EFG_ECOLI
ID EFG_ECOLI Reviewed; 704 AA.
AC P0A6M8; P02996; Q2M705; Q9F439;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Elongation factor G;
DE Short=EF-G;
GN Name=fusA; Synonyms=far, fus; OrderedLocusNames=b3340, JW3302;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6322136; DOI=10.1093/nar/12.4.2181;
RA Zengel J.M., Archer R.H., Lindahl L.;
RT "The nucleotide sequence of the Escherichia coli fus gene, coding for
RT elongation factor G.";
RL Nucleic Acids Res. 12:2181-2192(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1398129; DOI=10.1016/0378-1119(92)90014-g;
RA Johanson U., Hughes D.;
RT "Comparison of the complete sequence of the str operon in Salmonella
RT typhimurium and Escherichia coli.";
RL Gene 120:93-98(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-704.
RX PubMed=7042386; DOI=10.1016/0014-5793(82)80503-6;
RA Ovchinnikov Y.A., Alakhov Y.B., Bundulis Y.P., Bundule M.A., Dovgas N.V.,
RA Kozlov V.P., Motuz L.P., Vinokurov L.M.;
RT "The primary structure of elongation factor G from Escherichia coli. A
RT complete amino acid sequence.";
RL FEBS Lett. 139:130-135(1982).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94.
RC STRAIN=K12;
RX PubMed=6989816; DOI=10.1016/s0021-9258(19)85545-x;
RA Post L.E., Nomura M.;
RT "DNA sequences from the str operon of Escherichia coli.";
RL J. Biol. Chem. 255:4660-4666(1980).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC STRAIN=L44;
RA Weigel C.T.O.;
RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9]
RP PROTEIN SEQUENCE OF 476-702.
RX PubMed=7016587; DOI=10.1016/0014-5793(81)80237-2;
RA Alakhov Y.B., Dovgas N.V., Motuz L.P., Vinokurov L.M., Ovchinnikov Y.A.;
RT "The primary structure of the elongation factor G from Escherichia coli:
RT amino acid sequence of the C-terminal domain.";
RL FEBS Lett. 126:183-186(1981).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 684-704.
RX PubMed=7011903; DOI=10.1016/0378-1119(80)90012-8;
RA Yokota T., Sugisaki H., Takanami M., Kaziro Y.;
RT "The nucleotide sequence of the cloned tufA gene of Escherichia coli.";
RL Gene 12:25-31(1980).
RN [11]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-504 AND LYS-643, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [13]
RP 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES WITH EF-G.
RX PubMed=12859903; DOI=10.1016/s0092-8674(03)00476-8;
RA Valle M., Zavialov A., Sengupta J., Rawat U., Ehrenberg M., Frank J.;
RT "Locking and unlocking of ribosomal motions.";
RL Cell 114:123-134(2003).
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000305}.
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DR EMBL; X00415; CAA25120.1; -; Genomic_DNA.
DR EMBL; X64592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U18997; AAA58137.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76365.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77951.1; -; Genomic_DNA.
DR EMBL; J01689; AAA50991.1; -; Genomic_DNA.
DR EMBL; X65735; CAA46645.1; -; Genomic_DNA.
DR PIR; G65127; EFECG.
DR RefSeq; NP_417799.1; NC_000913.3.
DR RefSeq; WP_000124700.1; NZ_STEB01000004.1.
DR PDB; 2RDO; EM; 9.10 A; 7=1-704.
DR PDB; 3J0E; EM; 9.90 A; H=2-703.
DR PDB; 3J9Z; EM; 3.60 A; S1=2-703.
DR PDB; 3JA1; EM; 3.60 A; S3=2-703.
DR PDB; 4V7B; EM; 6.80 A; AY=1-704.
DR PDB; 4V7D; EM; 7.60 A; BZ=2-704.
DR PDB; 4V9O; X-ray; 2.90 A; BV/DV/FV/HV=1-704.
DR PDB; 4V9P; X-ray; 2.90 A; BV/DV/FV/HV=1-704.
DR PDB; 7N2C; EM; 2.72 A; EF=2-704.
DR PDB; 7PJV; EM; 3.10 A; x=1-704.
DR PDB; 7PJY; EM; 3.10 A; x=1-704.
DR PDBsum; 2RDO; -.
DR PDBsum; 3J0E; -.
DR PDBsum; 3J9Z; -.
DR PDBsum; 3JA1; -.
DR PDBsum; 4V7B; -.
DR PDBsum; 4V7D; -.
DR PDBsum; 4V9O; -.
DR PDBsum; 4V9P; -.
DR PDBsum; 7N2C; -.
DR PDBsum; 7PJV; -.
DR PDBsum; 7PJY; -.
DR AlphaFoldDB; P0A6M8; -.
DR SMR; P0A6M8; -.
DR BioGRID; 4259389; 142.
DR BioGRID; 852158; 1.
DR DIP; DIP-31836N; -.
DR IntAct; P0A6M8; 76.
DR STRING; 511145.b3340; -.
DR CarbonylDB; P0A6M8; -.
DR iPTMnet; P0A6M8; -.
DR SWISS-2DPAGE; P0A6M8; -.
DR jPOST; P0A6M8; -.
DR PaxDb; P0A6M8; -.
DR PRIDE; P0A6M8; -.
DR EnsemblBacteria; AAC76365; AAC76365; b3340.
DR EnsemblBacteria; BAE77951; BAE77951; BAE77951.
DR GeneID; 67416971; -.
DR GeneID; 947847; -.
DR KEGG; ecj:JW3302; -.
DR KEGG; eco:b3340; -.
DR PATRIC; fig|1411691.4.peg.3391; -.
DR EchoBASE; EB0355; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_6; -.
DR InParanoid; P0A6M8; -.
DR OMA; AATTCHW; -.
DR PhylomeDB; P0A6M8; -.
DR BioCyc; EcoCyc:EG10360-MON; -.
DR BRENDA; 3.6.5.3; 2026.
DR EvolutionaryTrace; P0A6M8; -.
DR PRO; PR:P0A6M8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR035649; EFG_V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR004540; Transl_elong_EFG/EF2.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00484; EF-G; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Elongation factor; GTP-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7042386,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 2..704
FT /note="Elongation factor G"
FT /id="PRO_0000091119"
FT DOMAIN 8..290
FT /note="tr-type G"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 88..92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 504
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 643
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT CONFLICT 296..297
FT /note="NG -> DC (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 300..302
FT /note="Missing (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="T -> C (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="I -> V (in Ref. 5; AA sequence and 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="H -> K (in Ref. 5; AA sequence and 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="K -> H (in Ref. 5; AA sequence and 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="E -> Q (in Ref. 5; AA sequence and 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="E -> Q (in Ref. 5; AA sequence and 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="E -> Q (in Ref. 5; AA sequence and 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="E -> EQ (in Ref. 5; AA sequence and 9; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:4V9O"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 107..117
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 166..175
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:4V9O"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:4V9O"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:4V9O"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:4V9O"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 318..327
FT /evidence="ECO:0007829|PDB:4V9O"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 331..344
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:4V9O"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 368..378
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 416..421
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 428..441
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 463..477
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 498..504
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 517..524
FT /evidence="ECO:0007829|PDB:4V9O"
FT TURN 529..532
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 533..537
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:4V9O"
FT TURN 547..549
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 550..560
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:4V9O"
FT TURN 565..567
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 573..582
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 590..604
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 610..623
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 628..637
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 651..660
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 666..673
FT /evidence="ECO:0007829|PDB:4V9O"
FT TURN 674..676
FT /evidence="ECO:0007829|PDB:4V9O"
FT STRAND 680..689
FT /evidence="ECO:0007829|PDB:4V9O"
FT HELIX 692..697
FT /evidence="ECO:0007829|PDB:4V9O"
SQ SEQUENCE 704 AA; 77581 MW; 8C72B9F87253BC7B CRC64;
MARTTPIARY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHDGAATM DWMEQEQERG
ITITSAATTA FWSGMAKQYE PHRINIIDTP GHVDFTIEVE RSMRVLDGAV MVYCAVGGVQ
PQSETVWRQA NKYKVPRIAF VNKMDRMGAN FLKVVNQIKT RLGANPVPLQ LAIGAEEHFT
GVVDLVKMKA INWNDADQGV TFEYEDIPAD MVELANEWHQ NLIESAAEAS EELMEKYLGG
EELTEAEIKG ALRQRVLNNE IILVTCGSAF KNKGVQAMLD AVIDYLPSPV DVPAINGILD
DGKDTPAERH ASDDEPFSAL AFKIATDPFV GNLTFFRVYS GVVNSGDTVL NSVKAARERF
GRIVQMHANK REEIKEVRAG DIAAAIGLKD VTTGDTLCDP DAPIILERME FPEPVISIAV
EPKTKADQEK MGLALGRLAK EDPSFRVWTD EESNQTIIAG MGELHLDIIV DRMKREFNVE
ANVGKPQVAY RETIRQKVTD VEGKHAKQSG GRGQYGHVVI DMYPLEPGSN PKGYEFINDI
KGGVIPGEYI PAVDKGIQEQ LKAGPLAGYP VVDMGIRLHF GSYHDVDSSE LAFKLAASIA
FKEGFKKAKP VLLEPIMKVE VETPEENTGD VIGDLSRRRG MLKGQESEVT GVKIHAEVPL
SEMFGYATQL RSLTKGRASY TMEFLKYDEA PSNVAQAVIE ARGK
