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P0A6P1

- EFTS_ECOLI

UniProt

P0A6P1 - EFTS_ECOLI

Protein

Elongation factor Ts

Gene

tsf

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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.

    GO - Molecular functioni

    1. guanyl-nucleotide exchange factor activity Source: EcoCyc
    2. protein binding Source: IntAct
    3. translation elongation factor activity Source: UniProtKB-HAMAP
    4. zinc ion binding Source: EcoliWiki

    GO - Biological processi

    1. positive regulation of GTPase activity Source: GOC

    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
    Gene namesi
    Name:tsf
    Ordered Locus Names:b0170, JW0165
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11033. tsf.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi24 – 241K → A: No change in binding to EF-Tu and in promoting GDP exchange. 1 Publication
    Mutagenesisi81 – 811D → A: 2 to 3-fold less active in promoting GDP exchange and slightly lower binding constant for interaction with EF-Tu. 1 Publication
    Mutagenesisi82 – 821F → A: 2 to 3-fold less active in promoting GDP exchange and 6-fold less active in binding to EF-Tu. 1 Publication
    Mutagenesisi148 – 1481H → A: At least 100-fold decrease in affinity between EF-Ts and EF-Tu and only small amount of GDP exchange activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 283282Elongation factor TsPRO_0000161117Add
    BLAST

    Proteomic databases

    PaxDbiP0A6P1.
    PRIDEiP0A6P1.

    2D gel databases

    SWISS-2DPAGEP0A6P1.

    PTM databases

    PhosSiteiP0810442.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A6P1.

    Interactioni

    Subunit structurei

    Heterotetramer composed of two EF-Ts.EF-Tu dimer complexes.

    Binary interactionsi

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

    Protein-protein interaction databases

    DIPiDIP-31835N.
    IntActiP0A6P1. 10 interactions.
    MINTiMINT-1273899.
    STRINGi511145.b0170.

    Structurei

    Secondary structure

    1
    283
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 1611
    Helixi20 – 2910
    Turni30 – 323
    Helixi34 – 5219
    Beta strandi59 – 679
    Beta strandi70 – 7910
    Helixi81 – 844
    Helixi87 – 10216
    Helixi108 – 12619
    Beta strandi131 – 1399
    Beta strandi141 – 1488
    Turni149 – 1513
    Beta strandi152 – 1609
    Helixi163 – 17614
    Beta strandi179 – 1824
    Helixi183 – 1853
    Helixi188 – 20417
    Helixi209 – 22719
    Turni229 – 2313
    Beta strandi232 – 2343
    Beta strandi237 – 2415
    Helixi242 – 2476
    Turni248 – 2503
    Beta strandi252 – 2609
    Turni261 – 2644
    Helixi272 – 2798

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EFUX-ray2.50B/D2-283[»]
    3MMPX-ray2.50A/C1-283[»]
    ProteinModelPortaliP0A6P1.
    SMRiP0A6P1. Positions 2-283.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6P1.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni80 – 834Involved in Mg(2+) ion dislocation from EF-Tu

    Sequence similaritiesi

    Belongs to the EF-Ts family.Curated

    Phylogenomic databases

    eggNOGiCOG0264.
    HOGENOMiHOG000220986.
    KOiK02357.
    OMAiNFVRLEV.
    OrthoDBiEOG66B42N.
    PhylomeDBiP0A6P1.

    Family and domain databases

    Gene3Di3.30.479.20. 2 hits.
    HAMAPiMF_00050. EF_Ts.
    InterProiIPR001816. Transl_elong_EFTs/EF1B.
    IPR014039. Transl_elong_EFTs/EF1B_dimer.
    IPR018101. Transl_elong_Ts_CS.
    IPR009060. UBA-like.
    IPR000449. UBA/Ts_N.
    [Graphical view]
    PANTHERiPTHR11741. PTHR11741. 1 hit.
    PfamiPF00889. EF_TS. 1 hit.
    PF00627. UBA. 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

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    MAEITASLVK ELRERTGAGM MDCKKALTEA NGDIELAIEN MRKSGAIKAA    50
    KKAGNVAADG VIKTKIDGNY GIILEVNCQT DFVAKDAGFQ AFADKVLDAA 100
    VAGKITDVEV LKAQFEEERV ALVAKIGENI NIRRVAALEG DVLGSYQHGA 150
    RIGVLVAAKG ADEELVKHIA MHVAASKPEF IKPEDVSAEV VEKEYQVQLD 200
    IAMQSGKPKE IAEKMVEGRM KKFTGEVSLT GQPFVMEPSK TVGQLLKEHN 250
    AEVTGFIRFE VGEGIEKVET DFAAEVAAMS KQS 283
    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:
    EMBL
    GenBank
    DDBJ
    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.
    YP_488472.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73281; AAC73281; b0170.
    BAB96746; BAB96746; BAB96746.
    GeneIDi12931801.
    944866.
    KEGGiecj:Y75_p0166.
    eco:b0170.
    PATRICi32115449. VBIEscCol129921_0176.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_488472.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EFU X-ray 2.50 B/D 2-283 [» ]
    3MMP X-ray 2.50 A/C 1-283 [» ]
    ProteinModelPortali P0A6P1.
    SMRi P0A6P1. Positions 2-283.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-31835N.
    IntActi P0A6P1. 10 interactions.
    MINTi MINT-1273899.
    STRINGi 511145.b0170.

    PTM databases

    PhosSitei P0810442.

    2D gel databases

    SWISS-2DPAGE P0A6P1.

    Proteomic databases

    PaxDbi P0A6P1.
    PRIDEi P0A6P1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73281 ; AAC73281 ; b0170 .
    BAB96746 ; BAB96746 ; BAB96746 .
    GeneIDi 12931801.
    944866.
    KEGGi ecj:Y75_p0166.
    eco:b0170.
    PATRICi 32115449. VBIEscCol129921_0176.

    Organism-specific databases

    EchoBASEi EB1026.
    EcoGenei EG11033. tsf.

    Phylogenomic databases

    eggNOGi COG0264.
    HOGENOMi HOG000220986.
    KOi K02357.
    OMAi NFVRLEV.
    OrthoDBi EOG66B42N.
    PhylomeDBi P0A6P1.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG11033-MONOMER.
    ECOL316407:JW0165-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A6P1.
    PROi P0A6P1.

    Gene expression databases

    Genevestigatori P0A6P1.

    Family and domain databases

    Gene3Di 3.30.479.20. 2 hits.
    HAMAPi MF_00050. EF_Ts.
    InterProi IPR001816. Transl_elong_EFTs/EF1B.
    IPR014039. Transl_elong_EFTs/EF1B_dimer.
    IPR018101. Transl_elong_Ts_CS.
    IPR009060. UBA-like.
    IPR000449. UBA/Ts_N.
    [Graphical view ]
    PANTHERi PTHR11741. PTHR11741. 1 hit.
    Pfami PF00889. EF_TS. 1 hit.
    PF00627. UBA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46934. SSF46934. 1 hit.
    SSF54713. SSF54713. 2 hits.
    TIGRFAMsi TIGR00116. tsf. 1 hit.
    PROSITEi PS01126. EF_TS_1. 1 hit.
    PS01127. EF_TS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Organization and nucleotide sequence of a new ribosomal operon in Escherichia coli containing the genes for ribosomal protein S2 and elongation factor Ts."
      An G., Bendiak D.S., Mamelak L.A., Friesen J.D.
      Nucleic Acids Res. 9:4163-4172(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
      Fujita N., Mori H., Yura T., Ishihama A.
      Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
      Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. Cited for: PROTEIN SEQUENCE OF 2-14.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-22.
      Strain: K12 / EMG2.
    9. Cited for: PROTEIN SEQUENCE OF 2-5.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    10. "Analysis and crystallization of a 25 kDa C-terminal fragment of cloned elongation factor Ts from Escherichia coli."
      Boegestrand S., Wiborg O., Thirup S., Nyborg J.
      FEBS Lett. 368:49-54(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 52-56, MASS SPECTROMETRY.
    11. "Identification and characterization of the smbA gene, a suppressor of the mukB null mutant of Escherichia coli."
      Yamanaka K., Ogura T., Niki H., Hiraga S.
      J. Bacteriol. 174:7517-7526(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 179-283.
    12. "Localization of the ribosome-releasing factor gene in the Escherichia coli chromosome."
      Ichikawa S., Ryoji M., Siegfried Z., Kaji A.
      J. Bacteriol. 171:3689-3695(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-275.
    13. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    14. "The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5-A resolution."
      Kawashima T., Berthet-Colominas C., Wulff M., Cusack S., Leberman R.
      Nature 379:511-518(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH EF-TU.
    15. "Mutational analysis of the roles of residues in Escherichia coli elongation factor Ts in the interaction with elongation factor Tu."
      Zhang Y., Yu N.-J., Spremulli L.L.
      J. Biol. Chem. 273:4556-4562(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-24; ASP-81; PHE-82 AND HIS-148.

    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: October 1, 2014
    This is version 100 of the entry and version 2 of the sequence. [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

    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

    External Data

    Dasty 3