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P0A6M8

- EFG_ECOLI

UniProt

P0A6M8 - EFG_ECOLI

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Protein
Elongation factor G
Gene
fusA, far, fus, b3340, JW3302
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 248GTP By similarity
Nucleotide bindingi88 – 925GTP By similarity
Nucleotide bindingi142 – 1454GTP By similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-HAMAP
  2. GTPase activity Source: InterPro
  3. translation elongation factor activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10360-MONOMER.
    ECOL316407:JW3302-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor G
    Short name:
    EF-G
    Gene namesi
    Name:fusA
    Synonyms:far, fus
    Ordered Locus Names:b3340, JW3302
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10360. fusA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 704703Elongation factor GUniRule annotation
    PRO_0000091119Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei504 – 5041N6-acetyllysine1 Publication
    Modified residuei643 – 6431N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP0A6M8.
    PRIDEiP0A6M8.

    2D gel databases

    SWISS-2DPAGEP0A6M8.

    PTM databases

    PhosSiteiP0809388.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A6M8.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-31836N.
    IntActiP0A6M8. 42 interactions.
    STRINGi511145.b3340.

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 167
    Beta strandi18 – 203
    Turni21 – 244
    Helixi25 – 3410
    Helixi54 – 585
    Beta strandi66 – 727
    Beta strandi82 – 887
    Beta strandi92 – 954
    Helixi97 – 1048
    Beta strandi107 – 11711
    Helixi121 – 13212
    Beta strandi138 – 1425
    Helixi151 – 16010
    Beta strandi166 – 17510
    Beta strandi178 – 1847
    Turni185 – 1884
    Beta strandi195 – 1995
    Turni209 – 2113
    Helixi212 – 2154
    Helixi220 – 2278
    Helixi231 – 2388
    Helixi245 – 25612
    Turni257 – 2593
    Beta strandi262 – 2643
    Turni269 – 2724
    Helixi275 – 28511
    Beta strandi289 – 2924
    Beta strandi300 – 3023
    Beta strandi318 – 32710
    Turni328 – 3303
    Beta strandi331 – 34414
    Beta strandi348 – 3514
    Turni352 – 3554
    Beta strandi356 – 3594
    Beta strandi363 – 3664
    Beta strandi368 – 37811
    Beta strandi382 – 3865
    Beta strandi396 – 3994
    Beta strandi400 – 4023
    Beta strandi416 – 4216
    Helixi425 – 4273
    Helixi428 – 44114
    Beta strandi446 – 4494
    Beta strandi451 – 4533
    Beta strandi456 – 4627
    Helixi463 – 47715
    Beta strandi482 – 4843
    Beta strandi491 – 4966
    Beta strandi498 – 5047
    Beta strandi509 – 5124
    Beta strandi517 – 5248
    Turni529 – 5324
    Beta strandi533 – 5375
    Beta strandi542 – 5454
    Turni547 – 5493
    Helixi550 – 56011
    Beta strandi562 – 5643
    Turni565 – 5673
    Beta strandi573 – 58210
    Beta strandi585 – 5873
    Helixi590 – 60415
    Helixi606 – 6083
    Beta strandi610 – 62314
    Helixi625 – 6273
    Helixi628 – 63710
    Beta strandi641 – 6444
    Beta strandi651 – 66010
    Helixi666 – 6738
    Turni674 – 6763
    Beta strandi680 – 68910
    Helixi692 – 6976

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP0A6M8.
    SMRiP0A6M8. Positions 2-703.

    Miscellaneous databases

    EvolutionaryTraceiP0A6M8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 290283tr-type G
    Add
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0480.
    HOGENOMiHOG000231585.
    KOiK02355.
    OMAiSGVQPQT.
    OrthoDBiEOG6X6RBF.
    PhylomeDBiP0A6M8.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.30.70.240. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_00054_B. EF_G_EF_2_B.
    InterProiIPR000795. 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]
    PfamiPF00679. 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]
    PRINTSiPR00315. ELONGATNFCT.
    SMARTiSM00838. EFG_C. 1 hit.
    SM00889. EFG_IV. 1 hit.
    [Graphical view]
    SUPFAMiSSF50447. SSF50447. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF54980. SSF54980. 2 hits.
    TIGRFAMsiTIGR00484. EF-G. 1 hit.
    TIGR00231. small_GTP. 1 hit.
    PROSITEiPS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A6M8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARTTPIARY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHDGAATM    50
    DWMEQEQERG ITITSAATTA FWSGMAKQYE PHRINIIDTP GHVDFTIEVE 100
    RSMRVLDGAV MVYCAVGGVQ PQSETVWRQA NKYKVPRIAF VNKMDRMGAN 150
    FLKVVNQIKT RLGANPVPLQ LAIGAEEHFT GVVDLVKMKA INWNDADQGV 200
    TFEYEDIPAD MVELANEWHQ NLIESAAEAS EELMEKYLGG EELTEAEIKG 250
    ALRQRVLNNE IILVTCGSAF KNKGVQAMLD AVIDYLPSPV DVPAINGILD 300
    DGKDTPAERH ASDDEPFSAL AFKIATDPFV GNLTFFRVYS GVVNSGDTVL 350
    NSVKAARERF GRIVQMHANK REEIKEVRAG DIAAAIGLKD VTTGDTLCDP 400
    DAPIILERME FPEPVISIAV EPKTKADQEK MGLALGRLAK EDPSFRVWTD 450
    EESNQTIIAG MGELHLDIIV DRMKREFNVE ANVGKPQVAY RETIRQKVTD 500
    VEGKHAKQSG GRGQYGHVVI DMYPLEPGSN PKGYEFINDI KGGVIPGEYI 550
    PAVDKGIQEQ LKAGPLAGYP VVDMGIRLHF GSYHDVDSSE LAFKLAASIA 600
    FKEGFKKAKP VLLEPIMKVE VETPEENTGD VIGDLSRRRG MLKGQESEVT 650
    GVKIHAEVPL SEMFGYATQL RSLTKGRASY TMEFLKYDEA PSNVAQAVIE 700
    ARGK 704
    Length:704
    Mass (Da):77,581
    Last modified:January 23, 2007 - v2
    Checksum:i8C72B9F87253BC7B
    GO

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti296 – 2972NG → DC AA sequence 1 Publication
    Sequence conflicti300 – 3023Missing AA sequence 1 Publication
    Sequence conflicti396 – 3961T → C AA sequence 1 Publication
    Sequence conflicti576 – 5761I → V AA sequence 1 Publication
    Sequence conflicti576 – 5761I → V AA sequence 1 Publication
    Sequence conflicti584 – 5841H → K AA sequence 1 Publication
    Sequence conflicti584 – 5841H → K AA sequence 1 Publication
    Sequence conflicti594 – 5941K → H AA sequence 1 Publication
    Sequence conflicti594 – 5941K → H AA sequence 1 Publication
    Sequence conflicti626 – 6261E → Q AA sequence 1 Publication
    Sequence conflicti626 – 6261E → Q AA sequence 1 Publication
    Sequence conflicti646 – 6461E → Q AA sequence 1 Publication
    Sequence conflicti646 – 6461E → Q AA sequence 1 Publication
    Sequence conflicti657 – 6571E → Q AA sequence 1 Publication
    Sequence conflicti657 – 6571E → Q AA sequence 1 Publication
    Sequence conflicti662 – 6621E → EQ AA sequence 1 Publication
    Sequence conflicti662 – 6621E → EQ AA sequence 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiG65127. EFECG.
    RefSeqiNP_417799.1. NC_000913.3.
    YP_492092.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76365; AAC76365; b3340.
    BAE77951; BAE77951; BAE77951.
    GeneIDi12930395.
    947847.
    KEGGiecj:Y75_p3836.
    eco:b3340.
    PATRICi32122112. VBIEscCol129921_3433.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi G65127. EFECG.
    RefSeqi NP_417799.1. NC_000913.3.
    YP_492092.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RDO electron microscopy 9.10 7 1-704 [» ]
    3J0E electron microscopy 9.90 H 2-703 [» ]
    3J5N electron microscopy 6.80 Y 1-704 [» ]
    3J5X electron microscopy 7.60 Z 2-704 [» ]
    4KIY X-ray 2.90 V 1-704 [» ]
    4KJ0 X-ray 2.90 V 1-704 [» ]
    4KJ2 X-ray 2.90 V 1-704 [» ]
    4KJ4 X-ray 2.90 V 1-704 [» ]
    4KJ6 X-ray 2.90 V 1-704 [» ]
    4KJ8 X-ray 2.90 V 1-704 [» ]
    4KJA X-ray 2.90 V 1-704 [» ]
    4KJC X-ray 2.90 V 1-704 [» ]
    ProteinModelPortali P0A6M8.
    SMRi P0A6M8. Positions 2-703.
    ModBasei Search...

    Protein-protein interaction databases

    DIPi DIP-31836N.
    IntActi P0A6M8. 42 interactions.
    STRINGi 511145.b3340.

    PTM databases

    PhosSitei P0809388.

    2D gel databases

    SWISS-2DPAGE P0A6M8.

    Proteomic databases

    PaxDbi P0A6M8.
    PRIDEi P0A6M8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76365 ; AAC76365 ; b3340 .
    BAE77951 ; BAE77951 ; BAE77951 .
    GeneIDi 12930395.
    947847.
    KEGGi ecj:Y75_p3836.
    eco:b3340.
    PATRICi 32122112. VBIEscCol129921_3433.

    Organism-specific databases

    EchoBASEi EB0355.
    EcoGenei EG10360. fusA.

    Phylogenomic databases

    eggNOGi COG0480.
    HOGENOMi HOG000231585.
    KOi K02355.
    OMAi SGVQPQT.
    OrthoDBi EOG6X6RBF.
    PhylomeDBi P0A6M8.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10360-MONOMER.
    ECOL316407:JW3302-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A6M8.
    PROi P0A6M8.

    Gene expression databases

    Genevestigatori P0A6M8.

    Family and domain databases

    Gene3Di 3.30.230.10. 1 hit.
    3.30.70.240. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPi MF_00054_B. EF_G_EF_2_B.
    InterProi IPR000795. 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 ]
    Pfami PF00679. 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 ]
    PRINTSi PR00315. ELONGATNFCT.
    SMARTi SM00838. EFG_C. 1 hit.
    SM00889. EFG_IV. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50447. SSF50447. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF54980. SSF54980. 2 hits.
    TIGRFAMsi TIGR00484. EF-G. 1 hit.
    TIGR00231. small_GTP. 1 hit.
    PROSITEi PS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    « Hide 'large scale' publications
    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. 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. Cited for: 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES WITH EF-G.

    Entry informationi

    Entry nameiEFG_ECOLI
    AccessioniPrimary (citable) accession number: P0A6M8
    Secondary accession number(s): P02996, Q2M705, Q9F439
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: September 3, 2014
    This is version 89 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi