Reviewed, UniProtKB/Swiss-Prot P60338 (EFTU1_THETH)

Names and origin

Protein names

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

Gene names

Name:	tufA
Synonyms:	tuf

Organism

Thermus thermophilus

Taxonomic identifier

274 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	406 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 MF_00118
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm. HAMAP MF_00118
Post-translational modification	Phosphorylated on a threonine By similarity.
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.
Caution	The sequence shown here has been extracted from PDB entry 1EXM.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding
Molecular function	Elongation factor
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	translational elongation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm 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 HAMAP MF_00118

Chain

2 – 406

405

Elongation factor Tu-A HAMAP MF_00118

PRO_0000091422

Regions

Nucleotide binding

19 – 26

8

GTP HAMAP MF_00118

Nucleotide binding

82 – 86

5

GTP HAMAP MF_00118

Nucleotide binding

137 – 140

4

GTP HAMAP MF_00118

Amino acid modifications

Modified residue

395

1

Phosphothreonine By similarity

Secondary structure

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406

Helix Strand Turn

Details...

Beta strand

12 – 18

7

Helix

25 – 39

15

Helix

48 – 51

4

Helix

55 – 60

6

Beta strand

67 – 72

6

Beta strand

77 – 82

6

Helix

87 – 89

3

Helix

90 – 97

8

Beta strand

101 – 108

8

Turn

109 – 111

3

Helix

115 – 126

12

Beta strand

132 – 137

6

Helix

139 – 141

3

Helix

145 – 161

17

Turn

166 – 168

3

Beta strand

171 – 173

3

Helix

176 – 185

10

Helix

195 – 210

16

Beta strand

223 – 225

3

Beta strand

228 – 232

5

Turn

233 – 235

3

Beta strand

236 – 242

7

Beta strand

245 – 249

5

Beta strand

253 – 262

10

Beta strand

264 – 273

10

Beta strand

279 – 282

4

Beta strand

286 – 291

6

Turn

296 – 298

3

Beta strand

304 – 307

4

Beta strand

314 – 323

10

Helix

326 – 328

3

Beta strand

342 – 345

4

Beta strand

348 – 355

8

Beta strand

368 – 379

12

Beta strand

386 – 391

6

Beta strand

394 – 404

11

Sequences

	Sequence		Length	Mass (Da)
	P60338-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: BA597518358269E4	FASTA	406	44,782
	10 20 30 40 50 60 MAKGEFVRTK PHVNVGTIGH VDHGKTTLTA ALTYVAAAEN PNVEVKDYGD IDKAPEERAR 70 80 90 100 110 120 GITINTAHVE YETAKRHYSH VDCPGHADYI KNMITGAAQM DGAILVVSAA DGPMPQTREH 130 140 150 160 170 180 ILLARQVGVP YIVVFMNKVD MVDDPELLDL VEMEVRDLLN QYEFPGDEVP VIRGSALLAL 190 200 210 220 230 240 EQMHRNPKTR RGENEWVDKI WELLDAIDEY IPTPVRDVDK PFLMPVEDVF TITGRGTVAT 250 260 270 280 290 300 GRIERGKVKV GDEVEIVGLA PETRRTVVTG VEMHRKTLQE GIAGDNVGVL LRGVSREEVE 310 320 330 340 350 360 RGQVLAKPGS ITPHTKFEAS VYVLKKEEGG RHTGFFSGYR PQFYFRTTDV TGVVQLPPGV 370 380 390 400 EMVMPGDNVT FTVELIKPVA LEEGLRFAIR EGGRTVGAGV VTKILE

References

[1]	"Crystal structure of active elongation factor Tu reveals major domain rearrangements." Berchtold H., Reshetnikova L., Reiser C.O.A., Schirmer N.K., Sprinzl M., Hilgenfeld R. Nature 365:126-132(1993) [PubMed: 8371755] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[2]	"Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus." Wang Y., Jiang Y., Meyering-Voss M., Sprinzl M., Sigler P.B. Nat. Struct. Biol. 4:650-656(1997) [PubMed: 9253415] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH EF-TS.
[3]	"The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA." Nissen P., Thirup S., Kjeldgaard M., Nyborg J. Structure 7:143-156(1999) [PubMed: 10368282] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

S00229.
S17146.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AIP	X-ray	3.00	A/B/E/F	2-406	[»]
1EXM	X-ray	1.70	A	2-406	[»]
1ZC8	electron microscopy	13.00	Y	2-406	[»]

ModBase

Search...

Family and domain databases

HAMAP

MF_00118.
[Tree]

InterPro

IPR000795. ProtSyn_GTP_bd.
IPR005225. Small_GTP_bd.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004541. Transl_elong_EFTu/EF1A_bac/org.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]

PANTHER

PTHR23115:SF31. Transl_elong_EFTu/EF1A_bac/org. 1 hit.

Pfam

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

PRINTS

PR00315. ELONGATNFCT.

TIGRFAMs

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

PROSITE

PS00301. EFACTOR_GTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

EFTU1_THETH

Accession

Primary (citable) accession number: P60338
Secondary accession number(s): P07157

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)