P0CE48 (EFTU2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongation factor Tu 2
Short name=EF-Tu 2

Alternative name(s):
P-43

Gene names

Name:	tufB
Ordered Locus Names:	b3980, JW3943

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

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. HAMAP-Rule MF_00118_B May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation. HAMAP-Rule MF_00118_B
Subunit structure	Monomer.
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. Ref.8 Ref.10
Post-translational modification	The N-terminus is blocked. HAMAP-Rule MF_00118_B Methylated in vivo on Lys-57 in response to nutrient starvation. Ref.8 Ref.12 Phosphorylated in vitro by HipA on Thr-383. Ref.11 Ref.20
Miscellaneous	This chain is also used in bacteriophage Q-beta RNA polymerase. HAMAP-Rule MF_00118_B Present with about 70,000 molecules/cell (Ref.10). HAMAP-Rule MF_00118_B The antibiotic kirromycin inhibits protein biosynthesis by inhibiting the release of EF-Tu from the ribosome. TufA resistance to kirromycin is conferred by mutations to Gln-125, Gly-317 and Ala-376. This has not been formally proven for tufB, but is certainly correct. HAMAP-Rule MF_00118_B The antibiotic pulvomycin inhibits protein biosynthesis by disrupting the allosteric control mechanism of EF-Tu TufA resistance to pulvomycin is conferred by Arg-231, Arg-334 and Thr-335. This has not been formally proven for tufB, but is certainly correct. HAMAP-Rule MF_00118_B
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.
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.

Ontologies

Keywords
Biological process	Antibiotic resistance Protein biosynthesis
Cellular component	Cell inner membrane 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 Reference proteome
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTP binding Inferred from electronic annotation. Source: HAMAP GTPase activity Inferred from electronic annotation. Source: InterPro translation elongation factor activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5 Ref.6

Chain

2 – 394

393

Elongation factor Tu 2 HAMAP-Rule MF_00118_B

PRO_0000392289

Regions

Nucleotide binding

19 – 26

8

GTP HAMAP-Rule MF_00118_B

Nucleotide binding

81 – 85

5

GTP HAMAP-Rule MF_00118_B

Nucleotide binding

136 – 139

4

GTP HAMAP-Rule MF_00118_B

Amino acid modifications

Modified residue

2

1

N-acetylserine HAMAP-Rule MF_00118_B

Modified residue

38

1

N6-succinyllysine Ref.21

Modified residue

57

1

N6,N6-dimethyllysine; alternate Ref.8 Ref.12

Modified residue

57

1

N6-methyllysine; alternate Ref.8 Ref.12

Modified residue

177

1

N6-succinyllysine Ref.21

Modified residue

249

1

N6-succinyllysine Ref.21

Modified residue

253

1

N6-succinyllysine Ref.21

Modified residue

295

1

N6-succinyllysine Ref.21

Modified residue

314

1

N6-acetyllysine; alternate Ref.19

Modified residue

314

1

N6-succinyllysine; alternate Ref.21

Modified residue

383

1

Phosphothreonine Ref.11

Experimental info

Mutagenesis

20

1

H → A: No change in binding GDP and 3-fold reduction in binding EF-Ts. Ref.18

Mutagenesis

115

1

Q → A: Weaker binding for GDP and for EF-Ts. Ref.18

Mutagenesis

137

1

K → R, Q, E or I: Reduces affinity for GDP. Ref.14

Mutagenesis

139

1

D → N: Reduces affinity for GDP; increases affinity for XDP. Ref.13

Mutagenesis

223

1

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

Mutagenesis

349

1

E → A: No change in binding GDP but higher binding constant for EF-Ts. Ref.18

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

Helix

61 – 63

3

Beta strand

67 – 71

5

Beta strand

76 – 81

6

Helix

86 – 88

3

Helix

89 – 96

8

Beta strand

102 – 107

6

Turn

108 – 110

3

Helix

114 – 126

13

Beta strand

131 – 136

6

Helix

138 – 140

3

Helix

144 – 160

17

Turn

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

218 – 221

4

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 – 281

8

Helix

284 – 286

3

Beta strand

292 – 295

4

Beta strand

300 – 311

12

Helix

314 – 316

3

Beta strand

330 – 333

4

Beta strand

336 – 343

8

Beta strand

356 – 369

14

Beta strand

374 – 379

6

Beta strand

382 – 392

11

Sequences

	Sequence		Length	Mass (Da)
	P0CE48 [UniParc]. Last modified March 23, 2010. Version 1. 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 tufB and four nearby tRNA structural genes of Escherichia coli." An G., Friesen J.D. Gene 12:33-39(1980) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-394.
[6]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-394.
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[8]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 153-176 AND 262-290, METHYLATION AT LYS-57 IN RESPONSE TO NUTRIENT STARVATION, SUBCELLULAR LOCATION. Strain: B/R.
[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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 311-322, BLOCKAGE OF N-TERMINUS. Strain: K12 / EMG2.
[10]	"Abundance and membrane association of elongation factor Tu in E. coli." Jacobson G.R., Rosenbusch J.P. Nature 261:23-26(1976) [PubMed] [Europe PMC] [Abstract] Cited for: BLOCKAGE OF N-TERMINUS, SUBCELLULAR LOCATION. Strain: K12 / BHB 960.
[11]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-383, PROTEIN SEQUENCE OF 290-304 AND 383-391.
[12]	"Location of the site of methylation in elongation factor Tu." L'Italien J.J., Laursen R.A. FEBS Lett. 107:359-362(1979) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-57.
[13]	"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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASP-139.
[14]	"Mutagenesis of bacterial elongation factor Tu at lysine 136. A conserved amino acid in GTP regulatory proteins." Hwang Y.-W., Sanchez A., Miller D.L. J. Biol. Chem. 264:8304-8309(1989) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF LYS-137.
[15]	"Site-directed mutagenesis of the GDP binding domain of bacterial elongation factor Tu." Hwang Y.-W., McCabe P.G., Innis M.A., Miller D.L. Arch. Biochem. Biophys. 274:394-403(1989) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[16]	"The G222D mutation in elongation factor Tu inhibits the codon-induced conformational changes leading to GTPase activation on the ribosome." Vorstenbosch E., Pape T., Rodnina M.V., Kraal B., Wintermeyer W. EMBO J. 15:6766-6774(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF MUTANT ASP-223.
[17]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[18]	"Mutational analysis of the roles of residues in Escherichia coli elongation factor Ts in the interaction with elongation factor Tu." Zhang Y., Yu N.-J., Spremulli L.L. J. Biol. Chem. 273:4556-4562(1998) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-20; GLN-115 AND GLU-349.
[19]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-314, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[20]	"Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB." Schumacher M.A., Piro K.M., Xu W., Hansen S., Lewis K., Brennan R.G. Science 323:396-401(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY HIPA.
[21]	"Identification of lysine succinylation as a new post-translational modification." Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y. Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUCCINYLATION AT LYS-38; LYS-177; LYS-249; LYS-253; LYS-295 AND LYS-314. Strain: K12.
[22]	"Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins." Jurnak F. Science 230:32-36(1985) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-394 OF A TRYPSIN-MODIFIED EF-TU-GDP.
[23]	"Refined structure of elongation factor EF-Tu from Escherichia coli." Kjeldgaard M., Nyborg J. J. Mol. Biol. 223:721-742(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[24]	"The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5-A resolution." Kawashima T., Berthet-Colominas C., Wulff M., Cusack S., Leberman R. Nature 379:511-518(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 10-394 IN COMPLEX WITH EF-TS.
[25]	Erratum Kawashima T., Berthet-Colominas C., Wulff M., Cusack S., Leberman R. Nature 381:172-172(1996)
[26]	"An alpha to beta conformational switch in EF-Tu." Abel K., Yoder M.D., Hilgenfeld R., Jurnak F. Structure 4:1153-1159(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GDP AND ANTIBIOTIC GE2270A.
[27]	"Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05-A resolution." Song H., Parsons M.R., Rowsell S., Leonard G., Phillips S.E.V. J. Mol. Biol. 285:1245-1256(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
[28]	"Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process." Valle M., Sengupta J., Swami N.K., Grassucci R.A., Burkhardt N., Nierhaus K.H., Agrawal R.K., Frank J. EMBO J. 21:3557-3567(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (16.8 ANGSTROMS) OF 2-393 IN THE 70S RIBOSOME.
[29]	"Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy." Valle M., Zavialov A., Li W., Stagg S.M., Sengupta J., Nielsen R.C., Nissen P., Harvey S.C., Ehrenberg M., Frank J. Nat. Struct. Biol. 10:899-906(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 3-394, STRUCTURE BY ELECTRON MICROSCOPY (10.0 ANGSTROMS) OF 2-393 IN COMPLEX WITH THE 70S RIBOSOME.
[30]	"Enacyloxin IIa pinpoints a binding pocket of elongation factor Tu for development of novel antibiotics." Parmeggiani A., Krab I.M., Watanabe T., Nielsen R.C., Dahlberg C., Nyborg J., Nissen P. J. Biol. Chem. 281:2893-2900(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-394 OF EF-TU-GUANYLYL IMINODIPHOSPHATE (GDPNP) ENACYLOXIN IIA COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X57091 Genomic DNA. Translation: CAA40370.1.
J01717 Genomic DNA. Translation: AAA24669.1.
U00006 Genomic DNA. Translation: AAC43078.1.
U00096 Genomic DNA. Translation: AAC76954.1.
AP009048 Genomic DNA. Translation: BAE77340.1.

PIR

EFECT. A91478.

RefSeq

NP_418407.1. NC_000913.2.
YP_491481.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DG1	X-ray	2.50	G/H	1-394	[»]
1EFM	X-ray	2.70	A	2-394	[»]
1EFU	X-ray	2.50	A/C	10-394	[»]
1LS2	electron microscopy	16.80	A	2-394	[»]
1OB2	X-ray	3.35	A	3-394	[»]
1QZD	electron microscopy	-	A	2-394	[»]
2BVN	X-ray	2.30	A/B	2-394	[»]
3FIH	electron microscopy	6.70	Z	2-394	[»]
3IZV	electron microscopy	-	C	2-394	[»]
3IZW	electron microscopy	-	C	2-394	[»]
3MMP	X-ray	2.50	A/C	1-394	[»]

ProteinModelPortal

P0CE48.

SMR

P0CE48. Positions 9-394.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1234073.

Proteomic databases

PRIDE

P0CE48.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76954; AAC76954; b3980.
BAE77340; BAE77340; BAE77340.

GeneID

12932406.
948482.

KEGG

ecj:Y75_p3217.
eco:b3980.

PATRIC

32123481. VBIEscCol129921_4093.

Organism-specific databases

EchoBASE

EB1030.

EcoGene

EG11037. tufB.

Phylogenomic databases

KO

K02358.

OMA

CEFVGYN.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11037-MONOMER.

Gene expression databases

Genevestigator

P0A6N1.

Family and domain databases

HAMAP

MF_00118_B. EF_Tu_B.

InterPro

IPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004541. Transl_elong_EFTu/EF1A_bac/org.
IPR004160. Transl_elong_EFTu/EF1A_C.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]

Pfam

PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]

PRINTS

PR00315. ELONGATNFCT.

SUPFAM

SSF50465. Elong_init_C. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF50447. Translat_factor. 1 hit.

TIGRFAMs

TIGR00485. EF-Tu. 1 hit.
TIGR00231. small_GTP. 1 hit.

PROSITE

PS00301. EFACTOR_GTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0CE48.

Entry information

Entry name

EFTU2_ECOLI

Accession

Primary (citable) accession number: P0CE48
Secondary accession number(s): O68929 , P02990, P0A6N1, Q2M704, Q2M8R6, Q8X4S9, Q8XED3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 23, 2010
Last sequence update:	March 23, 2010
Last modified:	May 29, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program