UniProtKB - P0A6P1 (EFTS_ECOLI)
Elongation factor Ts
tsf
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.
UniRule annotation(Microbial infection) In case of infection by bacteriophage Qbeta (and related Leviviruses), 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(Microbial infection) Promotes the tRNase activity of CdiA-CT from E.coli strain EC869 (CdiA-CT-EC869); required in vivo but less so in vitro. Probably loads charged tRNA onto EF-Tu, making more ternary GTP-EF-Tu-aa-tRNA complexes. The guanine nucleotide exchange factor capacity of this protein does not seem to be needed as no GTP hydrolysis occurs during tRNA cleavage. Also required in vivo for toxic activity of CdiA-CT from E.coli strains NC101 and CdiA-CT-96.154. CdiA-CT is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (PubMed:28223500).
EF-Ts interacts with at least 2 different toxic CT domains, the 2 toxins are different and degrade tRNA at different positions (PubMed:28973472, PubMed:28223500).
2 Publications(Microbial infection) Promotes the tRNase activity of CdiA-CT from E.coli strain NC101 (CdiA-CT-NC101); required in vivo and in vitro. Probably loads charged tRNA onto EF-Tu, making more ternary GTP-EF-Tu-aa-tRNA complexes. The guanine nucleotide exchange factor capacity of this protein does not seem to be needed as no GTP hydrolysis occurs during tRNA cleavage. CdiA-CT is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (PubMed:28973472).
EF-Ts interacts with at least 2 different toxic CT domains, the 2 toxins are different and degrade tRNA at different positions (PubMed:28973472, PubMed:28223500).
2 PublicationsMiscellaneous
GO - Molecular functioni
- guanyl-nucleotide exchange factor activity Source: EcoCyc
- translation elongation factor activity Source: GO_Central
- zinc ion binding Source: EcoliWiki
GO - Biological processi
- translational elongation Source: GO_Central
Keywordsi
Molecular function | Elongation factor |
Biological process | Protein biosynthesis |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11033-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: Elongation factor TsUniRule annotationShort name: EF-TsUniRule annotation Alternative name(s): Bacteriophage Q beta RNA-directed RNA polymerase subunit IV1 Publication |
Gene namesi | Name:tsfUniRule annotation Ordered Locus Names:b0170, JW0165 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation
Cytosol
- cytosol Source: EcoCyc
Other locations
- cytoplasm Source: UniProtKB
- guanyl-nucleotide exchange factor complex Source: ComplexPortal
- membrane Source: UniProtKB
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 24 | K → A: No change in binding to EF-Tu and in promoting GDP exchange. 1 Publication | 1 | |
Mutagenesisi | 81 | D → A: 2 to 3-fold less active in promoting GDP exchange and slightly lower binding constant for interaction with EF-Tu. 1 Publication | 1 | |
Mutagenesisi | 82 | F → A: 2 to 3-fold less active in promoting GDP exchange and 6-fold less active in binding to EF-Tu. 1 Publication | 1 | |
Mutagenesisi | 148 | H → A: At least 100-fold decrease in affinity between EF-Ts and EF-Tu and only small amount of GDP exchange activity. 1 Publication | 1 | |
Mutagenesisi | 186 – 225 | VSAEV…KKFTG → EPGGEA: Resistant to toxins CdiA-CT-EC869, CdiA-CT-NC101 and CdiA-CT-96.154, but not other CdiA toxins in growth competition experiments, in vitro prevents CdiA-CT-EC869 from digesting tRNA(GUG-Gln). Resistant to bacteriophage R17. 1 PublicationAdd BLAST | 40 | |
Mutagenesisi | 188 – 227 | Missing : Still associates with EF-Tu, no longer forms the Qbeta viral RNA polymerase complex. 1 PublicationAdd BLAST | 40 | |
Mutagenesisi | 202 | A → E: Resistant to toxin CdiA-CT-EC869, partially resistant to toxins CdiA-CT-NC101 and CdiA-CT-96.154, but not resistant to other CdiA toxins in growth competition experiments, in vitro prevents CdiA-CT-EC869 from digesting tRNA(GUG-Gln). Partially resistant to bacteriophage R17. 1 Publication | 1 | |
Mutagenesisi | 219 | R → P: Resistant to toxin CdiA-CT-EC869, partially resistant to toxins CdiA-CT-NC101 and CdiA-CT-96.154, but not resistant to other CdiA toxins in growth competition experiments. Resistant to bacteriophage R17. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed3 Publications | |||
ChainiPRO_0000161117 | 2 – 283 | Elongation factor TsAdd BLAST | 282 |
Proteomic databases
jPOSTi | P0A6P1 |
PaxDbi | P0A6P1 |
PRIDEi | P0A6P1 |
2D gel databases
SWISS-2DPAGEi | P0A6P1 |
PTM databases
CarbonylDBi | P0A6P1 |
Interactioni
Subunit structurei
Heterotetramer composed of two EF-Ts.EF-Tu dimer complexes.
1 PublicationBinary interactionsi
P0A6P1
With | #Exp. | IntAct |
---|---|---|
tufA [P0CE47] | 12 | EBI-301164,EBI-301077 |
tufB [P0CE48] | 3 | EBI-301164,EBI-9010251 |
P14647 from Escherichia virus Qbeta. | 2 | EBI-301164,EBI-9010000 |
Protein-protein interaction databases
BioGRIDi | 4260795, 54 interactors |
ComplexPortali | CPX-2853, Elongation Factor TU-TS, tufB variant CPX-6035, Elongation Factor TU-TS, tufA variant |
DIPi | DIP-31835N |
IntActi | P0A6P1, 12 interactors |
STRINGi | 511145.b0170 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P0A6P1 |
SMRi | P0A6P1 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A6P1 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 80 – 83 | Involved in Mg(2+) ion dislocation from EF-TuUniRule annotation | 4 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0264, Bacteria |
HOGENOMi | CLU_047155_0_2_6 |
InParanoidi | P0A6P1 |
OMAi | DAGMMDC |
PhylomeDBi | P0A6P1 |
Family and domain databases
Gene3Di | 3.30.479.20, 2 hits |
HAMAPi | MF_00050, EF_Ts, 1 hit |
InterProi | View 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 |
PANTHERi | PTHR11741, PTHR11741, 1 hit |
Pfami | View protein in Pfam PF00889, EF_TS, 1 hit |
SUPFAMi | SSF46934, SSF46934, 1 hit SSF54713, SSF54713, 2 hits |
TIGRFAMsi | TIGR00116, tsf, 1 hit |
PROSITEi | View protein in PROSITE PS01126, EF_TS_1, 1 hit PS01127, EF_TS_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Mass spectrometryi
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 |
PIRi | A03525, EFECS |
RefSeqi | NP_414712.1, NC_000913.3 WP_000818114.1, NZ_STEB01000032.1 |
Genome annotation databases
EnsemblBacteriai | AAC73281; AAC73281; b0170 BAB96746; BAB96746; BAB96746 |
GeneIDi | 66671542 944866 |
KEGGi | ecj:JW0165 eco:b0170 |
PATRICi | fig|1411691.4.peg.2110 |
Similar proteinsi
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 |
PIRi | A03525, EFECS |
RefSeqi | NP_414712.1, NC_000913.3 WP_000818114.1, NZ_STEB01000032.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1EFU | X-ray | 2.50 | B/D | 2-283 | [»] | |
3AGP | X-ray | 2.80 | A | 1-283 | [»] | |
3AGQ | X-ray | 3.22 | A | 1-283 | [»] | |
3AVT | X-ray | 2.61 | A | 1-283 | [»] | |
3AVU | X-ray | 2.91 | A | 1-283 | [»] | |
3AVV | X-ray | 3.12 | A | 1-283 | [»] | |
3AVW | X-ray | 2.60 | A | 1-283 | [»] | |
3AVX | X-ray | 2.41 | A | 1-283 | [»] | |
3AVY | X-ray | 2.62 | A | 1-283 | [»] | |
3MMP | X-ray | 2.50 | A/C | 1-283 | [»] | |
3VNU | X-ray | 3.20 | A | 1-283 | [»] | |
3VNV | X-ray | 2.60 | A | 1-283 | [»] | |
4FWT | X-ray | 3.20 | A | 1-283 | [»] | |
4PC3 | X-ray | 1.83 | C/D | 2-283 | [»] | |
4PC7 | X-ray | 3.60 | C | 2-283 | [»] | |
4Q7J | X-ray | 2.90 | A/E | 2-283 | [»] | |
4R71 | X-ray | 3.21 | A/C | 1-283 | [»] | |
AlphaFoldDBi | P0A6P1 | |||||
SMRi | P0A6P1 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260795, 54 interactors |
ComplexPortali | CPX-2853, Elongation Factor TU-TS, tufB variant CPX-6035, Elongation Factor TU-TS, tufA variant |
DIPi | DIP-31835N |
IntActi | P0A6P1, 12 interactors |
STRINGi | 511145.b0170 |
PTM databases
CarbonylDBi | P0A6P1 |
2D gel databases
SWISS-2DPAGEi | P0A6P1 |
Proteomic databases
jPOSTi | P0A6P1 |
PaxDbi | P0A6P1 |
PRIDEi | P0A6P1 |
Genome annotation databases
EnsemblBacteriai | AAC73281; AAC73281; b0170 BAB96746; BAB96746; BAB96746 |
GeneIDi | 66671542 944866 |
KEGGi | ecj:JW0165 eco:b0170 |
PATRICi | fig|1411691.4.peg.2110 |
Organism-specific databases
EchoBASEi | EB1026 |
Phylogenomic databases
eggNOGi | COG0264, Bacteria |
HOGENOMi | CLU_047155_0_2_6 |
InParanoidi | P0A6P1 |
OMAi | DAGMMDC |
PhylomeDBi | P0A6P1 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11033-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P0A6P1 |
PROi | PR:P0A6P1 |
Family and domain databases
Gene3Di | 3.30.479.20, 2 hits |
HAMAPi | MF_00050, EF_Ts, 1 hit |
InterProi | View 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 |
PANTHERi | PTHR11741, PTHR11741, 1 hit |
Pfami | View protein in Pfam PF00889, EF_TS, 1 hit |
SUPFAMi | SSF46934, SSF46934, 1 hit SSF54713, SSF54713, 2 hits |
TIGRFAMsi | TIGR00116, tsf, 1 hit |
PROSITEi | View protein in PROSITE PS01126, EF_TS_1, 1 hit PS01127, EF_TS_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | EFTS_ECOLI | |
Accessioni | P0A6P1Primary (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: | May 25, 2022 | |
This is version 151 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families