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 28-MAR-2018, entry version 71. 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; Proteobacteria; 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 RT of 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., RA Daniels D.L.; RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the RT region 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., RA Mau B., 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 RT MG1655 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 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 [6] 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 [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 RT tRNA genes and inhibition by guanosine-5'-diphosphate-3'- RT 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 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 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 [11] 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 [12] 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 [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; 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 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 [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; 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., RA 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., 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 [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- RT Ts and 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 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 [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 RP 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., 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 [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. 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 RP ANTIBIOTIC 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 RT coli 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 RT accommodation process."; RL EMBO J. 21:3557-3567(2002). RN [34] RP X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 3-394, AND STRUCTURE BY RP ELECTRON MICROSCOPY (10.0 ANGSTROMS) OF 2-393 IN COMPLEX WITH THE 70S RP 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- RT electron 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., RA 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 RP MUTAGENESIS 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 RP MUTAGENESIS 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 RT Qbeta 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 RT using ribosomal protein S1."; RL Nucleic Acids Res. 42:10809-10822(2014). 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 (PubMed:22245970). With the beta subunit helps CC form the exit tunnel for template RNA. The GTPase activity of this CC subunit is not required for viral RNA replication CC (PubMed:20798060). {ECO:0000269|PubMed:20534494, CC ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970, CC ECO:0000269|PubMed:22884418, ECO:0000269|PubMed:25122749, CC ECO:0000269|PubMed:816798}. 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 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:20534494, CC ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970, CC ECO:0000269|PubMed:22884418, ECO:0000269|PubMed:25122749, CC ECO:0000269|PubMed:816798, ECO:0000269|PubMed:8596629, CC ECO:0000269|PubMed:8939740}. CC -!- INTERACTION: CC 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 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: In order to produce high amounts of bacteriophage CC Qbeta RNA polymerase catalytic core, a fusion protein consisting CC of tsf-tufB-replicase with a cleavable linker between tufB and the CC viral replicase subunit is frequently used. CC {ECO:0000269|PubMed:16781472, ECO:0000269|PubMed:20798060, CC ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418, CC 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 CC biosynthesis by inhibiting the release of EF-Tu from the ribosome. CC TufA resistance to kirromycin is conferred by mutations to Gln- CC 125, Gly-317 and Ala-376. This has not been formally proven for CC tufB, but is certainly correct. {ECO:0000305}. CC -!- MISCELLANEOUS: The antibiotic pulvomycin inhibits protein CC biosynthesis by disrupting the allosteric control mechanism of EF- CC Tu TufA resistance to pulvomycin is conferred by Arg-231, Arg-334 CC and Thr-335. This has not been formally proven for tufB, but is CC certainly correct. {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 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}. 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_LN832404.1. 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; 4V69; EM; 6.70 A; Z=2-394. 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 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; 4V69; -. DR PDBsum; 4V6K; -. DR PDBsum; 4V6L; -. DR PDBsum; 5AFI; -. DR ProteinModelPortal; P0CE48; -. DR SMR; P0CE48; -. DR BioGrid; 4261400; 34. DR BioGrid; 852776; 1. DR DIP; DIP-60620N; -. DR IntAct; P0CE48; 112. DR STRING; 316385.ECDH10B_4168; -. DR iPTMnet; P0CE48; -. DR PaxDb; P0CE48; -. DR PRIDE; P0CE48; -. DR EnsemblBacteria; AAC76954; AAC76954; b3980. DR EnsemblBacteria; BAE77340; BAE77340; BAE77340. DR GeneID; 948482; -. DR KEGG; ecj:JW3943; -. DR KEGG; eco:b3980; -. DR PATRIC; fig|1411691.4.peg.2732; -. DR EchoBASE; EB1030; -. DR EcoGene; EG11037; tufB. DR eggNOG; ENOG4105CGV; Bacteria. DR eggNOG; COG0050; LUCA. DR InParanoid; P0CE48; -. DR KO; K02358; -. DR OMA; YGHIDCP; -. 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:0005829; C:cytosol; IDA:EcoCyc. 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 2. FT /FTId=PRO_0000392289. 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 38 38 N6-succinyllysine. FT {ECO:0000269|PubMed:21151122}. 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 177 177 N6-succinyllysine. FT {ECO:0000269|PubMed:21151122}. FT MOD_RES 249 249 N6-succinyllysine. FT {ECO:0000269|PubMed:21151122}. FT MOD_RES 253 253 N6-succinyllysine. FT {ECO:0000269|PubMed:21151122}. FT MOD_RES 295 295 N6-succinyllysine. FT {ECO:0000269|PubMed:21151122}. FT MOD_RES 314 314 N6-acetyllysine; alternate. FT {ECO:0000269|PubMed:18723842}. FT MOD_RES 314 314 N6-succinyllysine; alternate. FT {ECO:0000269|PubMed:21151122}. FT MOD_RES 383 383 Phosphothreonine. FT {ECO:0000305|PubMed:19150849, FT ECO:0000305|PubMed:24141193, FT ECO:0000305|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 115 115 Q->A: Weaker binding for GDP and for EF- FT Ts. {ECO:0000269|PubMed:9468511}. 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 262 263 Missing: Still associates with EF-Ts, no FT longer forms the Qbeta viral RNA FT polymerase complex. FT {ECO:0000269|PubMed:20798060}. FT MUTAGEN 262 262 F->A: Still associates with EF-Ts, very FT little Qbeta viral RNA polymerase complex FT forms. {ECO:0000269|PubMed:20798060}. FT MUTAGEN 289 289 R->A: 50% loss of Qbeta viral RNA FT polymerase activity. FT {ECO:0000269|PubMed:22245970}. 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 378 378 R->A: 60% loss of Qbeta viral RNA FT polymerase elongation activity. FT {ECO:0000269|PubMed:22245970}. FT MUTAGEN 382 382 R->A: 25% loss of Qbeta viral RNA FT polymerase elongation activity. FT {ECO:0000269|PubMed:22245970}. FT MUTAGEN 383 383 T->V: No longer phosphorylated by phage FT protein doc. FT {ECO:0000269|PubMed:24141193}. FT HELIX 3 7 {ECO:0000244|PDB:4R71}. FT STRAND 12 18 {ECO:0000244|PDB:2BVN}. FT HELIX 21 23 {ECO:0000244|PDB:4R71}. FT HELIX 25 40 {ECO:0000244|PDB:2BVN}. FT HELIX 47 51 {ECO:0000244|PDB:1DG1}. FT STRAND 55 58 {ECO:0000244|PDB:1DG1}. FT HELIX 61 63 {ECO:0000244|PDB:2BVN}. FT STRAND 67 71 {ECO:0000244|PDB:2BVN}. FT STRAND 76 81 {ECO:0000244|PDB:2BVN}. FT HELIX 86 88 {ECO:0000244|PDB:2BVN}. FT HELIX 89 96 {ECO:0000244|PDB:2BVN}. FT STRAND 102 107 {ECO:0000244|PDB:2BVN}. FT TURN 108 110 {ECO:0000244|PDB:2BVN}. FT HELIX 114 126 {ECO:0000244|PDB:2BVN}. FT STRAND 131 136 {ECO:0000244|PDB:2BVN}. FT HELIX 138 140 {ECO:0000244|PDB:2BVN}. FT HELIX 144 160 {ECO:0000244|PDB:2BVN}. FT TURN 165 167 {ECO:0000244|PDB:2BVN}. FT STRAND 170 172 {ECO:0000244|PDB:2BVN}. FT HELIX 175 179 {ECO:0000244|PDB:2BVN}. FT HELIX 183 199 {ECO:0000244|PDB:2BVN}. FT HELIX 206 208 {ECO:0000244|PDB:1DG1}. FT STRAND 212 214 {ECO:0000244|PDB:2BVN}. FT STRAND 218 221 {ECO:0000244|PDB:2BVN}. FT TURN 222 224 {ECO:0000244|PDB:2BVN}. FT STRAND 225 231 {ECO:0000244|PDB:2BVN}. FT STRAND 234 238 {ECO:0000244|PDB:2BVN}. FT STRAND 242 249 {ECO:0000244|PDB:2BVN}. FT STRAND 252 261 {ECO:0000244|PDB:2BVN}. FT STRAND 264 270 {ECO:0000244|PDB:2BVN}. FT STRAND 274 281 {ECO:0000244|PDB:2BVN}. FT HELIX 284 286 {ECO:0000244|PDB:2BVN}. FT STRAND 292 295 {ECO:0000244|PDB:2BVN}. FT STRAND 300 311 {ECO:0000244|PDB:2BVN}. FT HELIX 314 316 {ECO:0000244|PDB:2BVN}. FT STRAND 330 333 {ECO:0000244|PDB:2BVN}. FT STRAND 336 343 {ECO:0000244|PDB:2BVN}. FT STRAND 356 369 {ECO:0000244|PDB:2BVN}. FT STRAND 374 379 {ECO:0000244|PDB:2BVN}. FT STRAND 382 392 {ECO:0000244|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 //