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Database: UniProt/SWISS-PROT
Entry: EFTU1_ECOLI
LinkDB: EFTU1_ECOLI
Original site: EFTU1_ECOLI 
ID   EFTU1_ECOLI             Reviewed;         394 AA.
AC   P0CE47; O68929; P02990; P0A6N1; Q2M704; Q2M8R6; Q8X4S9; Q8XED3;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   22-NOV-2017, entry version 69.
DE   RecName: Full=Elongation factor Tu 1 {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu 1 {ECO:0000255|HAMAP-Rule:MF_00118};
DE   AltName: Full=Bacteriophage Q beta RNA-directed RNA polymerase subunit III {ECO:0000303|PubMed:816798};
DE   AltName: Full=P-43;
GN   Name=tufA {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=b3339, JW3301;
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=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
RT   coli.";
RL   Gene 12:25-31(1980).
RN   [2]
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.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-394, ACETYLATION AT SER-2, AND METHYLATION AT
RP   LYS-57.
RC   STRAIN=B;
RX   PubMed=6997043; DOI=10.1111/j.1432-1033.1980.tb04748.x;
RA   Jones M.D., Petersen T.E., Nielsen K.M., Magnusson S.,
RA   Sottrup-Jensen L., Gausing K., Clark B.F.C.;
RT   "The complete amino-acid sequence of elongation factor Tu from
RT   Escherichia coli.";
RL   Eur. J. Biochem. 108:507-526(1980).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-394, ACETYLATION AT SER-2, AND METHYLATION AT
RP   LYS-57.
RX   PubMed=7021545;
RA   Laursen R.A., L'Italien J.J., Nagarkatti S., Miller D.L.;
RT   "The amino acid sequence of elongation factor Tu of Escherichia coli.
RT   The complete sequence.";
RL   J. Biol. Chem. 256:8102-8109(1981).
RN   [6]
RP   PROTEIN SEQUENCE OF 46-59, AND METHYLATION AT LYS-57.
RC   STRAIN=B;
RX   PubMed=389663; DOI=10.1016/0014-5793(79)80407-X;
RA   L'Italien J.J., Laursen R.A.;
RT   "Location of the site of methylation in elongation factor Tu.";
RL   FEBS Lett. 107:359-362(1979).
RN   [7]
RP   PROTEIN SEQUENCE OF 76-90, AND MUTAGENESIS OF PRO-83.
RX   PubMed=2157708;
RA   Cool R.H., Jensen M., Jonak J., Clark B.F.C., Parmeggiani A.;
RT   "Substitution of proline 82 by threonine induces autophosphorylating
RT   activity in GTP-binding domain of elongation factor Tu.";
RL   J. Biol. Chem. 265:6744-6749(1990).
RN   [8]
RP   PROTEIN SEQUENCE OF 153-176 AND 262-290, METHYLATION AT LYS-57 IN
RP   RESPONSE TO NUTRIENT STARVATION, AND SUBCELLULAR LOCATION.
RC   STRAIN=B/R;
RX   PubMed=2022614; DOI=10.1128/jb.173.10.3096-3100.1991;
RA   Young C.C., Bernlohr R.W.;
RT   "Elongation factor Tu is methylated in response to nutrient
RT   deprivation in Escherichia coli.";
RL   J. Bacteriol. 173:3096-3100(1991).
RN   [9]
RP   PROTEIN SEQUENCE OF 311-322, AND BLOCKAGE OF N-TERMINUS.
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
RT   in the genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 369-394.
RC   STRAIN=ECOR 30;
RA   Noorani S.M., Lindahl L., Zengel J.M.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   BLOCKAGE OF N-TERMINUS, AND SUBCELLULAR LOCATION.
RC   STRAIN=K12 / BHB 960;
RX   PubMed=775340; DOI=10.1038/261023a0;
RA   Jacobson G.R., Rosenbusch J.P.;
RT   "Abundance and membrane association of elongation factor Tu in E.
RT   coli.";
RL   Nature 261:23-26(1976).
RN   [12]
RP   FUNCTION IN VIRAL RNA REPLICATION, AND SUBUNIT.
RX   PubMed=816798;
RA   Carmichael G.G., Landers T.A., Weber K.;
RT   "Immunochemical analysis of the functions of the subunits of phage
RT   Qbeta ribonucleic acid replicase.";
RL   J. Biol. Chem. 251:2744-2748(1976).
RN   [13]
RP   PHOSPHORYLATION AT THR-383, AND PROTEIN SEQUENCE OF 290-304 AND
RP   383-391.
RX   PubMed=8416965;
RA   Lippmann C., Lindschau C., Vijgenboom E., Schroeder W., Bosch L.,
RA   Erdmann V.A.;
RT   "Prokaryotic elongation factor Tu is phosphorylated in vivo.";
RL   J. Biol. Chem. 268:601-607(1993).
RN   [14]
RP   MUTAGENESIS OF ASP-139.
RX   PubMed=3308869;
RA   Hwang Y.-W., Miller D.L.;
RT   "A mutation that alters the nucleotide specificity of elongation
RT   factor Tu, a GTP regulatory protein.";
RL   J. Biol. Chem. 262:13081-13085(1987).
RN   [15]
RP   MUTAGENESIS OF VAL-21.
RX   PubMed=2684669; DOI=10.1111/j.1432-1033.1989.tb15121.x;
RA   Jacquet E., Parmeggiani A.;
RT   "Substitution of Val20 by Gly in elongation factor Tu. Effects on the
RT   interaction with elongation factors Ts, aminoacyl-tRNA and
RT   ribosomes.";
RL   Eur. J. Biochem. 185:341-346(1989).
RN   [16]
RP   MUTAGENESIS OF LYS-137.
RX   PubMed=2498311;
RA   Hwang Y.-W., Sanchez A., Miller D.L.;
RT   "Mutagenesis of bacterial elongation factor Tu at lysine 136. A
RT   conserved amino acid in GTP regulatory proteins.";
RL   J. Biol. Chem. 264:8304-8309(1989).
RN   [17]
RP   MUTAGENESIS.
RX   PubMed=2508560; DOI=10.1016/0003-9861(89)90452-9;
RA   Hwang Y.-W., McCabe P.G., Innis M.A., Miller D.L.;
RT   "Site-directed mutagenesis of the GDP binding domain of bacterial
RT   elongation factor Tu.";
RL   Arch. Biochem. Biophys. 274:394-403(1989).
RN   [18]
RP   CHARACTERIZATION OF MUTANT ASP-223.
RX   PubMed=8978702;
RA   Vorstenbosch E., Pape T., Rodnina M.V., Kraal B., Wintermeyer W.;
RT   "The G222D mutation in elongation factor Tu inhibits the codon-induced
RT   conformational changes leading to GTPase activation on the ribosome.";
RL   EMBO J. 15:6766-6774(1996).
RN   [19]
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.,
RA   Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [20]
RP   MUTAGENESIS OF HIS-20; GLN-115 AND GLU-349.
RX   PubMed=9468511; DOI=10.1074/jbc.273.8.4556;
RA   Zhang Y., Yu N.-J., Spremulli L.L.;
RT   "Mutational analysis of the roles of residues in Escherichia coli
RT   elongation factor Ts in the interaction with elongation factor Tu.";
RL   J. Biol. Chem. 273:4556-4562(1998).
RN   [21]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-314, AND IDENTIFICATION BY
RP   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   [22]
RP   VARIANTS RESISTANT TO KIRROMYCIN.
RX   PubMed=7525272;
RA   Mesters J.R., Zeef L.A.H., Hilgenfeld R., de Graaf J.M., Kraal B.,
RA   Bosch L.;
RT   "The structural and functional basis for the kirromycin resistance of
RT   mutant EF-Tu species in Escherichia coli.";
RL   EMBO J. 13:4877-4885(1994).
RN   [23]
RP   VARIANTS RESISTANT TO PULVOMYCIN.
RX   PubMed=7957075;
RA   Zeef L.A.H., Bosch L., Anborgh P.H., Cetin R., Parmeggiani A.,
RA   Hilgenfeld R.;
RT   "Pulvomycin-resistant mutants of E.coli elongation factor Tu.";
RL   EMBO J. 13:5113-5120(1994).
RN   [24]
RP   FUNCTION IN TRANS-TRANSLATION, AND TMRNA-BINDING.
RC   STRAIN=K12 / BW25113;
RX   PubMed=15069072; DOI=10.1074/jbc.M314086200;
RA   Hallier M., Ivanova N., Rametti A., Pavlov M., Ehrenberg M.,
RA   Felden B.;
RT   "Pre-binding of small protein B to a stalled ribosome triggers trans-
RT   translation.";
RL   J. Biol. Chem. 279:25978-25985(2004).
RN   [25]
RP   PHOSPHORYLATION AT THR-383 BY HIPA.
RX   PubMed=19150849; DOI=10.1126/science.1163806;
RA   Schumacher M.A., Piro K.M., Xu W., Hansen S., Lewis K., Brennan R.G.;
RT   "Molecular mechanisms of HipA-mediated multidrug tolerance and its
RT   neutralization by HipB.";
RL   Science 323:396-401(2009).
RN   [26]
RP   LACK OF PHOSPHORYLATION BY HIPA.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=24095282; DOI=10.1016/j.molcel.2013.08.045;
RA   Germain E., Castro-Roa D., Zenkin N., Gerdes K.;
RT   "Molecular mechanism of bacterial persistence by HipA.";
RL   Mol. Cell 52:248-254(2013).
RN   [27]
RP   PHOSPHORYLATION AT THR-383 BY DOC, AND MUTAGENESIS OF THR-383.
RX   PubMed=24141193; DOI=10.1038/nchembio.1364;
RA   Castro-Roa D., Garcia-Pino A., De Gieter S., van Nuland N.A.,
RA   Loris R., Zenkin N.;
RT   "The Fic protein Doc uses an inverted substrate to phosphorylate and
RT   inactivate EF-Tu.";
RL   Nat. Chem. Biol. 9:811-817(2013).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 2-392 IN A MODIFIED FORM.
RX   PubMed=3908095;
RA   la Cour T.F., Nyborg J., Thirup S., Clark B.F.;
RT   "Structural details of the binding of guanosine diphosphate to
RT   elongation factor Tu from E. coli as studied by X-ray
RT   crystallography.";
RL   EMBO J. 4:2385-2388(1985).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2-394 IN COMPLEX WITH GDP.
RX   PubMed=9918724; DOI=10.1006/jmbi.1998.2387;
RA   Song H., Parsons M.R., Rowsell S., Leonard G., Phillips S.E.V.;
RT   "Crystal structure of intact elongation factor EF-Tu from Escherichia
RT   coli in GDP conformation at 2.05-A resolution.";
RL   J. Mol. Biol. 285:1245-1256(1999).
RN   [30]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 2-393 IN COMPLEX WITH
RP   ANTIBIOTIC GE2270A.
RX   PubMed=10625477; DOI=10.1021/bi9913597;
RA   Heffron S.E., Jurnak F.;
RT   "Structure of an EF-Tu complex with a thiazolyl peptide antibiotic
RT   determined at 2.35 A resolution: atomic basis for GE2270A inhibition
RT   of EF-Tu.";
RL   Biochemistry 39:37-45(2000).
RN   [31]
RP   X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF EF-TU-GDP.
RX   PubMed=16552145; DOI=10.1107/S0907444906004021;
RA   Heffron S.E., Moeller R., Jurnak F.;
RT   "Solving the structure of Escherichia coli elongation factor Tu using
RT   a twinned data set.";
RL   Acta Crystallogr. D 62:433-438(2006).
RN   [32]
RP   X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 9-44 AND 60-393 IN COMPLEX
RP   WITH TETRACYCLINE.
RX   PubMed=17057344; DOI=10.1107/S0907444906035426;
RA   Heffron S.E., Mui S., Aorora A., Abel K., Bergmann E., Jurnak F.;
RT   "Molecular complementarity between tetracycline and the GTPase active
RT   site of elongation factor Tu.";
RL   Acta Crystallogr. D 62:1392-1400(2006).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis.
CC   -!- FUNCTION: May play an important regulatory role in cell growth and
CC       in the bacterial response to nutrient deprivation.
CC   -!- FUNCTION: In case of infection by bacteriophage Qbeta, part of the
CC       viral RNA-dependent RNA polymerase complex. With EF-Ts may provide
CC       a stabilizing scaffold for the beta (catalytic) subunit. Helps
CC       separate the double-stranded RNA of the template and growing RNA
CC       during elongation. With the beta subunit helps form the exit
CC       tunnel for template RNA. {ECO:0000269|PubMed:816798, ECO:0000305}.
CC   -!- FUNCTION: Plays a stimulatory role in trans-translation; binds
CC       tmRNA. {ECO:0000269|PubMed:15069072}.
CC   -!- FUNCTION: Protects glycyl-tRNA(Gly) from hydrolysis by E.coli D-
CC       aminoacyl-tRNA deacylase (dtd) (By similarity).
CC       {ECO:0000250|UniProtKB:Q5SHN6}.
CC   -!- SUBUNIT: Monomer. In case of infection by bacteriophage Qbeta,
CC       part of the viral RNA-dependent RNA polymerase complex, the other
CC       subunits are the viral replicase catalytic subunit (AC P14647),
CC       host ribosomal protein S1 and EF-Ts (PubMed:816798).
CC       {ECO:0000255|HAMAP-Rule:MF_00118, ECO:0000269|PubMed:10625477,
CC       ECO:0000269|PubMed:17057344, ECO:0000269|PubMed:816798,
CC       ECO:0000269|PubMed:9918724, ECO:0000305}.
CC   -!- INTERACTION:
CC       P14647:- (xeno); NbExp=2; IntAct=EBI-301077, EBI-9010000;
CC       P61517:can; NbExp=2; IntAct=EBI-301077, EBI-562106;
CC       P76251:dmlA; NbExp=2; IntAct=EBI-301077, EBI-560661;
CC       Q06259:doc (xeno); NbExp=5; IntAct=EBI-301077, EBI-2908816;
CC       P15038:helD; NbExp=3; IntAct=EBI-301077, EBI-551473;
CC       P0A6Y5:hslO; NbExp=3; IntAct=EBI-301077, EBI-562857;
CC       P00956:ileS; NbExp=2; IntAct=EBI-301077, EBI-552928;
CC       P04951:kdsB; NbExp=2; IntAct=EBI-301077, EBI-544810;
CC       P10441:lpxB; NbExp=3; IntAct=EBI-301077, EBI-553692;
CC       P22634:murI; NbExp=2; IntAct=EBI-301077, EBI-554903;
CC       P23909:mutS; NbExp=2; IntAct=EBI-301077, EBI-554920;
CC       P33590:nikA; NbExp=2; IntAct=EBI-301077, EBI-555182;
CC       P0A6Z6:nikR; NbExp=3; IntAct=EBI-301077, EBI-562488;
CC       P77756:queC; NbExp=3; IntAct=EBI-301077, EBI-560024;
CC       P0AG30:rho; NbExp=2; IntAct=EBI-301077, EBI-545468;
CC       P0ADX9:rsmD; NbExp=2; IntAct=EBI-301077, EBI-561207;
CC       P0A6P1:tsf; NbExp=12; IntAct=EBI-301077, EBI-301164;
CC       P0A8J4:ybeD; NbExp=3; IntAct=EBI-301077, EBI-370708;
CC       P63389:yheS; NbExp=3; IntAct=EBI-301077, EBI-561198;
CC       P39408:yjjV; NbExp=2; IntAct=EBI-301077, EBI-561387;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral
CC       membrane protein. Note=Between 50-80% of the protein is associated
CC       with the cell inner membrane. Localization to the membrane has
CC       been suggested to follow nutrient stress.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- PTM: Methylated in vivo on Lys-57 in response to nutrient
CC       starvation. {ECO:0000269|PubMed:2022614,
CC       ECO:0000269|PubMed:389663, ECO:0000269|PubMed:6997043,
CC       ECO:0000269|PubMed:7021545}.
CC   -!- PTM: Phosphorylated in vitro by phage protein doc on Thr-383.
CC       {ECO:0000269|PubMed:19150849, ECO:0000269|PubMed:24141193,
CC       ECO:0000269|PubMed:8416965}.
CC   -!- PTM: Phosphorylated in vitro by HipA on Thr-383 (PubMed:19150849),
CC       this has since been reported not to occur in vivo
CC       (PubMed:24095282). {ECO:0000269|PubMed:19150849,
CC       ECO:0000269|PubMed:24095282, ECO:0000269|PubMed:24141193,
CC       ECO:0000269|PubMed:8416965}.
CC   -!- MISCELLANEOUS: Present with about 70,000 molecules/cell.
CC       {ECO:0000305|PubMed:775340}.
CC   -!- MISCELLANEOUS: This chain is also used in bacteriophage Q-beta RNA
CC       polymerase. {ECO:0000269|PubMed:816798}.
CC   -!- MISCELLANEOUS: The antibiotic kirromycin inhibits protein
CC       biosynthesis by inhibiting the release of EF-Tu from the ribosome.
CC       {ECO:0000269|PubMed:7525272}.
CC   -!- MISCELLANEOUS: The antibiotic pulvomycin inhibits protein
CC       biosynthesis by disrupting the allosteric control mechanism of EF-
CC       Tu. {ECO:0000269|PubMed:7957075}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- CAUTION: EF-Tu 1 and EF-Tu 2 differ in a single position and are
CC       no longer merged. However, many papers are found in both entries
CC       as it is not always possible to determine for each paper which of
CC       EF-Tu 1 or EF-Tu 2 was being worked upon. {ECO:0000305}.
DR   EMBL; J01690; AAA50993.1; -; Genomic_DNA.
DR   EMBL; M10459; AAA24702.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76364.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77952.1; -; Genomic_DNA.
DR   EMBL; U18997; AAA58136.1; -; Genomic_DNA.
DR   EMBL; AF058450; AAC14286.1; -; Genomic_DNA.
DR   PIR; A91475; EFECTA.
DR   RefSeq; NP_417798.1; NC_000913.3.
DR   RefSeq; WP_000031783.1; NZ_LN832404.1.
DR   PDB; 1D8T; X-ray; 2.35 A; A/B=2-394.
DR   PDB; 1EFC; X-ray; 2.05 A; A/B=2-393.
DR   PDB; 1ETU; X-ray; 2.90 A; A=2-394.
DR   PDB; 1MJ1; EM; 13.00 A; A=8-389.
DR   PDB; 2FX3; X-ray; 3.40 A; A=2-394.
DR   PDB; 2HCJ; X-ray; 2.12 A; A=9-45, B=60-394.
DR   PDB; 2HDN; X-ray; 2.80 A; A/C/E/G/I/K=9-45, B/D/F/H/J/L=60-394.
DR   PDB; 3EP2; EM; -; X=2-393.
DR   PDB; 3EQ3; EM; -; X=2-393.
DR   PDB; 3EQ4; EM; -; X=2-393.
DR   PDB; 3U2Q; X-ray; 2.70 A; A=3-394.
DR   PDB; 3U6B; X-ray; 2.12 A; A/B=3-394.
DR   PDB; 3U6K; X-ray; 2.45 A; A/B=3-394.
DR   PDB; 4G5G; X-ray; 2.30 A; A=3-394.
DR   PDB; 4PC3; X-ray; 1.83 A; A/B=1-394.
DR   PDB; 4PC7; X-ray; 3.60 A; A=1-394.
DR   PDB; 4Q7J; X-ray; 2.90 A; B/F=2-394.
DR   PDB; 4V69; EM; 6.70 A; AZ=2-393.
DR   PDB; 5I4Q; X-ray; 2.35 A; C=178-394.
DR   PDB; 5I4R; X-ray; 3.30 A; D/H=60-394.
DR   PDB; 5JBQ; X-ray; 2.01 A; A=1-394.
DR   PDB; 5UYK; EM; 3.90 A; Z=2-393.
DR   PDB; 5UYL; EM; 3.60 A; Z=2-393.
DR   PDB; 5UYM; EM; 3.20 A; Z=2-393.
DR   PDB; 5UYN; EM; 4.00 A; Z=2-393.
DR   PDB; 5UYP; EM; 3.90 A; Z=2-393.
DR   PDB; 5UYQ; EM; 3.80 A; Z=2-393.
DR   PDBsum; 1D8T; -.
DR   PDBsum; 1EFC; -.
DR   PDBsum; 1ETU; -.
DR   PDBsum; 1MJ1; -.
DR   PDBsum; 2FX3; -.
DR   PDBsum; 2HCJ; -.
DR   PDBsum; 2HDN; -.
DR   PDBsum; 3EP2; -.
DR   PDBsum; 3EQ3; -.
DR   PDBsum; 3EQ4; -.
DR   PDBsum; 3U2Q; -.
DR   PDBsum; 3U6B; -.
DR   PDBsum; 3U6K; -.
DR   PDBsum; 4G5G; -.
DR   PDBsum; 4PC3; -.
DR   PDBsum; 4PC7; -.
DR   PDBsum; 4Q7J; -.
DR   PDBsum; 4V69; -.
DR   PDBsum; 5I4Q; -.
DR   PDBsum; 5I4R; -.
DR   PDBsum; 5JBQ; -.
DR   PDBsum; 5UYK; -.
DR   PDBsum; 5UYL; -.
DR   PDBsum; 5UYM; -.
DR   PDBsum; 5UYN; -.
DR   PDBsum; 5UYP; -.
DR   PDBsum; 5UYQ; -.
DR   ProteinModelPortal; P0CE47; -.
DR   SMR; P0CE47; -.
DR   BioGrid; 4259390; 74.
DR   BioGrid; 852150; 1.
DR   DIP; DIP-6159N; -.
DR   IntAct; P0CE47; 162.
DR   STRING; 316385.ECDH10B_3514; -.
DR   iPTMnet; P0CE47; -.
DR   PaxDb; P0CE47; -.
DR   PRIDE; P0CE47; -.
DR   EnsemblBacteria; AAC76364; AAC76364; b3339.
DR   EnsemblBacteria; BAE77952; BAE77952; BAE77952.
DR   GeneID; 947838; -.
DR   KEGG; ecj:JW3301; -.
DR   KEGG; eco:b3339; -.
DR   PATRIC; fig|1411691.4.peg.3392; -.
DR   EchoBASE; EB1029; -.
DR   EcoGene; EG11036; tufA.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   InParanoid; P0CE47; -.
DR   KO; K02358; -.
DR   PhylomeDB; P0CE47; -.
DR   BioCyc; EcoCyc:EG11036-MONOMER; -.
DR   EvolutionaryTrace; P0CE47; -.
DR   PRO; PR:P0CE47; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   CDD; cd03697; EFTU_II; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; TF_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00485; EF-Tu; 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; Antibiotic resistance; Cell inner membrane;
KW   Cell membrane; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Elongation factor; GTP-binding; Membrane;
KW   Methylation; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; RNA-binding.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:6997043,
FT                                ECO:0000269|PubMed:7021545}.
FT   CHAIN         2    394       Elongation factor Tu 1.
FT                                /FTId=PRO_0000091320.
FT   DOMAIN       10    204       tr-type G.
FT   NP_BIND      19     26       GTP.
FT   NP_BIND      81     85       GTP.
FT   NP_BIND     136    139       GTP.
FT   REGION       19     26       G1. {ECO:0000250}.
FT   REGION       60     64       G2. {ECO:0000250}.
FT   REGION       81     84       G3. {ECO:0000250}.
FT   REGION      136    139       G4. {ECO:0000250}.
FT   REGION      174    176       G5. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000269|PubMed:6997043,
FT                                ECO:0000269|PubMed:7021545}.
FT   MOD_RES      57     57       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000269|PubMed:2022614,
FT                                ECO:0000269|PubMed:389663,
FT                                ECO:0000269|PubMed:6997043,
FT                                ECO:0000269|PubMed:7021545}.
FT   MOD_RES      57     57       N6-methyllysine; alternate.
FT                                {ECO:0000269|PubMed:2022614,
FT                                ECO:0000269|PubMed:389663,
FT                                ECO:0000269|PubMed:6997043,
FT                                ECO:0000269|PubMed:7021545}.
FT   MOD_RES     314    314       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:18723842}.
FT   MOD_RES     383    383       Phosphothreonine.
FT                                {ECO:0000269|PubMed:19150849,
FT                                ECO:0000269|PubMed:24141193,
FT                                ECO:0000269|PubMed:8416965}.
FT   MUTAGEN      20     20       H->A: No change in binding GDP and 3-fold
FT                                reduction in binding EF-Ts.
FT                                {ECO:0000269|PubMed:9468511}.
FT   MUTAGEN      21     21       V->G: Lowers GTPase activity 5 to 10-
FT                                fold. {ECO:0000269|PubMed:2684669}.
FT   MUTAGEN      83     83       P->T: Loss of GTPase activity and
FT                                creation of an autophosphorylation site.
FT                                {ECO:0000269|PubMed:2157708}.
FT   MUTAGEN     115    115       Q->A: Weaker binding for GDP and for EF-
FT                                Ts. {ECO:0000269|PubMed:9468511}.
FT   MUTAGEN     125    125       Q->K: Kirromycin resistant.
FT                                {ECO:0000269|PubMed:2508560}.
FT   MUTAGEN     137    137       K->R,Q,E,I: Reduces affinity for GDP.
FT                                {ECO:0000269|PubMed:2498311}.
FT   MUTAGEN     139    139       D->N: Reduces affinity for GDP; increases
FT                                affinity for XDP.
FT                                {ECO:0000269|PubMed:3308869}.
FT   MUTAGEN     223    223       G->D: Inhibits codon-induced
FT                                conformational changes leading to GTPase
FT                                activation on the ribosome.
FT                                {ECO:0000269|PubMed:2508560}.
FT   MUTAGEN     231    231       R->C: Pulvomycin resistant.
FT                                {ECO:0000269|PubMed:2508560}.
FT   MUTAGEN     317    317       G->D: Kirromycin resistant.
FT                                {ECO:0000269|PubMed:2508560}.
FT   MUTAGEN     334    334       R->C: Pulvomycin resistant.
FT                                {ECO:0000269|PubMed:2508560}.
FT   MUTAGEN     335    335       T->A: Pulvomycin resistant.
FT                                {ECO:0000269|PubMed:2508560}.
FT   MUTAGEN     349    349       E->A: No change in binding GDP but higher
FT                                binding constant for EF-Ts.
FT                                {ECO:0000269|PubMed:9468511}.
FT   MUTAGEN     376    376       A->T,V: Kirromycin resistant.
FT                                {ECO:0000269|PubMed:2508560}.
FT   MUTAGEN     383    383       T->V: No longer phosphorylated by phage
FT                                protein doc, has no effect on
FT                                translation.
FT                                {ECO:0000269|PubMed:24141193}.
FT   HELIX         4      7       {ECO:0000244|PDB:5JBQ}.
FT   STRAND       12     19       {ECO:0000244|PDB:4PC3}.
FT   STRAND       20     24       {ECO:0000244|PDB:1ETU}.
FT   HELIX        25     40       {ECO:0000244|PDB:4PC3}.
FT   HELIX        47     51       {ECO:0000244|PDB:5JBQ}.
FT   STRAND       55     60       {ECO:0000244|PDB:5JBQ}.
FT   STRAND       62     64       {ECO:0000244|PDB:5JBQ}.
FT   STRAND       68     71       {ECO:0000244|PDB:4PC3}.
FT   STRAND       76     81       {ECO:0000244|PDB:4PC3}.
FT   HELIX        85     94       {ECO:0000244|PDB:4PC3}.
FT   STRAND       95     97       {ECO:0000244|PDB:3U6B}.
FT   STRAND      100    107       {ECO:0000244|PDB:4PC3}.
FT   TURN        108    110       {ECO:0000244|PDB:4PC3}.
FT   HELIX       116    125       {ECO:0000244|PDB:4PC3}.
FT   STRAND      131    136       {ECO:0000244|PDB:4PC3}.
FT   HELIX       138    140       {ECO:0000244|PDB:4PC3}.
FT   HELIX       144    160       {ECO:0000244|PDB:4PC3}.
FT   TURN        165    167       {ECO:0000244|PDB:4PC3}.
FT   STRAND      170    172       {ECO:0000244|PDB:4PC3}.
FT   HELIX       175    179       {ECO:0000244|PDB:4PC3}.
FT   HELIX       183    199       {ECO:0000244|PDB:4PC3}.
FT   HELIX       206    208       {ECO:0000244|PDB:4PC3}.
FT   STRAND      212    214       {ECO:0000244|PDB:4PC3}.
FT   STRAND      217    221       {ECO:0000244|PDB:4PC3}.
FT   TURN        222    224       {ECO:0000244|PDB:4PC3}.
FT   STRAND      225    231       {ECO:0000244|PDB:4PC3}.
FT   STRAND      234    238       {ECO:0000244|PDB:4PC3}.
FT   STRAND      242    249       {ECO:0000244|PDB:4PC3}.
FT   STRAND      252    261       {ECO:0000244|PDB:4PC3}.
FT   STRAND      264    270       {ECO:0000244|PDB:4PC3}.
FT   STRAND      274    281       {ECO:0000244|PDB:4PC3}.
FT   HELIX       284    286       {ECO:0000244|PDB:4PC3}.
FT   STRAND      292    294       {ECO:0000244|PDB:4PC3}.
FT   TURN        296    298       {ECO:0000244|PDB:4Q7J}.
FT   STRAND      301    311       {ECO:0000244|PDB:4PC3}.
FT   TURN        314    317       {ECO:0000244|PDB:4PC3}.
FT   STRAND      323    327       {ECO:0000244|PDB:3U6K}.
FT   STRAND      330    333       {ECO:0000244|PDB:4PC3}.
FT   STRAND      336    343       {ECO:0000244|PDB:4PC3}.
FT   STRAND      356    368       {ECO:0000244|PDB:4PC3}.
FT   STRAND      374    379       {ECO:0000244|PDB:4PC3}.
FT   STRAND      382    394       {ECO:0000244|PDB:4PC3}.
SQ   SEQUENCE   394 AA;  43284 MW;  731A60255F43358F CRC64;
     MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI DNAPEEKARG
     ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
     LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE
     GDAEWEAKIL ELAGFLDSYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG
     EEVEIVGIKE TQKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGTIK
     PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV
     VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLG
//
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