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Q5SHN6

- EFTU1_THET8

UniProt

Q5SHN6 - EFTU1_THET8

Protein

Elongation factor Tu-A

Gene

tufA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi19 – 268GTP
    Nucleotide bindingi82 – 865GTP
    Nucleotide bindingi137 – 1404GTP

    GO - Molecular functioni

    1. GTPase activity Source: InterPro
    2. GTP binding Source: UniProtKB-HAMAP
    3. translation elongation factor activity Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciTTHE300852:GH8R-1733-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor Tu-AUniRule annotation
    Short name:
    EF-Tu-AUniRule annotation
    Gene namesi
    Name:tufAUniRule annotation
    Synonyms:tuf
    Ordered Locus Names:TTHA1694
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000532: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 406405Elongation factor Tu-APRO_0000091423Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei395 – 3951Phosphothreonine1 Publication

    Post-translational modificationi

    Phosphorylated on a threonine.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ5SHN6.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi300852.TTHA1694.

    Structurei

    Secondary structure

    1
    406
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 187
    Beta strandi20 – 245
    Helixi25 – 3814
    Helixi48 – 514
    Helixi55 – 606
    Beta strandi67 – 726
    Beta strandi77 – 826
    Helixi87 – 893
    Helixi90 – 978
    Beta strandi101 – 1088
    Turni109 – 1113
    Helixi115 – 12612
    Beta strandi132 – 1376
    Helixi139 – 1413
    Helixi145 – 16117
    Turni166 – 1683
    Beta strandi171 – 1733
    Helixi176 – 18510
    Beta strandi191 – 1933
    Helixi195 – 21016
    Beta strandi218 – 2203
    Beta strandi223 – 2253
    Beta strandi228 – 2325
    Turni233 – 2353
    Beta strandi236 – 2427
    Beta strandi245 – 2495
    Beta strandi253 – 26210
    Beta strandi264 – 27310
    Beta strandi276 – 2827
    Beta strandi286 – 2938
    Turni296 – 2983
    Beta strandi304 – 3074
    Beta strandi310 – 32314
    Helixi326 – 3283
    Beta strandi342 – 3454
    Beta strandi348 – 3558
    Beta strandi357 – 3593
    Beta strandi365 – 3673
    Beta strandi368 – 38114
    Beta strandi386 – 3916
    Beta strandi394 – 40411

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HA3X-ray2.00A/B2-406[»]
    2C78X-ray1.40A2-406[»]
    2WRNX-ray3.60Z1-406[»]
    2WRQX-ray3.60Z1-406[»]
    2Y0UX-ray3.10Z2-406[»]
    2Y0WX-ray3.10Z2-406[»]
    2Y0YX-ray3.10Z2-406[»]
    2Y10X-ray3.10Z2-406[»]
    2Y12X-ray3.10Z2-406[»]
    2Y14X-ray3.10Z2-406[»]
    2Y16X-ray3.10Z2-406[»]
    2Y18X-ray3.10Z2-406[»]
    4ABRX-ray3.10Z2-406[»]
    ProteinModelPortaliQ5SHN6.
    SMRiQ5SHN6. Positions 10-406.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5SHN6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 215206tr-type GAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni19 – 268G1By similarity
    Regioni61 – 655G2By similarity
    Regioni82 – 854G3By similarity
    Regioni137 – 1404G4By similarity
    Regioni175 – 1773G5By similarity

    Sequence similaritiesi

    Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0050.
    HOGENOMiHOG000229290.
    KOiK02358.
    OMAiGTEMCMP.
    OrthoDBiEOG6R5C6X.
    PhylomeDBiQ5SHN6.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00118_B. EF_Tu_B.
    InterProiIPR000795. EF_GTP-bd_dom.
    IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR009000. Transl_B-barrel.
    IPR009001. Transl_elong_EF1A/Init_IF2_C.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    IPR004541. Transl_elong_EFTu/EF1A_bac/org.
    IPR004160. Transl_elong_EFTu/EF1A_C.
    [Graphical view]
    PfamiPF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    PF03143. GTP_EFTU_D3. 1 hit.
    [Graphical view]
    PRINTSiPR00315. ELONGATNFCT.
    SUPFAMiSSF50447. SSF50447. 1 hit.
    SSF50465. SSF50465. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00485. EF-Tu. 1 hit.
    TIGR00231. small_GTP. 1 hit.
    PROSITEiPS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q5SHN6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKGEFVRTK PHVNVGTIGH VDHGKTTLTA ALTYVAAAEN PNVEVKDYGD    50
    IDKAPEERAR GITINTAHVE YETAKRHYSH VDCPGHADYI KNMITGAAQM 100
    DGAILVVSAA DGPMPQTREH ILLARQVGVP YIVVFMNKVD MVDDPELLDL 150
    VEMEVRDLLN QYEFPGDEVP VIRGSALLAL EQMHRNPKTR RGENEWVDKI 200
    WELLDAIDEY IPTPVRDVDK PFLMPVEDVF TITGRGTVAT GRIERGKVKV 250
    GDEVEIVGLA PETRRTVVTG VEMHRKTLQE GIAGDNVGVL LRGVSREEVE 300
    RGQVLAKPGS ITPHTKFEAS VYVLKKEEGG RHTGFFSGYR PQFYFRTTDV 350
    TGVVQLPPGV EMVMPGDNVT FTVELIKPVA LEEGLRFAIR EGGRTVGAGV 400
    VTKILE 406
    Length:406
    Mass (Da):44,782
    Last modified:January 23, 2007 - v3
    Checksum:iBA597518358269E4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti380 – 3801A → G in CAA29397. (PubMed:3317278)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05977 Genomic DNA. Translation: CAA29397.1.
    X06657 Genomic DNA. Translation: CAA29856.1.
    AP008226 Genomic DNA. Translation: BAD71517.1.
    PIRiS00229.
    S17146.
    RefSeqiWP_011228847.1. NC_006461.1.
    YP_144960.1. NC_006461.1.

    Genome annotation databases

    EnsemblBacteriaiBAD71517; BAD71517; BAD71517.
    GeneIDi3167925.
    KEGGittj:TTHA1694.
    PATRICi23958343. VBITheThe93045_1664.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05977 Genomic DNA. Translation: CAA29397.1 .
    X06657 Genomic DNA. Translation: CAA29856.1 .
    AP008226 Genomic DNA. Translation: BAD71517.1 .
    PIRi S00229.
    S17146.
    RefSeqi WP_011228847.1. NC_006461.1.
    YP_144960.1. NC_006461.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HA3 X-ray 2.00 A/B 2-406 [» ]
    2C78 X-ray 1.40 A 2-406 [» ]
    2WRN X-ray 3.60 Z 1-406 [» ]
    2WRQ X-ray 3.60 Z 1-406 [» ]
    2Y0U X-ray 3.10 Z 2-406 [» ]
    2Y0W X-ray 3.10 Z 2-406 [» ]
    2Y0Y X-ray 3.10 Z 2-406 [» ]
    2Y10 X-ray 3.10 Z 2-406 [» ]
    2Y12 X-ray 3.10 Z 2-406 [» ]
    2Y14 X-ray 3.10 Z 2-406 [» ]
    2Y16 X-ray 3.10 Z 2-406 [» ]
    2Y18 X-ray 3.10 Z 2-406 [» ]
    4ABR X-ray 3.10 Z 2-406 [» ]
    ProteinModelPortali Q5SHN6.
    SMRi Q5SHN6. Positions 10-406.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 300852.TTHA1694.

    Proteomic databases

    PRIDEi Q5SHN6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD71517 ; BAD71517 ; BAD71517 .
    GeneIDi 3167925.
    KEGGi ttj:TTHA1694.
    PATRICi 23958343. VBITheThe93045_1664.

    Phylogenomic databases

    eggNOGi COG0050.
    HOGENOMi HOG000229290.
    KOi K02358.
    OMAi GTEMCMP.
    OrthoDBi EOG6R5C6X.
    PhylomeDBi Q5SHN6.

    Enzyme and pathway databases

    BioCyci TTHE300852:GH8R-1733-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q5SHN6.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    HAMAPi MF_00118_B. EF_Tu_B.
    InterProi IPR000795. EF_GTP-bd_dom.
    IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR009000. Transl_B-barrel.
    IPR009001. Transl_elong_EF1A/Init_IF2_C.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    IPR004541. Transl_elong_EFTu/EF1A_bac/org.
    IPR004160. Transl_elong_EFTu/EF1A_C.
    [Graphical view ]
    Pfami PF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    PF03143. GTP_EFTU_D3. 1 hit.
    [Graphical view ]
    PRINTSi PR00315. ELONGATNFCT.
    SUPFAMi SSF50447. SSF50447. 1 hit.
    SSF50465. SSF50465. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00485. EF-Tu. 1 hit.
    TIGR00231. small_GTP. 1 hit.
    PROSITEi PS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and identification of the nucleotide binding site for the elongation factor Tu from Thermus thermophilus HB8."
      Seidler L., Peter M., Meissner F., Sprinzl M.
      Nucleic Acids Res. 15:9263-9277(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Molecular cloning and sequence determination of the tuf gene coding for the elongation factor Tu of Thermus thermophilus HB8."
      Kushiro A., Shimizu M., Tomita K.
      Eur. J. Biochem. 170:93-98(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete genome sequence of Thermus thermophilus HB8."
      Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HB8 / ATCC 27634 / DSM 579.
    4. "Prokaryotic elongation factor Tu is phosphorylated in vivo."
      Lippmann C., Lindschau C., Vijgenboom E., Schroeder W., Bosch L., Erdmann V.A.
      J. Biol. Chem. 268:601-607(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    5. "Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox."
      Vogeley L., Palm G.J., Mesters J.R., Hilgenfeld R.
      J. Biol. Chem. 276:17149-17155(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF COMPLEX WITH GDP AND AURODOX.

    Entry informationi

    Entry nameiEFTU1_THET8
    AccessioniPrimary (citable) accession number: Q5SHN6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 82 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3