Reviewed, UniProtKB/Swiss-Prot P43895 (EFTS_THET8)

Names and origin

Protein names

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

Gene names

Name:	tsf
Ordered Locus Names:	TTHA0860

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Complete proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	196 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 MF_00050
Subunit structure	Heterotetramer composed of two EF-Ts.EF-Tu dimer complex. HAMAP MF_00050
Subcellular location	Cytoplasm. HAMAP MF_00050
Sequence similarities	Belongs to the EF-Ts family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Molecular function	Elongation factor
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	translational elongation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	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

Chain

1 – 196

196

Elongation factor Ts HAMAP MF_00050

PRO_0000161222

Regions

Region

80 – 83

4

Involved in Mg(2+) ion dislocation from EF-Tu By similarity

Secondary structure

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196

Helix Strand Turn

Details...

Helix

3 – 14

12

Helix

18 – 27

10

Turn

28 – 30

3

Helix

32 – 50

19

Beta strand

57 – 64

8

Beta strand

68 – 79

12

Helix

81 – 85

5

Helix

87 – 103

17

Beta strand

106 – 109

4

Helix

110 – 112

3

Helix

115 – 130

16

Turn

131 – 133

3

Helix

136 – 154

19

Helix

156 – 158

3

Beta strand

159 – 161

3

Beta strand

164 – 168

5

Helix

169 – 180

12

Beta strand

185 – 193

9

Sequences

	Sequence		Length	Mass (Da)
	P43895-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 36A771F686BBB0DD	FASTA	196	22,413
	10 20 30 40 50 60 MSQMELIKKL REATGAGMMD VKRALEDAGW DEEKAVQLLR ERGAMKAAKK ADREAREGII 70 80 90 100 110 120 GHYIHHNQRV GVLVELNCET DFVARNELFQ NLAKDLAMHI AMMNPRYVSA EEIPAEELEK 130 140 150 160 170 180 ERQIYIQAAL NEGKPQQIAE KIAEGRLKKY LEEVVLLEQP FVKDDKVKVK ELIQQAIAKI 190 GENIVVRRFC RFELGA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Elongation factor Ts from Thermus thermophilus -- overproduction in Escherichia coli, quaternary structure and interaction with elongation factor Tu." Blank J., Nock S., Kreutzer R., Sprinzl M. Eur. J. Biochem. 236:222-227(1996) [PubMed: 8617268] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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-TU.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X83598 Genomic DNA. Translation: CAA58578.1.
AP008226 Genomic DNA. Translation: BAD70683.1.

RefSeq

YP_144126.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AIP	X-ray	3.00	C/D/G/H	1-196	[»]
1TFE	X-ray	1.70	A	55-196	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6078N.

STRING

P43895.

Genome annotation databases

GeneID

3170120.

GenomeReviews

Gene locus TTHA0860 in contig AP008226_GR.

KEGG

ttj:TTHA0860.

NMPDR

fig|300852.3.peg.917.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P43895.

OMA

MMDVKRA.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA0860-MON.

Family and domain databases

HAMAP

MF_00050.
[Tree]

InterPro

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

Gene3D

G3DSA:3.30.479.20. Transl_elong_EFTs/EF1B_dimer. 1 hit.

PANTHER

PTHR11741. Transl_elong_EFTs/EF1B. 1 hit.

Pfam

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

TIGRFAMs

TIGR00116. tsf. 1 hit.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

EFTS_THET8

Accession

Primary (citable) accession number: P43895
Secondary accession number(s): Q5SJZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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