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 03-AUG-2022, entry version 94.
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 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., Mau B.,
RA 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 MG1655
RT 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 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., Sottrup-Jensen L.,
RA Gausing K., Clark B.F.C.;
RT "The complete amino-acid sequence of elongation factor Tu from Escherichia
RT coli.";
RL Eur. J. Biochem. 108:507-526(1980).
RN [5]
RP PROTEIN SEQUENCE OF 2-394, ACETYLATION AT SER-2, AND METHYLATION AT LYS-57.
RX PubMed=7021545; DOI=10.1016/s0021-9258(18)43394-7;
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. The
RT 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; DOI=10.1016/s0021-9258(19)39212-9;
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 RESPONSE
RP 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 deprivation in
RT 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 in the
RT 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. coli.";
RL Nature 261:23-26(1976).
RN [12]
RP FUNCTION IN VIRAL RNA REPLICATION (MICROBIAL INFECTION), AND SUBUNIT
RP (MICROBIAL INFECTION).
RX PubMed=816798; DOI=10.1016/s0021-9258(17)33551-2;
RA Carmichael G.G., Landers T.A., Weber K.;
RT "Immunochemical analysis of the functions of the subunits of phage Qbeta
RT 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 383-391.
RX PubMed=8416965; DOI=10.1016/s0021-9258(18)54193-4;
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; DOI=10.1016/s0021-9258(18)45170-8;
RA Hwang Y.-W., Miller D.L.;
RT "A mutation that alters the nucleotide specificity of elongation factor Tu,
RT 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 ribosomes.";
RL Eur. J. Biochem. 185:341-346(1989).
RN [16]
RP MUTAGENESIS OF LYS-137.
RX PubMed=2498311; DOI=10.1016/s0021-9258(18)83183-0;
RA Hwang Y.-W., Sanchez A., Miller D.L.;
RT "Mutagenesis of bacterial elongation factor Tu at lysine 136. A conserved
RT 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; DOI=10.1002/j.1460-2075.1996.tb01066.x;
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., 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 MASS
RP 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; DOI=10.1002/j.1460-2075.1994.tb06815.x;
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; DOI=10.1002/j.1460-2075.1994.tb06840.x;
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., 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., Loris R.,
RA 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 FUNCTION IN CDI (MICROBIAL INFECTION), SUBUNIT, AND INTERACTION WITH
RP CDIA-CT-EC869 AND CDII-EC869 (MICROBIAL INFECTION).
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=28223500; DOI=10.1073/pnas.1619273114;
RA Jones A.M., Garza-Sanchez F., So J., Hayes C.S., Low D.A.;
RT "Activation of contact-dependent antibacterial tRNase toxins by translation
RT elongation factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E1951-E1957(2017).
RN [29] {ECO:0007744|PDB:1ETU}
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 elongation
RT factor Tu from E. coli as studied by X-ray crystallography.";
RL EMBO J. 4:2385-2388(1985).
RN [30] {ECO:0007744|PDB:1EFC}
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 coli
RT in GDP conformation at 2.05-A resolution.";
RL J. Mol. Biol. 285:1245-1256(1999).
RN [31] {ECO:0007744|PDB:1D8T}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 2-393 IN COMPLEX WITH ANTIBIOTIC
RP 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 of EF-
RT Tu.";
RL Biochemistry 39:37-45(2000).
RN [32] {ECO:0007744|PDB:2FX3}
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 a
RT twinned data set.";
RL Acta Crystallogr. D 62:433-438(2006).
RN [33] {ECO:0007744|PDB:2HCJ, ECO:0007744|PDB:2HDN}
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 9-44 AND 60-393 IN COMPLEX WITH
RP 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 site
RT of elongation factor Tu.";
RL Acta Crystallogr. D 62:1392-1400(2006).
RN [34] {ECO:0007744|PDB:5I4Q, ECO:0007744|PDB:5I4R}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 178-394 IN COMPLEX WITH GDP;
RP CDIA-CT-NC101 AND CDII-NC101, AND FUNCTION IN CDI (MICROBIAL INFECTION).
RX PubMed=28973472; DOI=10.1093/nar/gkx700;
RA Michalska K., Gucinski G.C., Garza-Sanchez F., Johnson P.M., Stols L.M.,
RA Eschenfeldt W.H., Babnigg G., Low D.A., Goulding C.W., Joachimiak A.,
RA Hayes C.S.;
RT "Structure of a novel antibacterial toxin that exploits elongation factor
RT Tu to cleave specific transfer RNAs.";
RL Nucleic Acids Res. 45:10306-10320(2017).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- FUNCTION: May play an important regulatory role in cell growth and in
CC the bacterial response to nutrient deprivation.
CC -!- FUNCTION: Plays a stimulatory role in trans-translation; binds tmRNA.
CC {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 -!- FUNCTION: (Microbial infection) Upon infection by bacteriophage Qbeta,
CC part of the viral RNA-dependent RNA polymerase complex. With EF-Ts may
CC provide a stabilizing scaffold for the beta (catalytic) subunit. Helps
CC separate the double-stranded RNA of the template and growing RNA during
CC elongation. With the beta subunit helps form the exit tunnel for
CC template RNA. {ECO:0000269|PubMed:816798, ECO:0000305}.
CC -!- FUNCTION: (Microbial infection) Required for the tRNase activity of
CC CdiA-CT from E.coli strain EC869; the toxic CT module is thought to
CC cleave tRNA in the context of translationally active GTP EF-Tu-aa-tRNA
CC complexes. GTP is required for tRNase activity but is not hydrolyzed.
CC CdiA-CT is the toxic component of a toxin-immunity protein module,
CC which functions as a cellular contact-dependent growth inhibition (CDI)
CC system. CDI modules allow bacteria to communicate with and inhibit the
CC growth of closely related neighboring bacteria in a contact-dependent
CC fashion (PubMed:28223500). EF-Tu interacts with at least 2 different
CC toxic CT domains, the 2 toxins are different and degrade tRNA at
CC different positions (PubMed:28973472, PubMed:28223500).
CC {ECO:0000269|PubMed:28223500, ECO:0000269|PubMed:28973472}.
CC -!- FUNCTION: (Microbial infection) Required for the tRNase activity of
CC CdiA-CT from E.coli strain NC101; the toxic CT module is thought to
CC cleave tRNA in the context of translationally active GTP EF-Tu-aa-tRNA
CC complexes. The toxin may remodel the EF-Tu-aa-tRNA complex to displace
CC the 3'-end of the aa-tRNA so it can enter the toxin active site and be
CC cleaved. GTP is required for tRNase activity but is not hydrolyzed.
CC CdiA-CT is the toxic component of a toxin-immunity protein module,
CC which functions as a cellular contact-dependent growth inhibition (CDI)
CC system. CDI modules allow bacteria to communicate with and inhibit the
CC growth of closely related neighboring bacteria in a contact-dependent
CC fashion (PubMed:28223500). EF-Tu interacts with at least 2 different
CC toxic CT domains, the 2 toxins are different and degrade tRNA at
CC different positions (PubMed:28973472, PubMed:28223500).
CC {ECO:0000269|PubMed:28223500, ECO:0000269|PubMed:28973472}.
CC -!- SUBUNIT: Monomer. Heterotetramer composed of two EF-Ts.EF-Tu dimer
CC complexes (By similarity). {ECO:0000250|UniProtKB:P0CE48,
CC ECO:0000255|HAMAP-Rule:MF_00118, ECO:0000269|PubMed:10625477,
CC ECO:0000269|PubMed:17057344, ECO:0000269|PubMed:9918724, ECO:0000305}.
CC -!- SUBUNIT: (Microbial infection) Upon 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), host
CC ribosomal protein S1 and EF-Ts (PubMed:816798).
CC {ECO:0000269|PubMed:816798}.
CC -!- SUBUNIT: (Microbial infection) Forms a contact-dependent growth
CC inhibition complex of EF-Tu, CdiA-CT-EC869 and CdiI-EC869 as well as a
CC GTP, EF-Tu, CdiA-CT-EC869 complex. {ECO:0000269|PubMed:28223500}.
CC -!- SUBUNIT: (Microbial infection) Forms a contact-dependent growth
CC inhibition complex of CdiA-CT-NC101, CdiI-NC101 and EF-Tu; the complex
CC is a dimer of heterotrimers. {ECO:0000269|PubMed:28973472}.
CC -!- INTERACTION:
CC P0CE47; P61517: can; NbExp=2; IntAct=EBI-301077, EBI-562106;
CC P0CE47; P76251: dmlA; NbExp=2; IntAct=EBI-301077, EBI-560661;
CC P0CE47; P15038: helD; NbExp=3; IntAct=EBI-301077, EBI-551473;
CC P0CE47; P0A6Y5: hslO; NbExp=3; IntAct=EBI-301077, EBI-562857;
CC P0CE47; P00956: ileS; NbExp=2; IntAct=EBI-301077, EBI-552928;
CC P0CE47; P04951: kdsB; NbExp=2; IntAct=EBI-301077, EBI-544810;
CC P0CE47; P10441: lpxB; NbExp=3; IntAct=EBI-301077, EBI-553692;
CC P0CE47; P22634: murI; NbExp=2; IntAct=EBI-301077, EBI-554903;
CC P0CE47; P23909: mutS; NbExp=2; IntAct=EBI-301077, EBI-554920;
CC P0CE47; P33590: nikA; NbExp=2; IntAct=EBI-301077, EBI-555182;
CC P0CE47; P0A6Z6: nikR; NbExp=3; IntAct=EBI-301077, EBI-562488;
CC P0CE47; P77756: queC; NbExp=3; IntAct=EBI-301077, EBI-560024;
CC P0CE47; P0AG30: rho; NbExp=2; IntAct=EBI-301077, EBI-545468;
CC P0CE47; P0ADX9: rsmD; NbExp=2; IntAct=EBI-301077, EBI-561207;
CC P0CE47; P0A6P1: tsf; NbExp=12; IntAct=EBI-301077, EBI-301164;
CC P0CE47; P0A8J4: ybeD; NbExp=3; IntAct=EBI-301077, EBI-370708;
CC P0CE47; P63389: yheS; NbExp=3; IntAct=EBI-301077, EBI-561198;
CC P0CE47; P39408: yjjV; NbExp=2; IntAct=EBI-301077, EBI-561387;
CC P0CE47; Q06259: doc; Xeno; NbExp=5; IntAct=EBI-301077, EBI-2908816;
CC P0CE47; P14647; Xeno; NbExp=2; IntAct=EBI-301077, EBI-9010000;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral
CC membrane protein. Note=Between 50-80% of the protein is associated with
CC the cell inner membrane. Localization to the membrane has been
CC suggested to follow nutrient stress.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Methylated in vivo on Lys-57 in response to nutrient starvation.
CC {ECO:0000269|PubMed:2022614, ECO:0000269|PubMed:389663,
CC ECO:0000269|PubMed:6997043, 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), this
CC has since been reported not to occur in vivo (PubMed:24095282).
CC {ECO:0000269|PubMed:19150849, ECO:0000269|PubMed:24095282,
CC ECO:0000269|PubMed:24141193, 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 biosynthesis
CC by inhibiting the release of EF-Tu from the ribosome.
CC {ECO:0000269|PubMed:7525272}.
CC -!- MISCELLANEOUS: The antibiotic pulvomycin inhibits protein biosynthesis
CC by disrupting the allosteric control mechanism of EF-Tu.
CC {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 no
CC longer merged. However, many papers are found in both entries as it is
CC not always possible to determine for each paper which of EF-Tu 1 or EF-
CC Tu 2 was being worked upon. {ECO:0000305}.
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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_SSYX01000005.1.
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 AlphaFoldDB; P0CE47; -.
DR SMR; P0CE47; -.
DR BioGRID; 4259390; 79.
DR BioGRID; 852150; 1.
DR ComplexPortal; CPX-6035; Elongation Factor TU-TS, tufA variant.
DR DIP; DIP-6159N; -.
DR IntAct; P0CE47; 211.
DR STRING; 511145.b3339; -.
DR CarbonylDB; P0CE47; -.
DR iPTMnet; P0CE47; -.
DR jPOST; P0CE47; -.
DR PaxDb; P0CE47; -.
DR PRIDE; P0CE47; -.
DR EnsemblBacteria; AAC76364; AAC76364; b3339.
DR EnsemblBacteria; BAE77952; BAE77952; BAE77952.
DR GeneID; 66672781; -.
DR GeneID; 947838; -.
DR KEGG; ecj:JW3301; -.
DR KEGG; eco:b3339; -.
DR PATRIC; fig|1411691.4.peg.3392; -.
DR EchoBASE; EB1029; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_2_6; -.
DR InParanoid; P0CE47; -.
DR OMA; ERPHCNV; -.
DR PhylomeDB; P0CE47; -.
DR BioCyc; EcoCyc:EG11036-MON; -.
DR BRENDA; 3.6.5.3; 2026.
DR EvolutionaryTrace; P0CE47; -.
DR PRO; PR:P0CE47; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd01884; EF_Tu; 1.
DR CDD; cd03697; EFTU_II; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_B; EF_Tu_B; 1.
DR InterPro; IPR041709; EF-Tu_GTP-bd.
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; T_Tr_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; Cytoplasm; Direct protein sequencing; Elongation factor;
KW GTP-binding; Membrane; Methylation; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6997043,
FT ECO:0000269|PubMed:7021545"
FT CHAIN 2..394
FT /note="Elongation factor Tu 1"
FT /id="PRO_0000091320"
FT DOMAIN 10..204
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 60..64
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 81..84
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 136..139
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 174..176
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:6997043,
FT ECO:0000269|PubMed:7021545"
FT MOD_RES 57
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2022614,
FT ECO:0000269|PubMed:389663, ECO:0000269|PubMed:6997043,
FT ECO:0000269|PubMed:7021545"
FT MOD_RES 57
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2022614,
FT ECO:0000269|PubMed:389663, ECO:0000269|PubMed:6997043,
FT ECO:0000269|PubMed:7021545"
FT MOD_RES 314
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 383
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19150849,
FT ECO:0000269|PubMed:24141193, ECO:0000269|PubMed:8416965"
FT MUTAGEN 20
FT /note="H->A: No change in binding GDP and 3-fold reduction
FT in binding EF-Ts."
FT /evidence="ECO:0000269|PubMed:9468511"
FT MUTAGEN 21
FT /note="V->G: Lowers GTPase activity 5 to 10-fold."
FT /evidence="ECO:0000269|PubMed:2684669"
FT MUTAGEN 83
FT /note="P->T: Loss of GTPase activity and creation of an
FT autophosphorylation site."
FT /evidence="ECO:0000269|PubMed:2157708"
FT MUTAGEN 115
FT /note="Q->A: Weaker binding for GDP and for EF-Ts."
FT /evidence="ECO:0000269|PubMed:9468511"
FT MUTAGEN 125
FT /note="Q->K: Kirromycin resistant."
FT /evidence="ECO:0000269|PubMed:2508560"
FT MUTAGEN 137
FT /note="K->R,Q,E,I: Reduces affinity for GDP."
FT /evidence="ECO:0000269|PubMed:2498311"
FT MUTAGEN 139
FT /note="D->N: Reduces affinity for GDP; increases affinity
FT for XDP."
FT /evidence="ECO:0000269|PubMed:3308869"
FT MUTAGEN 223
FT /note="G->D: Inhibits codon-induced conformational changes
FT leading to GTPase activation on the ribosome."
FT /evidence="ECO:0000269|PubMed:2508560"
FT MUTAGEN 231
FT /note="R->C: Pulvomycin resistant."
FT /evidence="ECO:0000269|PubMed:2508560"
FT MUTAGEN 317
FT /note="G->D: Kirromycin resistant."
FT /evidence="ECO:0000269|PubMed:2508560"
FT MUTAGEN 334
FT /note="R->C: Pulvomycin resistant."
FT /evidence="ECO:0000269|PubMed:2508560"
FT MUTAGEN 335
FT /note="T->A: Pulvomycin resistant."
FT /evidence="ECO:0000269|PubMed:2508560"
FT MUTAGEN 349
FT /note="E->A: No change in binding GDP but higher binding
FT constant for EF-Ts."
FT /evidence="ECO:0000269|PubMed:9468511"
FT MUTAGEN 376
FT /note="A->T,V: Kirromycin resistant."
FT /evidence="ECO:0000269|PubMed:2508560"
FT MUTAGEN 383
FT /note="T->V: No longer phosphorylated by phage protein doc,
FT has no effect on translation."
FT /evidence="ECO:0000269|PubMed:24141193"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:5JBQ"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:1ETU"
FT HELIX 25..40
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:5JBQ"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:5JBQ"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5JBQ"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3U6B"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:4PC3"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 144..160
FT /evidence="ECO:0007829|PDB:4PC3"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:4PC3"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 252..261
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 274..281
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:4PC3"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:4Q7J"
FT STRAND 301..311
FT /evidence="ECO:0007829|PDB:4PC3"
FT TURN 314..317
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:3U6K"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 356..368
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 382..394
FT /evidence="ECO:0007829|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
