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Protein

Elongation factor Ts

Gene

tsf

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

GO - Molecular functioni

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

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG11033-MONOMER.
ECOL316407:JW0165-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
Complete GO annotation...

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-2DPAGEP0A6P1.

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

WithEntry#Exp.IntActNotes
tufAP0CE477EBI-301164,EBI-301077

Protein-protein interaction databases

BioGridi4260795. 5 interactors.
DIPiDIP-31835N.
IntActiP0A6P1. 10 interactors.
MINTiMINT-1273899.
STRINGi511145.b0170.

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.
OMAiFIMEPKK.
PhylomeDBiP0A6P1.

Family and domain databases

Gene3Di3.30.479.20. 2 hits.
HAMAPiMF_00050. EF_Ts. 1 hit.
InterProiIPR001816. Transl_elong_EFTs/EF1B.
IPR014039. Transl_elong_EFTs/EF1B_dimer.
IPR018101. Transl_elong_Ts_CS.
IPR009060. UBA-like.
[Graphical view]
PANTHERiPTHR11741. PTHR11741. 1 hit.
PfamiPF00889. EF_TS. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54713. SSF54713. 2 hits.
TIGRFAMsiTIGR00116. tsf. 1 hit.
PROSITEiPS01126. EF_TS_1. 1 hit.
PS01127. EF_TS_2. 1 hit.
[Graphical view]

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.
PATRICi32115449. VBIEscCol129921_0176.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi4260795. 5 interactors.
DIPiDIP-31835N.
IntActiP0A6P1. 10 interactors.
MINTiMINT-1273899.
STRINGi511145.b0170.

2D gel databases

SWISS-2DPAGEP0A6P1.

Proteomic databases

EPDiP0A6P1.
PaxDbiP0A6P1.
PRIDEiP0A6P1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73281; AAC73281; b0170.
BAB96746; BAB96746; BAB96746.
GeneIDi944866.
KEGGiecj:JW0165.
eco:b0170.
PATRICi32115449. VBIEscCol129921_0176.

Organism-specific databases

EchoBASEiEB1026.
EcoGeneiEG11033. tsf.

Phylogenomic databases

eggNOGiENOG4105CU7. Bacteria.
COG0264. LUCA.
HOGENOMiHOG000220986.
InParanoidiP0A6P1.
KOiK02357.
OMAiFIMEPKK.
PhylomeDBiP0A6P1.

Enzyme and pathway databases

BioCyciEcoCyc:EG11033-MONOMER.
ECOL316407:JW0165-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A6P1.
PROiP0A6P1.

Family and domain databases

Gene3Di3.30.479.20. 2 hits.
HAMAPiMF_00050. EF_Ts. 1 hit.
InterProiIPR001816. Transl_elong_EFTs/EF1B.
IPR014039. Transl_elong_EFTs/EF1B_dimer.
IPR018101. Transl_elong_Ts_CS.
IPR009060. UBA-like.
[Graphical view]
PANTHERiPTHR11741. PTHR11741. 1 hit.
PfamiPF00889. EF_TS. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54713. SSF54713. 2 hits.
TIGRFAMsiTIGR00116. tsf. 1 hit.
PROSITEiPS01126. EF_TS_1. 1 hit.
PS01127. EF_TS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEFTS_ECOLI
AccessioniPrimary (citable) accession number: P0A6P1
Secondary accession number(s): P02997
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.