NKYKVPRIAF VNKMDRMGAN FLKVVNQIKT RLGANPVPLQ LAIGAEEHFT 

       190        200        210        220        230        240 
GVVDLVKMKA INWNDADQGV TFEYEDIPAD MVELANEWHQ NLIESAAEAS EELMEKYLGG 

       250        260        270        280        290        300 
EELTEAEIKG ALRQRVLNNE IILVTCGSAF KNKGVQAMLD AVIDYLPSPV DVPAINGILD 

       310        320        330        340        350        360 
DGKDTPAERH ASDDEPFSAL AFKIATDPFV GNLTFFRVYS GVVNSGDTVL NSVKAARERF 

       370        380        390        400        410        420 
GRIVQMHANK REEIKEVRAG DIAAAIGLKD VTTGDTLCDP DAPIILERME FPEPVISIAV 

       430        440        450        460        470        480 
EPKTKADQEK MGLALGRLAK EDPSFRVWTD EESNQTIIAG MGELHLDIIV DRMKREFNVE 

       490        500        510        520        530        540 
ANVGKPQVAY RETIRQKVTD VEGKHAKQSG GRGQYGHVVI DMYPLEPGSN PKGYEFINDI 

       550        560        570        580        590        600 
KGGVIPGEYI PAVDKGIQEQ LKAGPLAGYP VVDMGIRLHF GSYHDVDSSE LAFKLAASIA 

       610        620        630        640        650        660 
FKEGFKKAKP VLLEPIMKVE VETPEENTGD VIGDLSRRRG MLKGQESEVT GVKIHAEVPL 

       670        680        690        700 
SEMFGYATQL RSLTKGRASY TMEFLKYDEA PSNVAQAVIE ARGK 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of the Escherichia coli fus gene, coding for elongation factor G."
Zengel J.M., Archer R.H., Lindahl L.
Nucleic Acids Res. 12:2181-2192(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Comparison of the complete sequence of the str operon in Salmonella typhimurium and Escherichia coli."
Johanson U., Hughes D.
Gene 120:93-98(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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 277:1453-1462(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The primary structure of elongation factor G from Escherichia coli. A complete amino acid sequence."
Ovchinnikov Y.A., Alakhov Y.B., Bundulis Y.P., Bundule M.A., Dovgas N.V., Kozlov V.P., Motuz L.P., Vinokurov L.M.
FEBS Lett. 139:130-135(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-704.
[6]"DNA sequences from the str operon of Escherichia coli."
Post L.E., Nomura M.
J. Biol. Chem. 255:4660-4666(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94.
Strain: K12.
[7]Weigel C.T.O.
Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
Strain: L44.
[8]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13.
Strain: K12 / EMG2.
[9]"The primary structure of the elongation factor G from Escherichia coli: amino acid sequence of the C-terminal domain."
Alakhov Y.B., Dovgas N.V., Motuz L.P., Vinokurov L.M., Ovchinnikov Y.A.
FEBS Lett. 126:183-186(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 476-702.
[10]"The nucleotide sequence of the cloned tufA gene of Escherichia coli."
Yokota T., Sugisaki H., Takanami M., Kaziro Y.
Gene 12:25-31(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 684-704.
[11]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[12]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-504 AND LYS-643, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[13]"Locking and unlocking of ribosomal motions."
Valle M., Zavialov A., Sengupta J., Rawat U., Ehrenberg M., Frank J.
Cell 114:123-134(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES WITH EF-G.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00415 Genomic DNA. Translation: CAA25120.1.
X64592 Genomic DNA. No translation available.
U18997 Genomic DNA. Translation: AAA58137.1.
U00096 Genomic DNA. Translation: AAC76365.1.
AP009048 Genomic DNA. Translation: BAE77951.1.
J01689 Genomic DNA. Translation: AAA50991.1.
X65735 Genomic DNA. Translation: CAA46645.1.
PIREFECG. G65127.
RefSeqNP_417799.1. NC_000913.3.
YP_492092.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RDOelectron microscopy9.1071-704[»]
3J0Eelectron microscopy9.90H2-703[»]
3J5Nelectron microscopy6.80Y1-704[»]
3J5Xelectron microscopy7.60Z2-704[»]
4KIYX-ray2.90V1-704[»]
4KJ0X-ray2.90V1-704[»]
4KJ2X-ray2.90V1-704[»]
4KJ4X-ray2.90V1-704[»]
4KJ6X-ray2.90V1-704[»]
4KJ8X-ray2.90V1-704[»]
4KJAX-ray2.90V1-704[»]
4KJCX-ray2.90V1-704[»]
ProteinModelPortalP0A6M8.
SMRP0A6M8. Positions 2-703.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-31836N.
IntActP0A6M8. 42 interactions.
STRING511145.b3340.

PTM databases

PhosSiteP0809388.

2D gel databases

SWISS-2DPAGEP0A6M8.

Proteomic databases

PaxDbP0A6M8.
PRIDEP0A6M8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76365; AAC76365; b3340.
BAE77951; BAE77951; BAE77951.
GeneID12930395.
947847.
KEGGecj:Y75_p3836.
eco:b3340.
PATRIC32122112. VBIEscCol129921_3433.

Organism-specific databases

EchoBASEEB0355.
EcoGeneEG10360. fusA.

Phylogenomic databases

eggNOGCOG0480.
HOGENOMHOG000231585.
KOK02355.
OMASGVQPQT.
OrthoDBEOG6X6RBF.
PhylomeDBP0A6M8.

Enzyme and pathway databases

BioCycEcoCyc:EG10360-MONOMER.
ECOL316407:JW3302-MONOMER.

Gene expression databases

GenevestigatorP0A6M8.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_00054_B. EF_G_EF_2_B.
InterProIPR000795. EF_GTP-bd_dom.
IPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR004540. Transl_elong_EFG/EF2.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SMARTSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsTIGR00484. EF-G. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A6M8.
PROP0A6M8.

Entry information

Entry nameEFG_ECOLI
AccessionPrimary (citable) accession number: P0A6M8
Secondary accession number(s): P02996, Q2M705, Q9F439
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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