EFTU2_ECOLI
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 03-AUG-2022, entry version 95.
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 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}.
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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; 5WFK; EM; 3.40 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 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; 5WFK; -.
DR PDBsum; 6EZE; -.
DR PDBsum; 7ABZ; -.
DR AlphaFoldDB; P0CE48; -.
DR SMR; P0CE48; -.
DR BioGRID; 4261400; 34.
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; P0CE48; -.
DR PRIDE; P0CE48; -.
DR EnsemblBacteria; AAC76954; AAC76954; b3980.
DR EnsemblBacteria; BAE77340; BAE77340; BAE77340.
DR GeneID; 66672109; -.
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; EGDKEWG; -.
DR PhylomeDB; P0CE48; -.
DR BioCyc; EcoCyc:EG11037-MON; -.
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 DisProt; DP01965; -.
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 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
