Reviewed, UniProtKB/Swiss-Prot P0A6N1 (EFTU_ECOLI)

Names and origin

Protein names

Recommended name:
    Elongation factor Tu
      Short name=EF-Tu
Alternative name(s):
    P-43

Gene names

Name:	tufA
Ordered Locus Names:	b3339, JW3301
AND
Name:	tufB
Ordered Locus Names:	b3980, JW3943

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.
Subunit structure	Monomer.
Subcellular location	Cytoplasm. Cell membrane; Peripheral membrane protein.
Miscellaneous	This chain is also used in bacteriophage Q-beta RNA polymerase. The antibiotic kirromycin inhibits protein biosynthesis by inhibiting the release of EF-Tu from the ribosome. The antibiotic pulvomycin inhibits protein biosynthesis by disrupting the allosteric control mechanism of EF-Tu. The sequence of the tufB gene is shown. TufA differs in a single position.
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.

Ontologies

Keywords
Biological process	Antibiotic resistance Protein biosynthesis
Cellular component	Cell membrane Cytoplasm Membrane
Ligand	GTP-binding Nucleotide-binding
Molecular function	Elongation factor
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW translational elongation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	GTP binding Inferred from electronic annotation. Source: HAMAP GTPase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct translation elongation factor activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
can	P61517	1	EBI-301077,EBI-562106
helD	P15038	1	EBI-301077,EBI-551473
hslO	P0A6Y5	1	EBI-301077,EBI-562857
ileS	P00956	1	EBI-301077,EBI-552928
kdsB	P04951	1	EBI-301077,EBI-544810
lpxB	P10441	1	EBI-301077,EBI-553692
metN	P30750	1	EBI-301077,EBI-541886
murI	P22634	1	EBI-301077,EBI-554903
mutL	P23367	1	EBI-301077,EBI-554913
mutS	P23909	1	EBI-301077,EBI-554920
nikA	P33590	1	EBI-301077,EBI-555182
nikR	P0A6Z6	1	EBI-301077,EBI-562488
priA	P17888	1	EBI-301077,EBI-552050
queC	P77756	1	EBI-301077,EBI-560024
rho	P0AG30	1	EBI-301077,EBI-545468
rsmD	P0ADX9	1	EBI-301077,EBI-561207
tsf	P0A6P1	2	EBI-301077,EBI-301164
ybeD	P0A8J4	1	EBI-301077,EBI-370708
ycfH	P0AFQ7	1	EBI-301077,EBI-560527
yeaU	P76251	1	EBI-301077,EBI-560661
yfbQ	P0A959	1	EBI-301077,EBI-545313
yheS	P63389	1	EBI-301077,EBI-561198
yjjV	P39408	1	EBI-301077,EBI-561387

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 394

393

Elongation factor Tu

PRO_0000091320

Regions

Nucleotide binding

19 – 26

8

GTP

Nucleotide binding

81 – 85

5

GTP

Nucleotide binding

136 – 139

4

GTP

Amino acid modifications

Modified residue

2

1

N-acetylserine

Modified residue

57

1

N6,N6-dimethyllysine; alternate

Modified residue

57

1

N6-methyllysine; alternate

Modified residue

314

1

N6-acetyllysine

Modified residue

383

1

Phosphothreonine

Natural variations

Natural variant

394

1

S → G in tufA.

Experimental info

Mutagenesis

20

1

H → A: No change in binding GDP and 3-fold reduction in binding EF-Ts

Mutagenesis

21

1

V → G: Lowers GTPase activity 5 to 10-fold

Mutagenesis

83

1

P → T: Loss of GTPase activity and creation of an autophosphorylation site

Mutagenesis

115

1

Q → A: Weaker binding for GDP and for EF-Ts

Mutagenesis

125

1

Q → K: Kirromycin resistant

Mutagenesis

137

1

K → R, Q, E or I: Reduces affinity for GDP

Mutagenesis

139

1

D → N: Reduces affinity for GDP; increases affinity for XDP

Mutagenesis

223

1

G → D: Inhibits codon-induced conformational changes leading to GTPase activation on the ribosome

Mutagenesis

231

1

R → C: Pulvomycin resistant

Mutagenesis

317

1

G → D: Kirromycin resistant

Mutagenesis

334

1

R → C: Pulvomycin resistant

Mutagenesis

335

1

T → A: Pulvomycin resistant

Mutagenesis

349

1

E → A: No change in binding GDP but higher binding constant for EF-Ts

Mutagenesis

376

1

A → T or V: Kirromycin resistant

Secondary structure

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394

Helix Strand Turn

Details...

Beta strand

12 – 18

7

Helix

25 – 40

16

Helix

47 – 51

5

Beta strand

55 – 58

4

Beta strand

61 – 64

4

Beta strand

66 – 71

6

Beta strand

76 – 81

6

Helix

85 – 94

10

Beta strand

100 – 107

8

Turn

108 – 110

3

Helix

114 – 126

13

Beta strand

131 – 136

6

Helix

138 – 140

3

Helix

144 – 160

17

Helix

165 – 167

3

Beta strand

170 – 172

3

Helix

175 – 179

5

Helix

183 – 199

17

Helix

206 – 208

3

Beta strand

212 – 214

3

Beta strand

217 – 221

5

Turn

222 – 224

3

Beta strand

225 – 231

7

Beta strand

234 – 238

5

Beta strand

242 – 249

8

Beta strand

252 – 261

10

Beta strand

264 – 270

7

Beta strand

274 – 279

6

Helix

284 – 286

3

Beta strand

292 – 294

3

Beta strand

300 – 311

12

Turn

314 – 317

4

Beta strand

330 – 333

4

Beta strand

336 – 343

8

Beta strand

356 – 369

14

Beta strand

374 – 379

6

Beta strand

382 – 393

12

Sequences

	Sequence		Length	Mass (Da)
	P0A6N1-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6EDA60255F43358F	FASTA	394	43,314
	10 20 30 40 50 60 MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI DNAPEEKARG 70 80 90 100 110 120 ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI 130 140 150 160 170 180 LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE 190 200 210 220 230 240 GDAEWEAKIL ELAGFLDSYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG 250 260 270 280 290 300 EEVEIVGIKE TQKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGTIK 310 320 330 340 350 360 PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV 370 380 390 VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of the cloned tufA gene of Escherichia coli." Yokota T., Sugisaki H., Takanami M., Kaziro Y. Gene 12:25-31(1980) [PubMed: 7011903] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TUFA).
[2]	"The nucleotide sequence of tufB and four nearby tRNA structural genes of Escherichia coli." An G., Friesen J.D. Gene 12:33-39(1980) [PubMed: 7011904] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TUFB).
[3]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TUFB). Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TUFA AND TUFB). Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TUFA AND TUFB). Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The complete amino-acid sequence of elongation factor Tu from Escherichia coli." Jones M.D., Petersen T.E., Nielsen K.M., Magnusson S., Sottrup-Jensen L., Gausing K., Clark B.F.C. Eur. J. Biochem. 108:507-526(1980) [PubMed: 6997043] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-394.
[7]	"The amino acid sequence of elongation factor Tu of Escherichia coli. The complete sequence." Laursen R.A., L'Italien J.J., Nagarkatti S., Miller D.L. J. Biol. Chem. 256:8102-8109(1981) [PubMed: 7021545] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-394.
[8]	"Transcription of the E. coli tufB gene: cotranscription with four tRNA genes and inhibition by guanosine-5'-diphosphate-3'-diphosphate." Miyajima A., Shibuya M., Kuchino Y., Kaziro Y. Mol. Gen. Genet. 183:13-19(1981) [PubMed: 7035813] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21 (TUFB).
[9]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13 AND 311-322. Strain: K12 / EMG2.
[10]	"Substitution of proline 82 by threonine induces autophosphorylating activity in GTP-binding domain of elongation factor Tu." Cool R.H., Jensen M., Jonak J., Clark B.F.C., Parmeggiani A. J. Biol. Chem. 265:6744-6749(1990) [PubMed: 2157708] [Abstract] Cited for: PROTEIN SEQUENCE OF 76-90, MUTAGENESIS OF PRO-83.
[11]	"Elongation factor Tu is methylated in response to nutrient deprivation in Escherichia coli." Young C.C., Bernlohr R.W. J. Bacteriol. 173:3096-3100(1991) [PubMed: 2022614] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE OF 153-176 AND 262-290. Strain: B/R.
[12]	Noorani S.M., Lindahl L., Zengel J.M. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 369-394 (TUFA). Strain: ECOR 30.
[13]	"Prokaryotic elongation factor Tu is phosphorylated in vivo." Lippmann C., Lindschau C., Vijgenboom E., Schroeder W., Bosch L., Erdmann V.A. J. Biol. Chem. 268:601-607(1993) [PubMed: 8416965] [Abstract] Cited for: PHOSPHORYLATION AT THR-383, PROTEIN SEQUENCE OF 290-304 AND 383-391.
[14]	"Location of the site of methylation in elongation factor Tu." L'Italien J.J., Laursen R.A. FEBS Lett. 107:359-362(1979) [PubMed: 389663] [Abstract] Cited for: METHYLATION AT LYS-57.
[15]	"A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP regulatory protein." Hwang Y.-W., Miller D.L. J. Biol. Chem. 262:13081-13085(1987) [PubMed: 3308869] [Abstract] Cited for: MUTAGENESIS OF ASP-139.
[16]	"Substitution of Val20 by Gly in elongation factor Tu. Effects on the interaction with elongation factors Ts, aminoacyl-tRNA and ribosomes." Jacquet E., Parmeggiani A. Eur. J. Biochem. 185:341-346(1989) [PubMed: 2684669] [Abstract]