P0A6P1 (EFTS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongation factor Ts
Short name=EF-Ts

Gene names

Name:	tsf
Ordered Locus Names:	b0170, JW0165

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	283 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	Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. HAMAP-Rule MF_00050
Subunit structure	Heterotetramer composed of two EF-Ts.EF-Tu dimer complexes.
Subcellular location	Cytoplasm HAMAP-Rule MF_00050.
Sequence similarities	Belongs to the EF-Ts family.
Mass spectrometry	Molecular mass is 30294±6 Da from positions 2 - 283. Determined by ESI. Ref.10

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Molecular function	Elongation factor
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from direct assay PubMed 16858726. Source: UniProtKB membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	translation elongation factor activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from direct assay PubMed 11985624. Source: EcoliWiki
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
tufA	P0CE47	7	EBI-301164,EBI-301077

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7 Ref.8 Ref.9

Chain

2 – 283

282

Elongation factor Ts HAMAP-Rule MF_00050

PRO_0000161117

Regions

Region

80 – 83

4

Involved in Mg(2+) ion dislocation from EF-Tu HAMAP-Rule MF_00050

Experimental info

Mutagenesis

24

1

K → A: No change in binding to EF-Tu and in promoting GDP exchange. Ref.15

Mutagenesis

81

1

D → A: 2 to 3-fold less active in promoting GDP exchange and slightly lower binding constant for interaction with EF-Tu. Ref.15

Mutagenesis

82

1

F → A: 2 to 3-fold less active in promoting GDP exchange and 6-fold less active in binding to EF-Tu. Ref.15

Mutagenesis

148

1

H → A: At least 100-fold decrease in affinity between EF-Ts and EF-Tu and only small amount of GDP exchange activity. Ref.15

Secondary structure

1

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283

Helix Strand Turn

Details...

Helix

6 – 16

11

Helix

20 – 29

10

Turn

30 – 32

3

Helix

34 – 52

19

Beta strand

59 – 67

9

Beta strand

70 – 79

10

Helix

81 – 84

4

Helix

87 – 102

16

Helix

108 – 126

19

Beta strand

131 – 139

9

Beta strand

141 – 148

8

Turn

149 – 151

3

Beta strand

152 – 160

9

Helix

163 – 176

14

Beta strand

179 – 182

4

Helix

183 – 185

3

Helix

188 – 204

17

Helix

209 – 227

19

Turn

229 – 231

3

Beta strand

232 – 234

3

Beta strand

237 – 241

5

Helix

242 – 247

6

Turn

248 – 250

3

Beta strand

252 – 260

9

Turn

261 – 264

4

Helix

272 – 279

8

Sequences

	Sequence		Length	Mass (Da)
	P0A6P1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 0B9D21E928A5051C	FASTA	283	30,423
	10 20 30 40 50 60 MAEITASLVK ELRERTGAGM MDCKKALTEA NGDIELAIEN MRKSGAIKAA KKAGNVAADG 70 80 90 100 110 120 VIKTKIDGNY GIILEVNCQT DFVAKDAGFQ AFADKVLDAA VAGKITDVEV LKAQFEEERV 130 140 150 160 170 180 ALVAKIGENI NIRRVAALEG DVLGSYQHGA RIGVLVAAKG ADEELVKHIA MHVAASKPEF 190 200 210 220 230 240 IKPEDVSAEV VEKEYQVQLD IAMQSGKPKE IAEKMVEGRM KKFTGEVSLT GQPFVMEPSK 250 260 270 280 TVGQLLKEHN AEVTGFIRFE VGEGIEKVET DFAAEVAAMS KQS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization and nucleotide sequence of a new ribosomal operon in Escherichia coli containing the genes for ribosomal protein S2 and elongation factor Ts." An G., Bendiak D.S., Mamelak L.A., Friesen J.D. Nucleic Acids Res. 9:4163-4172(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Fujita N., Mori H., Yura T., Ishihama A. Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region." Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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.
[6]	"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.
[7]	Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. Submitted (SEP-1994) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-14. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]	"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 2-22. Strain: K12 / EMG2.
[9]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]	"Analysis and crystallization of a 25 kDa C-terminal fragment of cloned elongation factor Ts from Escherichia coli." Boegestrand S., Wiborg O., Thirup S., Nyborg J. FEBS Lett. 368:49-54(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 52-56, MASS SPECTROMETRY.
[11]	"Identification and characterization of the smbA gene, a suppressor of the mukB null mutant of Escherichia coli." Yamanaka K., Ogura T., Niki H., Hiraga S. J. Bacteriol. 174:7517-7526(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 179-283.
[12]	"Localization of the ribosome-releasing factor gene in the Escherichia coli chromosome." Ichikawa S., Ryoji M., Siegfried Z., Kaji A. J. Bacteriol. 171:3689-3695(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-275.
[13]	"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.
[14]	"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 COMPLEX WITH EF-TU.
[15]	"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 LYS-24; ASP-81; PHE-82 AND HIS-148.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00343 Genomic DNA. Translation: CAA23632.1.
D13334 Genomic DNA. Translation: BAA02597.1.
U00096 Genomic DNA. Translation: AAC73281.1.
AP009048 Genomic DNA. Translation: BAB96746.1.
U70214 Genomic DNA. Translation: AAB08599.1.

PIR

EFECS. A03525.

RefSeq

NP_414712.1. NC_000913.2.
YP_488472.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EFU	X-ray	2.50	B/D	2-283	[»]
3MMP	X-ray	2.50	A/C	1-283	[»]

ProteinModelPortal

P0A6P1.

SMR

P0A6P1. Positions 2-283.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31835N.

IntAct

P0A6P1. 10 interactions.

MINT

MINT-1273899.

STRING

511145.b0170.

PTM databases

PhosSite

P0810442.

2D gel databases

SWISS-2DPAGE

P0A6P1.

Proteomic databases

PaxDb

P0A6P1.

PRIDE

P0A6P1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73281; AAC73281; b0170.
BAB96746; BAB96746; BAB96746.

GeneID

12931801.
944866.

KEGG

ecj:Y75_p0166.
eco:b0170.

PATRIC

32115449. VBIEscCol129921_0176.

Organism-specific databases

EchoBASE

EB1026.

EcoGene

EG11033. tsf.

Phylogenomic databases

eggNOG

COG0264.

HOGENOM

HOG000220986.

KO

K02357.

OMA

YLHGTRI.

ProtClustDB

PRK09377.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11033-MONOMER.
ECOL316407:JW0165-MONOMER.

Gene expression databases

Genevestigator

P0A6P1.

Family and domain databases

Gene3D

3.30.479.20. 2 hits.

HAMAP

MF_00050. EF_Ts.

InterPro

IPR001816. Transl_elong_EFTs/EF1B.
IPR014039. Transl_elong_EFTs/EF1B_dimer.
IPR018101. Transl_elong_Ts_CS.
IPR009060. UBA-like.
IPR000449. UBA/transl_elong_EF1B_N.
[Graphical view]

PANTHER

PTHR11741. PTHR11741. 1 hit.

Pfam

PF00889. EF_TS. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]

SUPFAM

SSF54713. EF_TS. 2 hits.
SSF46934. UBA_like. 1 hit.

TIGRFAMs

TIGR00116. tsf. 1 hit.

PROSITE

PS01126. EF_TS_1. 1 hit.
PS01127. EF_TS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A6P1.

Entry information

Entry name

EFTS_ECOLI

Accession

Primary (citable) accession number: P0A6P1
Secondary accession number(s): P02997

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program