ID EFTU2_ECOLI Reviewed; 394 AA. AC P0CE48; O68929; P02990; P0A6N1; Q2M704; Q2M8R6; Q8X4S9; Q8XED3; DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 23-MAR-2010, sequence version 1. DT 24-JUL-2024, entry version 105. DE RecName: Full=Elongation factor Tu 2 {ECO:0000255|HAMAP-Rule:MF_00118}; DE Short=EF-Tu 2 {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=tufB {ECO:0000255|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=b3980, JW3943; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7011904; DOI=10.1016/0378-1119(80)90013-x; RA An G., Friesen J.D.; RT "The nucleotide sequence of tufB and four nearby tRNA structural genes of RT Escherichia coli."; RL Gene 12:33-39(1980). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=8265357; DOI=10.1093/nar/21.23.5408; RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.; RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region RT from 89.2 to 92.8 minutes."; RL Nucleic Acids Res. 21:5408-5417(1993). 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 2-394, 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 [6] 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21. RX PubMed=7035813; DOI=10.1007/bf00270131; RA Miyajima A., Shibuya M., Kuchino Y., Kaziro Y.; RT "Transcription of the E. coli tufB gene: cotranscription with four tRNA RT genes and inhibition by guanosine-5'-diphosphate-3'-diphosphate."; RL Mol. Gen. Genet. 183:13-19(1981). 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 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 [11] RP FUNCTION IN VIRAL RNA REPLICATION, AND SUBUNIT. 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 [12] 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 [13] RP METHYLATION AT LYS-57. 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 [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 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 [16] 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 [17] 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 [18] 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 [19] 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 [20] 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 [21] RP CONSTRUCT TO PRODUCE QBETA VIRAL CATALYTIC CORE. RC STRAIN=A/lambda; RX PubMed=16781472; DOI=10.1263/jbb.101.421; RA Kita H., Cho J., Matsuura T., Nakaishi T., Taniguchi I., Ichikawa T., RA Shima Y., Urabe I., Yomo T.; RT "Functional Qbeta replicase genetically fusing essential subunits EF-Ts and RT EF-Tu with beta-subunit."; RL J. Biosci. Bioeng. 101:421-426(2006). RN [22] 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 [23] 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 [24] RP SUCCINYLATION AT LYS-38; LYS-177; LYS-249; LYS-253; LYS-295 AND LYS-314. RC STRAIN=K12; RX PubMed=21151122; DOI=10.1038/nchembio.495; RA Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.; RT "Identification of lysine succinylation as a new post-translational RT modification."; RL Nat. Chem. Biol. 7:58-63(2011). RN [25] 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 [26] 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 [27] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-394 OF A TRYPSIN-MODIFIED RP EF-TU-GDP. RX PubMed=3898365; DOI=10.1126/science.3898365; RA Jurnak F.; RT "Structure of the GDP domain of EF-Tu and location of the amino acids RT homologous to ras oncogene proteins."; RL Science 230:32-36(1985). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=1542116; DOI=10.1016/0022-2836(92)90986-t; RA Kjeldgaard M., Nyborg J.; RT "Refined structure of elongation factor EF-Tu from Escherichia coli."; RL J. Mol. Biol. 223:721-742(1992). RN [29] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 10-394 IN COMPLEX WITH EF-TS. RX PubMed=8596629; DOI=10.1038/379511a0; RA Kawashima T., Berthet-Colominas C., Wulff M., Cusack S., Leberman R.; RT "The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5-A RT resolution."; RL Nature 379:511-518(1996). RN [30] RP ERRATUM OF PUBMED:8596629. RA Kawashima T., Berthet-Colominas C., Wulff M., Cusack S., Leberman R.; RL Nature 381:172-172(1996). RN [31] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GDP AND ANTIBIOTIC RP GE2270A. RX PubMed=8939740; DOI=10.1016/s0969-2126(96)00123-2; RA Abel K., Yoder M.D., Hilgenfeld R., Jurnak F.; RT "An alpha to beta conformational switch in EF-Tu."; RL Structure 4:1153-1159(1996). RN [32] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS). 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 [33] RP STRUCTURE BY ELECTRON MICROSCOPY (16.8 ANGSTROMS) OF 2-393 IN THE 70S RP RIBOSOME. RX PubMed=12093756; DOI=10.1093/emboj/cdf326; RA Valle M., Sengupta J., Swami N.K., Grassucci R.A., Burkhardt N., RA Nierhaus K.H., Agrawal R.K., Frank J.; RT "Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation RT process."; RL EMBO J. 21:3557-3567(2002). RN [34] RP X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 3-394, AND STRUCTURE BY ELECTRON RP MICROSCOPY (10.0 ANGSTROMS) OF 2-393 IN COMPLEX WITH THE 70S RIBOSOME. RX PubMed=14566331; DOI=10.1038/nsb1003; RA Valle M., Zavialov A., Li W., Stagg S.M., Sengupta J., Nielsen R.C., RA Nissen P., Harvey S.C., Ehrenberg M., Frank J.; RT "Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron RT microscopy."; RL Nat. Struct. Biol. 10:899-906(2003). RN [35] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-394 OF EF-TU-GUANYLYL RP IMINODIPHOSPHATE (GDPNP) ENACYLOXIN IIA COMPLEX. RX PubMed=16257965; DOI=10.1074/jbc.m505951200; RA Parmeggiani A., Krab I.M., Watanabe T., Nielsen R.C., Dahlberg C., RA Nyborg J., Nissen P.; RT "Enacyloxin IIa pinpoints a binding pocket of elongation factor Tu for RT development of novel antibiotics."; RL J. Biol. Chem. 281:2893-2900(2006). RN [36] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN QBETA VIRUS RNA POLYMERASE RP CATALYTIC CORE, FUNCTION IN VIRAL RNA REPLICATION, AND SUBUNIT. RX PubMed=20534494; DOI=10.1073/pnas.1003015107; RA Kidmose R.T., Vasiliev N.N., Chetverin A.B., Andersen G.R., Knudsen C.R.; RT "Structure of the Qbeta replicase, an RNA-dependent RNA polymerase RT consisting of viral and host proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 107:10884-10889(2010). RN [37] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN QBETA VIRUS RNA POLYMERASE RP CATALYTIC CORE, FUNCTION IN VIRAL RNA REPLICATION, SUBUNIT, AND MUTAGENESIS RP OF PHE-262 AND 262-PHE-ARG-263. RX PubMed=20798060; DOI=10.1073/pnas.1006559107; RA Takeshita D., Tomita K.; RT "Assembly of Q{beta} viral RNA polymerase with host translational RT elongation factors EF-Tu and -Ts."; RL Proc. Natl. Acad. Sci. U.S.A. 107:15733-15738(2010). RN [38] RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) IN QBETA VIRUS RNA POLYMERASE RP CATALYTIC CORE, FUNCTION IN VIRAL RNA REPLICATION, SUBUNIT, AND MUTAGENESIS RP OF ARG-289; ARG-378 AND ARG-382. RX PubMed=22245970; DOI=10.1038/nsmb.2204; RA Takeshita D., Tomita K.; RT "Molecular basis for RNA polymerization by Qbeta replicase."; RL Nat. Struct. Mol. Biol. 19:229-237(2012). RN [39] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN QBETA VIRUS RNA POLYMERASE RP CATALYTIC CORE, FUNCTION IN VIRAL RNA REPLICATION, AND SUBUNIT. RX PubMed=22884418; DOI=10.1016/j.str.2012.07.004; RA Takeshita D., Yamashita S., Tomita K.; RT "Mechanism for template-independent terminal adenylation activity of Qbeta RT replicase."; RL Structure 20:1661-1669(2012). RN [40] RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN QBETA VIRUS RNA POLYMERASE, RP FUNCTION IN VIRAL RNA REPLICATION, AND SUBUNIT. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=25122749; DOI=10.1093/nar/gku745; RA Takeshita D., Yamashita S., Tomita K.; RT "Molecular insights into replication initiation by Qbeta replicase using RT ribosomal protein S1."; RL Nucleic Acids Res. 42:10809-10822(2014). 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 D-aminoacyl-tRNA CC deacylase (dtd) (By similarity). {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 (PubMed:22245970). With the beta subunit helps form the exit CC tunnel for template RNA. The GTPase activity of this subunit is not CC required for viral RNA replication (PubMed:20798060). CC {ECO:0000269|PubMed:20534494, ECO:0000269|PubMed:20798060, CC ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418, CC ECO:0000269|PubMed:25122749, ECO:0000269|PubMed:816798}. CC -!- SUBUNIT: Monomer. Heterotetramer composed of two EF-Ts.EF-Tu dimer CC complexes (PubMed:8596629). {ECO:0000255|HAMAP-Rule:MF_00118, CC ECO:0000269|PubMed:8596629, ECO:0000269|PubMed:8939740}. 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:20534494, ECO:0000269|PubMed:20798060, CC ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418, CC ECO:0000269|PubMed:25122749, ECO:0000269|PubMed:816798}. CC -!- INTERACTION: CC P0CE48; P0A6P1: tsf; NbExp=3; IntAct=EBI-9010251, EBI-301164; 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: In order to produce high amounts of bacteriophage Qbeta CC RNA polymerase catalytic core, a fusion protein consisting of tsf-tufB- CC replicase with a cleavable linker between tufB and the viral replicase CC subunit is frequently used. {ECO:0000269|PubMed:16781472, CC ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970, CC ECO:0000269|PubMed:22884418, ECO:0000269|PubMed:25122749}. CC -!- MISCELLANEOUS: Present with about 70,000 molecules/cell. CC {ECO:0000305|PubMed:775340}. CC -!- MISCELLANEOUS: The antibiotic kirromycin inhibits protein biosynthesis CC by inhibiting the release of EF-Tu from the ribosome. TufA resistance CC to kirromycin is conferred by mutations to Gln-125, Gly-317 and Ala- CC 376. This has not been formally proven for tufB, but is certainly CC correct. {ECO:0000305}. CC -!- MISCELLANEOUS: The antibiotic pulvomycin inhibits protein biosynthesis CC by disrupting the allosteric control mechanism of EF-Tu TufA resistance CC to pulvomycin is conferred by Arg-231, Arg-334 and Thr-335. This has CC not been formally proven for tufB, but is certainly correct. CC {ECO:0000305}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X57091; CAA40370.1; -; Genomic_DNA. DR EMBL; J01717; AAA24669.1; -; Genomic_DNA. DR EMBL; U00006; AAC43078.1; -; Genomic_DNA. DR EMBL; U00096; AAC76954.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77340.1; -; Genomic_DNA. DR PIR; A91478; EFECT. DR RefSeq; NP_418407.1; NC_000913.3. DR RefSeq; WP_000031784.1; NZ_SSYX01000041.1. DR PDB; 1DG1; X-ray; 2.50 A; G/H=1-394. DR PDB; 1EFM; X-ray; 2.70 A; A=2-394. DR PDB; 1EFU; X-ray; 2.50 A; A/C=10-394. DR PDB; 1LS2; EM; 16.80 A; A=2-394. DR PDB; 1OB2; X-ray; 3.35 A; A=3-394. DR PDB; 1QZD; EM; -; A=2-394. DR PDB; 2BVN; X-ray; 2.30 A; A/B=2-394. DR PDB; 3AGP; X-ray; 2.80 A; A=1-394. DR PDB; 3AGQ; X-ray; 3.22 A; A=1-394. DR PDB; 3AVT; X-ray; 2.61 A; A=1-394. DR PDB; 3AVU; X-ray; 2.91 A; A=1-394. DR PDB; 3AVV; X-ray; 3.12 A; A=1-394. DR PDB; 3AVW; X-ray; 2.60 A; A=1-394. DR PDB; 3AVX; X-ray; 2.41 A; A=1-394. DR PDB; 3AVY; X-ray; 2.62 A; A=1-394. DR PDB; 3MMP; X-ray; 2.50 A; A/C=1-394. DR PDB; 3VNU; X-ray; 3.20 A; A=1-394. DR PDB; 3VNV; X-ray; 2.60 A; A=1-394. DR PDB; 4FWT; X-ray; 3.20 A; A=1-394. DR PDB; 4R71; X-ray; 3.21 A; A/C=1-394. DR PDB; 4V6K; EM; 8.25 A; BC=2-394. DR PDB; 4V6L; EM; 13.20 A; AC=2-394. DR PDB; 5AFI; EM; 2.90 A; z=2-394. DR PDB; 5I4R; X-ray; 3.30 A; C/G=1-45. DR PDB; 5WDT; EM; 3.00 A; z=2-394. DR PDB; 5WE4; EM; 3.10 A; z=2-394. DR PDB; 5WE6; EM; 3.40 A; z=2-394. DR PDB; 5WF0; EM; 3.60 A; z=2-394. DR PDB; 5WFK; EM; 3.40 A; z=2-394. DR PDB; 5WFS; EM; 3.00 A; z=2-394. DR PDB; 6EZE; X-ray; 2.47 A; A/B=1-394. DR PDB; 7ABZ; EM; 3.21 A; 6=1-394. DR PDB; 7VMC; X-ray; 3.41 A; A=1-394. DR PDBsum; 1DG1; -. DR PDBsum; 1EFM; -. DR PDBsum; 1EFU; -. DR PDBsum; 1LS2; -. DR PDBsum; 1OB2; -. DR PDBsum; 1QZD; -. DR PDBsum; 2BVN; -. DR PDBsum; 3AGP; -. DR PDBsum; 3AGQ; -. DR PDBsum; 3AVT; -. DR PDBsum; 3AVU; -. DR PDBsum; 3AVV; -. DR PDBsum; 3AVW; -. DR PDBsum; 3AVX; -. DR PDBsum; 3AVY; -. DR PDBsum; 3MMP; -. DR PDBsum; 3VNU; -. DR PDBsum; 3VNV; -. DR PDBsum; 4FWT; -. DR PDBsum; 4R71; -. DR PDBsum; 4V6K; -. DR PDBsum; 4V6L; -. DR PDBsum; 5AFI; -. DR PDBsum; 5I4R; -. DR PDBsum; 5WDT; -. DR PDBsum; 5WE4; -. DR PDBsum; 5WE6; -. DR PDBsum; 5WF0; -. DR PDBsum; 5WFK; -. DR PDBsum; 5WFS; -. DR PDBsum; 6EZE; -. DR PDBsum; 7ABZ; -. DR PDBsum; 7VMC; -. DR AlphaFoldDB; P0CE48; -. DR EMDB; EMD-1055; -. DR EMDB; EMD-11710; -. DR EMDB; EMD-1849; -. DR EMDB; EMD-1850; -. DR EMDB; EMD-2847; -. DR EMDB; EMD-8813; -. DR EMDB; EMD-8814; -. DR EMDB; EMD-8815; -. DR EMDB; EMD-8828; -. DR SMR; P0CE48; -. DR BioGRID; 4261400; 35. DR BioGRID; 852776; 3. DR ComplexPortal; CPX-2853; Elongation Factor TU-TS, tufB variant. DR DIP; DIP-60620N; -. DR IntAct; P0CE48; 160. DR STRING; 511145.b3980; -. DR iPTMnet; P0CE48; -. DR jPOST; P0CE48; -. DR PaxDb; 511145-b3980; -. DR EnsemblBacteria; AAC76954; AAC76954; b3980. DR GeneID; 86948189; -. DR GeneID; 948482; -. DR KEGG; ecj:JW3943; -. DR KEGG; eco:b3980; -. DR PATRIC; fig|1411691.4.peg.2732; -. DR EchoBASE; EB1030; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_2_6; -. DR InParanoid; P0CE48; -. DR OMA; FHNNYRP; -. DR OrthoDB; 9803139at2; -. DR PhylomeDB; P0CE48; -. DR BioCyc; EcoCyc:EG11037-MONOMER; -. DR BRENDA; 3.6.5.3; 2026. DR EvolutionaryTrace; P0CE48; -. DR PRO; PR:P0CE48; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 CDD; cd03707; EFTU_III; 1. DR DisProt; DP01965; -. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 2. DR HAMAP; MF_00118_B; EF_Tu_B; 1. DR InterPro; IPR041709; EF-Tu_GTP-bd. DR InterPro; IPR050055; EF-Tu_GTPase. 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 NCBIfam; TIGR00485; EF-Tu; 1. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1. DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1. 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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50447; Translation proteins; 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 2" FT /id="PRO_0000392289" 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 38 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" 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 177 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 249 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 253 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 295 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 314 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:18723842" FT MOD_RES 314 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 383 FT /note="Phosphothreonine" FT /evidence="ECO:0000305|PubMed:19150849, FT ECO:0000305|PubMed:24141193, ECO:0000305|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 115 FT /note="Q->A: Weaker binding for GDP and for EF-Ts." FT /evidence="ECO:0000269|PubMed:9468511" 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 262..263 FT /note="Missing: Still associates with EF-Ts, no longer FT forms the Qbeta viral RNA polymerase complex." FT /evidence="ECO:0000269|PubMed:20798060" FT MUTAGEN 262 FT /note="F->A: Still associates with EF-Ts, very little Qbeta FT viral RNA polymerase complex forms." FT /evidence="ECO:0000269|PubMed:20798060" FT MUTAGEN 289 FT /note="R->A: 50% loss of Qbeta viral RNA polymerase FT activity." FT /evidence="ECO:0000269|PubMed:22245970" 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 378 FT /note="R->A: 60% loss of Qbeta viral RNA polymerase FT elongation activity." FT /evidence="ECO:0000269|PubMed:22245970" FT MUTAGEN 382 FT /note="R->A: 25% loss of Qbeta viral RNA polymerase FT elongation activity." FT /evidence="ECO:0000269|PubMed:22245970" FT MUTAGEN 383 FT /note="T->V: No longer phosphorylated by phage protein FT doc." FT /evidence="ECO:0000269|PubMed:24141193" FT HELIX 3..7 FT /evidence="ECO:0007829|PDB:4R71" FT STRAND 12..18 FT /evidence="ECO:0007829|PDB:2BVN" FT HELIX 21..23 FT /evidence="ECO:0007829|PDB:4R71" FT HELIX 25..40 FT /evidence="ECO:0007829|PDB:2BVN" FT HELIX 47..51 FT /evidence="ECO:0007829|PDB:6EZE" FT STRAND 55..60 FT /evidence="ECO:0007829|PDB:6EZE" FT HELIX 61..63 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 67..71 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 76..81 FT /evidence="ECO:0007829|PDB:2BVN" FT HELIX 86..88 FT /evidence="ECO:0007829|PDB:2BVN" FT HELIX 89..96 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 102..107 FT /evidence="ECO:0007829|PDB:2BVN" FT TURN 108..110 FT /evidence="ECO:0007829|PDB:2BVN" FT HELIX 114..126 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 131..136 FT /evidence="ECO:0007829|PDB:2BVN" FT HELIX 138..140 FT /evidence="ECO:0007829|PDB:2BVN" FT HELIX 144..160 FT /evidence="ECO:0007829|PDB:2BVN" FT TURN 165..167 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:2BVN" FT HELIX 175..179 FT /evidence="ECO:0007829|PDB:2BVN" FT HELIX 183..199 FT /evidence="ECO:0007829|PDB:2BVN" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:6EZE" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 218..221 FT /evidence="ECO:0007829|PDB:2BVN" FT TURN 222..224 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 225..231 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 234..238 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 242..249 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 252..261 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 264..270 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 274..281 FT /evidence="ECO:0007829|PDB:2BVN" FT HELIX 284..286 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 292..295 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 300..311 FT /evidence="ECO:0007829|PDB:2BVN" FT HELIX 314..316 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 330..333 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 336..343 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 356..369 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 374..379 FT /evidence="ECO:0007829|PDB:2BVN" FT STRAND 382..392 FT /evidence="ECO:0007829|PDB:2BVN" SQ SEQUENCE 394 AA; 43314 MW; 6EDA60255F43358F 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 KVLS //