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Protein

Elongation factor Ts

Gene

tsf

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.
In case of infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex. With EF-Tu may provide a stabilizing scaffold for the beta (catalytic) subunit, implicated in the elongation step of viral RNA synthesis where it fixes EF-Tu in an open conformation.6 Publications

Miscellaneous

In order to produce high amounts of bacteriophage Qbeta RNA polymerase catalytic core, a fusion protein consisting of tsf-tufB-replicase with a cleavable linker between tufB and the viral replicase subunit is frequently used.5 Publications

GO - Molecular functioni

  • guanyl-nucleotide exchange factor activity Source: EcoCyc
  • translation elongation factor activity Source: GO_Central
  • zinc ion binding Source: EcoliWiki

Keywordsi

Molecular functionElongation factor
Biological processProtein biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG11033-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor Ts
Short name:
EF-Ts
Alternative name(s):
Bacteriophage Q beta RNA-directed RNA polymerase subunit IV1 Publication
Gene namesi
Name:tsf
Ordered Locus Names:b0170, JW0165
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11033 tsf

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: EcoCyc
  • membrane Source: UniProtKB

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi24K → A: No change in binding to EF-Tu and in promoting GDP exchange. 1 Publication1
Mutagenesisi81D → A: 2 to 3-fold less active in promoting GDP exchange and slightly lower binding constant for interaction with EF-Tu. 1 Publication1
Mutagenesisi82F → A: 2 to 3-fold less active in promoting GDP exchange and 6-fold less active in binding to EF-Tu. 1 Publication1
Mutagenesisi148H → A: At least 100-fold decrease in affinity between EF-Ts and EF-Tu and only small amount of GDP exchange activity. 1 Publication1
Mutagenesisi188 – 227Missing : Still associates with EF-Tu, no longer forms the Qbeta viral RNA polymerase complex. 1 PublicationAdd BLAST40

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00001611172 – 283Elongation factor TsAdd BLAST282

Proteomic databases

EPDiP0A6P1
PaxDbiP0A6P1
PRIDEiP0A6P1

2D gel databases

SWISS-2DPAGEiP0A6P1

PTM databases

CarbonylDBiP0A6P1

Interactioni

Subunit structurei

Heterotetramer composed of two EF-Ts.EF-Tu dimer complexes. In case of infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex, the other subunits are the viral replicase catalytic subunit (AC P14647), host ribosomal protein S1 and EF-Tu (PubMed:816798).6 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • guanyl-nucleotide exchange factor activity Source: EcoCyc

Protein-protein interaction databases

BioGridi426079554 interactors.
DIPiDIP-31835N
IntActiP0A6P1 12 interactors.
STRINGi316385.ECDH10B_0150

Structurei

Secondary structure

1283
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 16Combined sources11
Helixi20 – 29Combined sources10
Turni30 – 32Combined sources3
Helixi34 – 52Combined sources19
Beta strandi59 – 67Combined sources9
Beta strandi70 – 79Combined sources10
Helixi81 – 85Combined sources5
Helixi87 – 103Combined sources17
Helixi108 – 126Combined sources19
Beta strandi131 – 139Combined sources9
Beta strandi141 – 148Combined sources8
Turni149 – 151Combined sources3
Beta strandi152 – 160Combined sources9
Helixi163 – 176Combined sources14
Beta strandi179 – 182Combined sources4
Helixi183 – 185Combined sources3
Helixi188 – 204Combined sources17
Helixi209 – 226Combined sources18
Turni229 – 231Combined sources3
Beta strandi232 – 234Combined sources3
Beta strandi237 – 241Combined sources5
Helixi242 – 248Combined sources7
Beta strandi252 – 260Combined sources9
Turni261 – 264Combined sources4
Helixi272 – 279Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EFUX-ray2.50B/D2-283[»]
3AGPX-ray2.80A1-283[»]
3AGQX-ray3.22A1-283[»]
3AVTX-ray2.61A1-283[»]
3AVUX-ray2.91A1-283[»]
3AVVX-ray3.12A1-283[»]
3AVWX-ray2.60A1-283[»]
3AVXX-ray2.41A1-283[»]
3AVYX-ray2.62A1-283[»]
3MMPX-ray2.50A/C1-283[»]
3VNUX-ray3.20A1-283[»]
3VNVX-ray2.60A1-283[»]
4FWTX-ray3.20A1-283[»]
4PC3X-ray1.83C/D2-283[»]
4PC7X-ray3.60C2-283[»]
4Q7JX-ray2.90A/E2-283[»]
4R71X-ray3.21A/C1-283[»]
ProteinModelPortaliP0A6P1
SMRiP0A6P1
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6P1

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni80 – 83Involved in Mg(2+) ion dislocation from EF-Tu4

Sequence similaritiesi

Belongs to the EF-Ts family.Curated

Phylogenomic databases

eggNOGiENOG4105CU7 Bacteria
COG0264 LUCA
HOGENOMiHOG000220986
InParanoidiP0A6P1
KOiK02357
OMAiDAGMMDC
PhylomeDBiP0A6P1

Family and domain databases

Gene3Di3.30.479.201 hit
HAMAPiMF_00050 EF_Ts, 1 hit
InterProiView protein in InterPro
IPR036402 EF-Ts_dimer_sf
IPR001816 Transl_elong_EFTs/EF1B
IPR014039 Transl_elong_EFTs/EF1B_dimer
IPR018101 Transl_elong_Ts_CS
IPR009060 UBA-like_sf
PANTHERiPTHR11741 PTHR11741, 1 hit
PfamiView protein in Pfam
PF00889 EF_TS, 1 hit
SUPFAMiSSF46934 SSF46934, 1 hit
SSF54713 SSF54713, 2 hits
TIGRFAMsiTIGR00116 tsf, 1 hit
PROSITEiView protein in PROSITE
PS01126 EF_TS_1, 1 hit
PS01127 EF_TS_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6P1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEITASLVK ELRERTGAGM MDCKKALTEA NGDIELAIEN MRKSGAIKAA
60 70 80 90 100
KKAGNVAADG VIKTKIDGNY GIILEVNCQT DFVAKDAGFQ AFADKVLDAA
110 120 130 140 150
VAGKITDVEV LKAQFEEERV ALVAKIGENI NIRRVAALEG DVLGSYQHGA
160 170 180 190 200
RIGVLVAAKG ADEELVKHIA MHVAASKPEF IKPEDVSAEV VEKEYQVQLD
210 220 230 240 250
IAMQSGKPKE IAEKMVEGRM KKFTGEVSLT GQPFVMEPSK TVGQLLKEHN
260 270 280
AEVTGFIRFE VGEGIEKVET DFAAEVAAMS KQS
Length:283
Mass (Da):30,423
Last modified:January 23, 2007 - v2
Checksum:i0B9D21E928A5051C
GO

Mass spectrometryi

Molecular mass is 30294±6 Da from positions 2 - 283. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
PIRiA03525 EFECS
RefSeqiNP_414712.1, NC_000913.3
WP_000818114.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73281; AAC73281; b0170
BAB96746; BAB96746; BAB96746
GeneIDi944866
KEGGiecj:JW0165
eco:b0170
PATRICifig|1411691.4.peg.2110

Similar proteinsi

Entry informationi

Entry nameiEFTS_ECOLI
AccessioniPrimary (citable) accession number: P0A6P1
Secondary accession number(s): P02997
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 129 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome