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Elongation factor Tu 1 (EF-Tu 1) (Bacteriophage Q beta RNA-directed RNA polymerase subunit III) (P-43)

 EFTU1_ECOLI             Reviewed;         394 AA.
P0CE47; O68929; P02990; P0A6N1; Q2M704; Q2M8R6; Q8X4S9; Q8XED3;
23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
23-MAR-2010, sequence version 1.
25-OCT-2017, entry version 68.
RecName: Full=Elongation factor Tu 1 {ECO:0000255|HAMAP-Rule:MF_00118};
Short=EF-Tu 1 {ECO:0000255|HAMAP-Rule:MF_00118};
AltName: Full=Bacteriophage Q beta RNA-directed RNA polymerase subunit III {ECO:0000303|PubMed:816798};
AltName: Full=P-43;
Name=tufA {ECO:0000255|HAMAP-Rule:MF_00118};
OrderedLocusNames=b3339, JW3301;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7011903; DOI=10.1016/0378-1119(80)90012-8;
Yokota T., Sugisaki H., Takanami M., Kaziro Y.;
"The nucleotide sequence of the cloned tufA gene of Escherichia
coli.";
Gene 12:25-31(1980).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
PROTEIN SEQUENCE OF 2-394, ACETYLATION AT SER-2, AND METHYLATION AT
LYS-57.
STRAIN=B;
PubMed=6997043; DOI=10.1111/j.1432-1033.1980.tb04748.x;
Jones M.D., Petersen T.E., Nielsen K.M., Magnusson S.,
Sottrup-Jensen L., Gausing K., Clark B.F.C.;
"The complete amino-acid sequence of elongation factor Tu from
Escherichia coli.";
Eur. J. Biochem. 108:507-526(1980).
[5]
PROTEIN SEQUENCE OF 2-394, ACETYLATION AT SER-2, AND METHYLATION AT
LYS-57.
PubMed=7021545;
Laursen R.A., L'Italien J.J., Nagarkatti S., Miller D.L.;
"The amino acid sequence of elongation factor Tu of Escherichia coli.
The complete sequence.";
J. Biol. Chem. 256:8102-8109(1981).
[6]
PROTEIN SEQUENCE OF 46-59, AND METHYLATION AT LYS-57.
STRAIN=B;
PubMed=389663; DOI=10.1016/0014-5793(79)80407-X;
L'Italien J.J., Laursen R.A.;
"Location of the site of methylation in elongation factor Tu.";
FEBS Lett. 107:359-362(1979).
[7]
PROTEIN SEQUENCE OF 76-90, AND MUTAGENESIS OF PRO-83.
PubMed=2157708;
Cool R.H., Jensen M., Jonak J., Clark B.F.C., Parmeggiani A.;
"Substitution of proline 82 by threonine induces autophosphorylating
activity in GTP-binding domain of elongation factor Tu.";
J. Biol. Chem. 265:6744-6749(1990).
[8]
PROTEIN SEQUENCE OF 153-176 AND 262-290, METHYLATION AT LYS-57 IN
RESPONSE TO NUTRIENT STARVATION, AND SUBCELLULAR LOCATION.
STRAIN=B/R;
PubMed=2022614; DOI=10.1128/jb.173.10.3096-3100.1991;
Young C.C., Bernlohr R.W.;
"Elongation factor Tu is methylated in response to nutrient
deprivation in Escherichia coli.";
J. Bacteriol. 173:3096-3100(1991).
[9]
PROTEIN SEQUENCE OF 311-322, AND BLOCKAGE OF N-TERMINUS.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 369-394.
STRAIN=ECOR 30;
Noorani S.M., Lindahl L., Zengel J.M.;
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[11]
BLOCKAGE OF N-TERMINUS, AND SUBCELLULAR LOCATION.
STRAIN=K12 / BHB 960;
PubMed=775340; DOI=10.1038/261023a0;
Jacobson G.R., Rosenbusch J.P.;
"Abundance and membrane association of elongation factor Tu in E.
coli.";
Nature 261:23-26(1976).
[12]
FUNCTION IN VIRAL RNA REPLICATION, AND SUBUNIT.
PubMed=816798;
Carmichael G.G., Landers T.A., Weber K.;
"Immunochemical analysis of the functions of the subunits of phage
Qbeta ribonucleic acid replicase.";
J. Biol. Chem. 251:2744-2748(1976).
[13]
PHOSPHORYLATION AT THR-383, AND PROTEIN SEQUENCE OF 290-304 AND
383-391.
PubMed=8416965;
Lippmann C., Lindschau C., Vijgenboom E., Schroeder W., Bosch L.,
Erdmann V.A.;
"Prokaryotic elongation factor Tu is phosphorylated in vivo.";
J. Biol. Chem. 268:601-607(1993).
[14]
MUTAGENESIS OF ASP-139.
PubMed=3308869;
Hwang Y.-W., Miller D.L.;
"A mutation that alters the nucleotide specificity of elongation
factor Tu, a GTP regulatory protein.";
J. Biol. Chem. 262:13081-13085(1987).
[15]
MUTAGENESIS OF VAL-21.
PubMed=2684669; DOI=10.1111/j.1432-1033.1989.tb15121.x;
Jacquet E., Parmeggiani A.;
"Substitution of Val20 by Gly in elongation factor Tu. Effects on the
interaction with elongation factors Ts, aminoacyl-tRNA and
ribosomes.";
Eur. J. Biochem. 185:341-346(1989).
[16]
MUTAGENESIS OF LYS-137.
PubMed=2498311;
Hwang Y.-W., Sanchez A., Miller D.L.;
"Mutagenesis of bacterial elongation factor Tu at lysine 136. A
conserved amino acid in GTP regulatory proteins.";
J. Biol. Chem. 264:8304-8309(1989).
[17]
MUTAGENESIS.
PubMed=2508560; DOI=10.1016/0003-9861(89)90452-9;
Hwang Y.-W., McCabe P.G., Innis M.A., Miller D.L.;
"Site-directed mutagenesis of the GDP binding domain of bacterial
elongation factor Tu.";
Arch. Biochem. Biophys. 274:394-403(1989).
[18]
CHARACTERIZATION OF MUTANT ASP-223.
PubMed=8978702;
Vorstenbosch E., Pape T., Rodnina M.V., Kraal B., Wintermeyer W.;
"The G222D mutation in elongation factor Tu inhibits the codon-induced
conformational changes leading to GTPase activation on the ribosome.";
EMBO J. 15:6766-6774(1996).
[19]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[20]
MUTAGENESIS OF HIS-20; GLN-115 AND GLU-349.
PubMed=9468511; DOI=10.1074/jbc.273.8.4556;
Zhang Y., Yu N.-J., Spremulli L.L.;
"Mutational analysis of the roles of residues in Escherichia coli
elongation factor Ts in the interaction with elongation factor Tu.";
J. Biol. Chem. 273:4556-4562(1998).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-314, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[22]
VARIANTS RESISTANT TO KIRROMYCIN.
PubMed=7525272;
Mesters J.R., Zeef L.A.H., Hilgenfeld R., de Graaf J.M., Kraal B.,
Bosch L.;
"The structural and functional basis for the kirromycin resistance of
mutant EF-Tu species in Escherichia coli.";
EMBO J. 13:4877-4885(1994).
[23]
VARIANTS RESISTANT TO PULVOMYCIN.
PubMed=7957075;
Zeef L.A.H., Bosch L., Anborgh P.H., Cetin R., Parmeggiani A.,
Hilgenfeld R.;
"Pulvomycin-resistant mutants of E.coli elongation factor Tu.";
EMBO J. 13:5113-5120(1994).
[24]
FUNCTION IN TRANS-TRANSLATION, AND TMRNA-BINDING.
STRAIN=K12 / BW25113;
PubMed=15069072; DOI=10.1074/jbc.M314086200;
Hallier M., Ivanova N., Rametti A., Pavlov M., Ehrenberg M.,
Felden B.;
"Pre-binding of small protein B to a stalled ribosome triggers trans-
translation.";
J. Biol. Chem. 279:25978-25985(2004).
[25]
PHOSPHORYLATION AT THR-383 BY HIPA.
PubMed=19150849; DOI=10.1126/science.1163806;
Schumacher M.A., Piro K.M., Xu W., Hansen S., Lewis K., Brennan R.G.;
"Molecular mechanisms of HipA-mediated multidrug tolerance and its
neutralization by HipB.";
Science 323:396-401(2009).
[26]
LACK OF PHOSPHORYLATION BY HIPA.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=24095282; DOI=10.1016/j.molcel.2013.08.045;
Germain E., Castro-Roa D., Zenkin N., Gerdes K.;
"Molecular mechanism of bacterial persistence by HipA.";
Mol. Cell 52:248-254(2013).
[27]
PHOSPHORYLATION AT THR-383 BY DOC, AND MUTAGENESIS OF THR-383.
PubMed=24141193; DOI=10.1038/nchembio.1364;
Castro-Roa D., Garcia-Pino A., De Gieter S., van Nuland N.A.,
Loris R., Zenkin N.;
"The Fic protein Doc uses an inverted substrate to phosphorylate and
inactivate EF-Tu.";
Nat. Chem. Biol. 9:811-817(2013).
[28]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 2-392 IN A MODIFIED FORM.
PubMed=3908095;
la Cour T.F., Nyborg J., Thirup S., Clark B.F.;
"Structural details of the binding of guanosine diphosphate to
elongation factor Tu from E. coli as studied by X-ray
crystallography.";
EMBO J. 4:2385-2388(1985).
[29]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2-394 IN COMPLEX WITH GDP.
PubMed=9918724; DOI=10.1006/jmbi.1998.2387;
Song H., Parsons M.R., Rowsell S., Leonard G., Phillips S.E.V.;
"Crystal structure of intact elongation factor EF-Tu from Escherichia
coli in GDP conformation at 2.05-A resolution.";
J. Mol. Biol. 285:1245-1256(1999).
[30]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 2-393 IN COMPLEX WITH
ANTIBIOTIC GE2270A.
PubMed=10625477; DOI=10.1021/bi9913597;
Heffron S.E., Jurnak F.;
"Structure of an EF-Tu complex with a thiazolyl peptide antibiotic
determined at 2.35 A resolution: atomic basis for GE2270A inhibition
of EF-Tu.";
Biochemistry 39:37-45(2000).
[31]
X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF EF-TU-GDP.
PubMed=16552145; DOI=10.1107/S0907444906004021;
Heffron S.E., Moeller R., Jurnak F.;
"Solving the structure of Escherichia coli elongation factor Tu using
a twinned data set.";
Acta Crystallogr. D 62:433-438(2006).
[32]
X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 9-44 AND 60-393 IN COMPLEX
WITH TETRACYCLINE.
PubMed=17057344; DOI=10.1107/S0907444906035426;
Heffron S.E., Mui S., Aorora A., Abel K., Bergmann E., Jurnak F.;
"Molecular complementarity between tetracycline and the GTPase active
site of elongation factor Tu.";
Acta Crystallogr. D 62:1392-1400(2006).
-!- FUNCTION: This protein promotes the GTP-dependent binding of
aminoacyl-tRNA to the A-site of ribosomes during protein
biosynthesis.
-!- FUNCTION: May play an important regulatory role in cell growth and
in the bacterial response to nutrient deprivation.
-!- FUNCTION: In case of infection by bacteriophage Qbeta, part of the
viral RNA-dependent RNA polymerase complex. With EF-Ts may provide
a stabilizing scaffold for the beta (catalytic) subunit. Helps
separate the double-stranded RNA of the template and growing RNA
during elongation. With the beta subunit helps form the exit
tunnel for template RNA. {ECO:0000269|PubMed:816798, ECO:0000305}.
-!- FUNCTION: Plays a stimulatory role in trans-translation; binds
tmRNA. {ECO:0000269|PubMed:15069072}.
-!- FUNCTION: Protects glycyl-tRNA(Gly) from hydrolysis by E.coli D-
aminoacyl-tRNA deacylase (dtd) (By similarity).
{ECO:0000250|UniProtKB:Q5SHN6}.
-!- SUBUNIT: Monomer. In case of infection by bacteriophage Qbeta,
part of the viral RNA-dependent RNA polymerase complex, the other
subunits are the viral replicase catalytic subunit (AC P14647),
host ribosomal protein S1 and EF-Ts (PubMed:816798).
{ECO:0000255|HAMAP-Rule:MF_00118, ECO:0000269|PubMed:10625477,
ECO:0000269|PubMed:17057344, ECO:0000269|PubMed:816798,
ECO:0000269|PubMed:9918724, ECO:0000305}.
-!- INTERACTION:
P14647:- (xeno); NbExp=2; IntAct=EBI-301077, EBI-9010000;
P61517:can; NbExp=2; IntAct=EBI-301077, EBI-562106;
P76251:dmlA; NbExp=2; IntAct=EBI-301077, EBI-560661;
Q06259:doc (xeno); NbExp=5; IntAct=EBI-301077, EBI-2908816;
P15038:helD; NbExp=3; IntAct=EBI-301077, EBI-551473;
P0A6Y5:hslO; NbExp=3; IntAct=EBI-301077, EBI-562857;
P00956:ileS; NbExp=2; IntAct=EBI-301077, EBI-552928;
P04951:kdsB; NbExp=2; IntAct=EBI-301077, EBI-544810;
P10441:lpxB; NbExp=3; IntAct=EBI-301077, EBI-553692;
P22634:murI; NbExp=2; IntAct=EBI-301077, EBI-554903;
P23909:mutS; NbExp=2; IntAct=EBI-301077, EBI-554920;
P33590:nikA; NbExp=2; IntAct=EBI-301077, EBI-555182;
P0A6Z6:nikR; NbExp=3; IntAct=EBI-301077, EBI-562488;
P77756:queC; NbExp=3; IntAct=EBI-301077, EBI-560024;
P0AG30:rho; NbExp=2; IntAct=EBI-301077, EBI-545468;
P0ADX9:rsmD; NbExp=2; IntAct=EBI-301077, EBI-561207;
P0A6P1:tsf; NbExp=12; IntAct=EBI-301077, EBI-301164;
P0A8J4:ybeD; NbExp=3; IntAct=EBI-301077, EBI-370708;
P63389:yheS; NbExp=3; IntAct=EBI-301077, EBI-561198;
P39408:yjjV; NbExp=2; IntAct=EBI-301077, EBI-561387;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral
membrane protein. Note=Between 50-80% of the protein is associated
with the cell inner membrane. Localization to the membrane has
been suggested to follow nutrient stress.
-!- PTM: The N-terminus is blocked.
-!- PTM: Methylated in vivo on Lys-57 in response to nutrient
starvation. {ECO:0000269|PubMed:2022614,
ECO:0000269|PubMed:389663, ECO:0000269|PubMed:6997043,
ECO:0000269|PubMed:7021545}.
-!- PTM: Phosphorylated in vitro by phage protein doc on Thr-383.
{ECO:0000269|PubMed:19150849, ECO:0000269|PubMed:24141193,
ECO:0000269|PubMed:8416965}.
-!- PTM: Phosphorylated in vitro by HipA on Thr-383 (PubMed:19150849),
this has since been reported not to occur in vivo
(PubMed:24095282). {ECO:0000269|PubMed:19150849,
ECO:0000269|PubMed:24095282, ECO:0000269|PubMed:24141193,
ECO:0000269|PubMed:8416965}.
-!- MISCELLANEOUS: Present with about 70,000 molecules/cell.
{ECO:0000305|PubMed:775340}.
-!- MISCELLANEOUS: This chain is also used in bacteriophage Q-beta RNA
polymerase. {ECO:0000269|PubMed:816798}.
-!- MISCELLANEOUS: The antibiotic kirromycin inhibits protein
biosynthesis by inhibiting the release of EF-Tu from the ribosome.
{ECO:0000269|PubMed:7525272}.
-!- MISCELLANEOUS: The antibiotic pulvomycin inhibits protein
biosynthesis by disrupting the allosteric control mechanism of EF-
Tu. {ECO:0000269|PubMed:7957075}.
-!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
subfamily. {ECO:0000255|HAMAP-Rule:MF_00118}.
-!- CAUTION: EF-Tu 1 and EF-Tu 2 differ in a single position and are
no longer merged. However, many papers are found in both entries
as it is not always possible to determine for each paper which of
EF-Tu 1 or EF-Tu 2 was being worked upon. {ECO:0000305}.
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EMBL; J01690; AAA50993.1; -; Genomic_DNA.
EMBL; M10459; AAA24702.1; -; Genomic_DNA.
EMBL; U00096; AAC76364.1; -; Genomic_DNA.
EMBL; AP009048; BAE77952.1; -; Genomic_DNA.
EMBL; U18997; AAA58136.1; -; Genomic_DNA.
EMBL; AF058450; AAC14286.1; -; Genomic_DNA.
PIR; A91475; EFECTA.
RefSeq; NP_417798.1; NC_000913.3.
RefSeq; WP_000031783.1; NZ_LN832404.1.
PDB; 1D8T; X-ray; 2.35 A; A/B=2-394.
PDB; 1EFC; X-ray; 2.05 A; A/B=2-393.
PDB; 1ETU; X-ray; 2.90 A; A=2-394.
PDB; 1MJ1; EM; 13.00 A; A=8-389.
PDB; 2FX3; X-ray; 3.40 A; A=2-394.
PDB; 2HCJ; X-ray; 2.12 A; A=9-45, B=60-394.
PDB; 2HDN; X-ray; 2.80 A; A/C/E/G/I/K=9-45, B/D/F/H/J/L=60-394.
PDB; 3EP2; EM; -; X=2-393.
PDB; 3EQ3; EM; -; X=2-393.
PDB; 3EQ4; EM; -; X=2-393.
PDB; 3U2Q; X-ray; 2.70 A; A=3-394.
PDB; 3U6B; X-ray; 2.12 A; A/B=3-394.
PDB; 3U6K; X-ray; 2.45 A; A/B=3-394.
PDB; 4G5G; X-ray; 2.30 A; A=3-394.
PDB; 4PC3; X-ray; 1.83 A; A/B=1-394.
PDB; 4PC7; X-ray; 3.60 A; A=1-394.
PDB; 4Q7J; X-ray; 2.90 A; B/F=2-394.
PDB; 4V69; EM; 6.70 A; AZ=2-393.
PDB; 5I4R; X-ray; 3.30 A; D/H=60-394.
PDB; 5JBQ; X-ray; 2.01 A; A=1-394.
PDB; 5UYK; EM; 3.90 A; Z=2-393.
PDB; 5UYL; EM; 3.60 A; Z=2-393.
PDB; 5UYM; EM; 3.20 A; Z=2-393.
PDB; 5UYN; EM; 4.00 A; Z=2-393.
PDB; 5UYP; EM; 3.90 A; Z=2-393.
PDB; 5UYQ; EM; 3.80 A; Z=2-393.
PDBsum; 1D8T; -.
PDBsum; 1EFC; -.
PDBsum; 1ETU; -.
PDBsum; 1MJ1; -.
PDBsum; 2FX3; -.
PDBsum; 2HCJ; -.
PDBsum; 2HDN; -.
PDBsum; 3EP2; -.
PDBsum; 3EQ3; -.
PDBsum; 3EQ4; -.
PDBsum; 3U2Q; -.
PDBsum; 3U6B; -.
PDBsum; 3U6K; -.
PDBsum; 4G5G; -.
PDBsum; 4PC3; -.
PDBsum; 4PC7; -.
PDBsum; 4Q7J; -.
PDBsum; 4V69; -.
PDBsum; 5I4R; -.
PDBsum; 5JBQ; -.
PDBsum; 5UYK; -.
PDBsum; 5UYL; -.
PDBsum; 5UYM; -.
PDBsum; 5UYN; -.
PDBsum; 5UYP; -.
PDBsum; 5UYQ; -.
ProteinModelPortal; P0CE47; -.
SMR; P0CE47; -.
BioGrid; 4259390; 74.
BioGrid; 852150; 1.
DIP; DIP-6159N; -.
IntAct; P0CE47; 162.
STRING; 316385.ECDH10B_3514; -.
iPTMnet; P0CE47; -.
PaxDb; P0CE47; -.
PRIDE; P0CE47; -.
EnsemblBacteria; AAC76364; AAC76364; b3339.
EnsemblBacteria; BAE77952; BAE77952; BAE77952.
GeneID; 947838; -.
KEGG; ecj:JW3301; -.
KEGG; eco:b3339; -.
PATRIC; fig|1411691.4.peg.3392; -.
EchoBASE; EB1029; -.
EcoGene; EG11036; tufA.
eggNOG; ENOG4105CGV; Bacteria.
eggNOG; COG0050; LUCA.
InParanoid; P0CE47; -.
KO; K02358; -.
PhylomeDB; P0CE47; -.
BioCyc; EcoCyc:EG11036-MONOMER; -.
EvolutionaryTrace; P0CE47; -.
PRO; PR:P0CE47; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
CDD; cd03697; EFTU_II; 1.
HAMAP; MF_00118_B; EF_Tu_B; 1.
InterPro; IPR004161; EFTu-like_2.
InterPro; IPR033720; EFTU_2.
InterPro; IPR031157; G_TR_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR000795; TF_GTP-bd_dom.
InterPro; IPR009000; Transl_B-barrel.
InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
Pfam; PF00009; GTP_EFTU; 1.
Pfam; PF03144; GTP_EFTU_D2; 1.
Pfam; PF03143; GTP_EFTU_D3; 1.
PRINTS; PR00315; ELONGATNFCT.
SUPFAM; SSF50447; SSF50447; 1.
SUPFAM; SSF50465; SSF50465; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00485; EF-Tu; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS00301; G_TR_1; 1.
PROSITE; PS51722; G_TR_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Antibiotic resistance; Cell inner membrane;
Cell membrane; Complete proteome; Cytoplasm;
Direct protein sequencing; Elongation factor; GTP-binding; Membrane;
Methylation; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
Reference proteome; RNA-binding.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6997043,
ECO:0000269|PubMed:7021545}.
CHAIN 2 394 Elongation factor Tu 1.
/FTId=PRO_0000091320.
DOMAIN 10 204 tr-type G.
NP_BIND 19 26 GTP.
NP_BIND 81 85 GTP.
NP_BIND 136 139 GTP.
REGION 19 26 G1. {ECO:0000250}.
REGION 60 64 G2. {ECO:0000250}.
REGION 81 84 G3. {ECO:0000250}.
REGION 136 139 G4. {ECO:0000250}.
REGION 174 176 G5. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:6997043,
ECO:0000269|PubMed:7021545}.
MOD_RES 57 57 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:2022614,
ECO:0000269|PubMed:389663,
ECO:0000269|PubMed:6997043,
ECO:0000269|PubMed:7021545}.
MOD_RES 57 57 N6-methyllysine; alternate.
{ECO:0000269|PubMed:2022614,
ECO:0000269|PubMed:389663,
ECO:0000269|PubMed:6997043,
ECO:0000269|PubMed:7021545}.
MOD_RES 314 314 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 383 383 Phosphothreonine.
{ECO:0000269|PubMed:19150849,
ECO:0000269|PubMed:24141193,
ECO:0000269|PubMed:8416965}.
MUTAGEN 20 20 H->A: No change in binding GDP and 3-fold
reduction in binding EF-Ts.
{ECO:0000269|PubMed:9468511}.
MUTAGEN 21 21 V->G: Lowers GTPase activity 5 to 10-
fold. {ECO:0000269|PubMed:2684669}.
MUTAGEN 83 83 P->T: Loss of GTPase activity and
creation of an autophosphorylation site.
{ECO:0000269|PubMed:2157708}.
MUTAGEN 115 115 Q->A: Weaker binding for GDP and for EF-
Ts. {ECO:0000269|PubMed:9468511}.
MUTAGEN 125 125 Q->K: Kirromycin resistant.
{ECO:0000269|PubMed:2508560}.
MUTAGEN 137 137 K->R,Q,E,I: Reduces affinity for GDP.
{ECO:0000269|PubMed:2498311}.
MUTAGEN 139 139 D->N: Reduces affinity for GDP; increases
affinity for XDP.
{ECO:0000269|PubMed:3308869}.
MUTAGEN 223 223 G->D: Inhibits codon-induced
conformational changes leading to GTPase
activation on the ribosome.
{ECO:0000269|PubMed:2508560}.
MUTAGEN 231 231 R->C: Pulvomycin resistant.
{ECO:0000269|PubMed:2508560}.
MUTAGEN 317 317 G->D: Kirromycin resistant.
{ECO:0000269|PubMed:2508560}.
MUTAGEN 334 334 R->C: Pulvomycin resistant.
{ECO:0000269|PubMed:2508560}.
MUTAGEN 335 335 T->A: Pulvomycin resistant.
{ECO:0000269|PubMed:2508560}.
MUTAGEN 349 349 E->A: No change in binding GDP but higher
binding constant for EF-Ts.
{ECO:0000269|PubMed:9468511}.
MUTAGEN 376 376 A->T,V: Kirromycin resistant.
{ECO:0000269|PubMed:2508560}.
MUTAGEN 383 383 T->V: No longer phosphorylated by phage
protein doc, has no effect on
translation.
{ECO:0000269|PubMed:24141193}.
HELIX 4 7 {ECO:0000244|PDB:5JBQ}.
STRAND 12 19 {ECO:0000244|PDB:4PC3}.
STRAND 20 24 {ECO:0000244|PDB:1ETU}.
HELIX 25 40 {ECO:0000244|PDB:4PC3}.
HELIX 47 51 {ECO:0000244|PDB:5JBQ}.
STRAND 55 60 {ECO:0000244|PDB:5JBQ}.
STRAND 62 64 {ECO:0000244|PDB:5JBQ}.
STRAND 68 71 {ECO:0000244|PDB:4PC3}.
STRAND 76 81 {ECO:0000244|PDB:4PC3}.
HELIX 85 94 {ECO:0000244|PDB:4PC3}.
STRAND 95 97 {ECO:0000244|PDB:3U6B}.
STRAND 100 107 {ECO:0000244|PDB:4PC3}.
TURN 108 110 {ECO:0000244|PDB:4PC3}.
HELIX 116 125 {ECO:0000244|PDB:4PC3}.
STRAND 131 136 {ECO:0000244|PDB:4PC3}.
HELIX 138 140 {ECO:0000244|PDB:4PC3}.
HELIX 144 160 {ECO:0000244|PDB:4PC3}.
TURN 165 167 {ECO:0000244|PDB:4PC3}.
STRAND 170 172 {ECO:0000244|PDB:4PC3}.
HELIX 175 179 {ECO:0000244|PDB:4PC3}.
HELIX 183 199 {ECO:0000244|PDB:4PC3}.
HELIX 206 208 {ECO:0000244|PDB:4PC3}.
STRAND 212 214 {ECO:0000244|PDB:4PC3}.
STRAND 217 221 {ECO:0000244|PDB:4PC3}.
TURN 222 224 {ECO:0000244|PDB:4PC3}.
STRAND 225 231 {ECO:0000244|PDB:4PC3}.
STRAND 234 238 {ECO:0000244|PDB:4PC3}.
STRAND 242 249 {ECO:0000244|PDB:4PC3}.
STRAND 252 261 {ECO:0000244|PDB:4PC3}.
STRAND 264 270 {ECO:0000244|PDB:4PC3}.
STRAND 274 281 {ECO:0000244|PDB:4PC3}.
HELIX 284 286 {ECO:0000244|PDB:4PC3}.
STRAND 292 294 {ECO:0000244|PDB:4PC3}.
TURN 296 298 {ECO:0000244|PDB:4Q7J}.
STRAND 301 311 {ECO:0000244|PDB:4PC3}.
TURN 314 317 {ECO:0000244|PDB:4PC3}.
STRAND 323 327 {ECO:0000244|PDB:3U6K}.
STRAND 330 333 {ECO:0000244|PDB:4PC3}.
STRAND 336 343 {ECO:0000244|PDB:4PC3}.
STRAND 356 368 {ECO:0000244|PDB:4PC3}.
STRAND 374 379 {ECO:0000244|PDB:4PC3}.
STRAND 382 394 {ECO:0000244|PDB:4PC3}.
SEQUENCE 394 AA; 43284 MW; 731A60255F43358F CRC64;
MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI DNAPEEKARG
ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE
GDAEWEAKIL ELAGFLDSYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG
EEVEIVGIKE TQKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGTIK
PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV
VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLG


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