P0A6P1 · EFTS_ECOLI
- ProteinElongation factor Ts
- Genetsf
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids283 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
(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.
(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:28223500, 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:28223500, PubMed:28973472).
(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:28223500, 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:28223500, PubMed:28973472).
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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | guanyl-nucleotide exchange factor complex | |
Cellular Component | membrane | |
Molecular Function | guanyl-nucleotide exchange factor activity | |
Molecular Function | translation elongation factor activity | |
Molecular Function | zinc ion binding | |
Biological Process | translational elongation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameElongation factor Ts
- Short namesEF-Ts
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0A6P1
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 24 | No change in binding to EF-Tu and in promoting GDP exchange. | ||||
Sequence: K → A | ||||||
Mutagenesis | 81 | 2 to 3-fold less active in promoting GDP exchange and slightly lower binding constant for interaction with EF-Tu. | ||||
Sequence: D → A | ||||||
Mutagenesis | 82 | 2 to 3-fold less active in promoting GDP exchange and 6-fold less active in binding to EF-Tu. | ||||
Sequence: F → A | ||||||
Mutagenesis | 148 | At least 100-fold decrease in affinity between EF-Ts and EF-Tu and only small amount of GDP exchange activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 186-225 | 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. | ||||
Sequence: VSAEVVEKEYQVQLDIAMQSGKPKEIAEKMVEGRMKKFTG → EPGGEA | ||||||
Mutagenesis | 188-227 | Still associates with EF-Tu, no longer forms the Qbeta viral RNA polymerase complex. | ||||
Sequence: Missing | ||||||
Mutagenesis | 202 | 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. | ||||
Sequence: A → E | ||||||
Mutagenesis | 219 | 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. | ||||
Sequence: R → P |
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000161117 | 2-283 | Elongation factor Ts | |||
Sequence: AEITASLVKELRERTGAGMMDCKKALTEANGDIELAIENMRKSGAIKAAKKAGNVAADGVIKTKIDGNYGIILEVNCQTDFVAKDAGFQAFADKVLDAAVAGKITDVEVLKAQFEEERVALVAKIGENINIRRVAALEGDVLGSYQHGARIGVLVAAKGADEELVKHIAMHVAASKPEFIKPEDVSAEVVEKEYQVQLDIAMQSGKPKEIAEKMVEGRMKKFTGEVSLTGQPFVMEPSKTVGQLLKEHNAEVTGFIRFEVGEGIEKVETDFAAEVAAMSKQS |
Proteomic databases
PTM databases
Interaction
Subunit
Heterotetramer composed of two EF-Ts.EF-Tu dimer complexes.
(Microbial infection) 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).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P0A6P1 | P14647 | 2 | EBI-301164, EBI-9010000 | |
BINARY | P0A6P1 | tufA P0CE47 | 12 | EBI-301164, EBI-301077 | |
BINARY | P0A6P1 | tufB P0CE48 | 3 | EBI-301164, EBI-9010251 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 80-83 | Involved in Mg2+ ion dislocation from EF-Tu | ||||
Sequence: TDFV |
Sequence similarities
Belongs to the EF-Ts family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length283
- Mass (Da)30,423
- Last updated2007-01-23 v2
- Checksum0B9D21E928A5051C
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
V00343 EMBL· GenBank· DDBJ | CAA23632.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D13334 EMBL· GenBank· DDBJ | BAA02597.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC73281.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAB96746.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U70214 EMBL· GenBank· DDBJ | AAB08599.1 EMBL· GenBank· DDBJ | Genomic DNA |