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Q5SHN5

- EFG_THET8

UniProt

Q5SHN5 - EFG_THET8

Protein

Elongation factor G

Gene

fusA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi19 – 268GTPBy similarity
    Nucleotide bindingi83 – 875GTPBy similarity
    Nucleotide bindingi137 – 1404GTPBy similarity

    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-1734-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor G
    Short name:
    EF-G
    Gene namesi
    Name:fusA
    Synonyms:fus
    Ordered Locus Names:TTHA1695
    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
    Chaini1 – 691691Elongation factor GPRO_0000091249Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi300852.TTHA1695.

    Structurei

    Secondary structure

    1
    691
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 113
    Beta strandi12 – 198
    Helixi21 – 244
    Helixi25 – 3612
    Turni37 – 415
    Helixi49 – 513
    Helixi57 – 604
    Beta strandi69 – 746
    Beta strandi77 – 826
    Helixi88 – 903
    Helixi91 – 10010
    Beta strandi102 – 1098
    Turni110 – 1123
    Helixi116 – 12712
    Beta strandi132 – 1376
    Helixi146 – 15510
    Beta strandi161 – 1633
    Beta strandi165 – 1695
    Helixi171 – 1733
    Beta strandi176 – 1794
    Turni180 – 1834
    Beta strandi184 – 1885
    Beta strandi190 – 1945
    Beta strandi196 – 1994
    Helixi203 – 2053
    Helixi206 – 22015
    Turni221 – 2233
    Helixi225 – 2339
    Helixi239 – 25113
    Beta strandi256 – 2605
    Helixi263 – 2653
    Helixi269 – 27911
    Turni283 – 2853
    Beta strandi289 – 2924
    Beta strandi294 – 2963
    Beta strandi298 – 3014
    Beta strandi310 – 31910
    Turni320 – 3223
    Beta strandi323 – 33816
    Beta strandi340 – 3434
    Turni344 – 3463
    Beta strandi349 – 3513
    Beta strandi354 – 3585
    Beta strandi363 – 3708
    Beta strandi374 – 3785
    Beta strandi388 – 3914
    Beta strandi409 – 4179
    Helixi418 – 4203
    Turni426 – 4338
    Beta strandi436 – 4383
    Beta strandi439 – 4413
    Beta strandi444 – 4463
    Beta strandi449 – 4546
    Helixi458 – 4636
    Beta strandi464 – 4674
    Beta strandi470 – 4734
    Turni474 – 4763
    Beta strandi484 – 4863
    Beta strandi491 – 4999
    Beta strandi502 – 5043
    Beta strandi506 – 51611
    Beta strandi523 – 5275
    Beta strandi531 – 5344
    Turni536 – 5383
    Helixi539 – 54911
    Turni554 – 5563
    Beta strandi562 – 5709
    Turni574 – 5763
    Helixi579 – 59517
    Beta strandi600 – 61213
    Turni614 – 6185
    Helixi619 – 6268
    Beta strandi631 – 6377
    Beta strandi640 – 6489
    Turni649 – 6513
    Beta strandi652 – 6543
    Helixi655 – 6628
    Turni663 – 6653
    Beta strandi668 – 67811
    Helixi681 – 6888

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DARX-ray2.40A1-691[»]
    1EFGX-ray2.70A1-691[»]
    1ELOX-ray2.80A1-691[»]
    1ZN0electron microscopy15.50B6-688[»]
    2EFGX-ray2.60A1-691[»]
    2WRIX-ray3.60Y1-691[»]
    2WRKX-ray3.60Y1-691[»]
    2XSYelectron microscopy7.80Y1-691[»]
    2XUYelectron microscopy7.60Y1-691[»]
    4B8FX-ray3.70Y1-691[»]
    4B8HX-ray3.70Y1-691[»]
    4CR1X-ray2.95Y1-691[»]
    4JUWX-ray2.86Y10-689[»]
    ProteinModelPortaliQ5SHN5.
    SMRiQ5SHN5. Positions 4-689.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5SHN5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 284275tr-type GAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0480.
    HOGENOMiHOG000231587.
    KOiK02355.
    OMAiSGVQPQT.
    OrthoDBiEOG6X6RBF.
    PhylomeDBiQ5SHN5.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.30.70.240. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_00054_B. EF_G_EF_2_B.
    InterProiIPR000795. EF_GTP-bd_dom.
    IPR009022. EFG_III-V.
    IPR000640. EFG_V.
    IPR027417. P-loop_NTPase.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR005225. Small_GTP-bd_dom.
    IPR009000. Transl_B-barrel.
    IPR004540. Transl_elong_EFG/EF2.
    IPR005517. Transl_elong_EFG/EF2_IV.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    [Graphical view]
    PfamiPF00679. EFG_C. 1 hit.
    PF14492. EFG_II. 1 hit.
    PF03764. EFG_IV. 1 hit.
    PF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    [Graphical view]
    PRINTSiPR00315. ELONGATNFCT.
    SMARTiSM00838. EFG_C. 1 hit.
    SM00889. EFG_IV. 1 hit.
    [Graphical view]
    SUPFAMiSSF50447. SSF50447. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF54980. SSF54980. 2 hits.
    TIGRFAMsiTIGR00484. EF-G. 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.

    Q5SHN5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVKVEYDLK RLRNIGIAAH IDAGKTTTTE RILYYTGRIH KIGEVHEGAA    50
    TMDFMEQERE RGITITAAVT TCFWKDHRIN IIDTPGHVDF TIEVERSMRV 100
    LDGAIVVFDS SQGVEPQSET VWRQAEKYKV PRIAFANKMD KTGADLWLVI 150
    RTMQERLGAR PVVMQLPIGR EDTFSGIIDV LRMKAYTYGN DLGTDIREIP 200
    IPEEYLDQAR EYHEKLVEVA ADFDENIMLK YLEGEEPTEE ELVAAIRKGT 250
    IDLKITPVFL GSALKNKGVQ LLLDAVVDYL PSPLDIPPIK GTTPEGEVVE 300
    IHPDPNGPLA ALAFKIMADP YVGRLTFIRV YSGTLTSGSY VYNTTKGRKE 350
    RVARLLRMHA NHREEVEELK AGDLGAVVGL KETITGDTLV GEDAPRVILE 400
    SIEVPEPVID VAIEPKTKAD QEKLSQALAR LAEEDPTFRV STHPETGQTI 450
    ISGMGELHLE IIVDRLKREF KVDANVGKPQ VAYRETITKP VDVEGKFIRQ 500
    TGGRGQYGHV KIKVEPLPRG SGFEFVNAIV GGVIPKEYIP AVQKGIEEAM 550
    QSGPLIGFPV VDIKVTLYDG SYHEVDSSEM AFKIAGSMAI KEAVQKGDPV 600
    ILEPIMRVEV TTPEEYMGDV IGDLNARRGQ ILGMEPRGNA QVIRAFVPLA 650
    EMFGYATDLR SKTQGRGSFV MFFDHYQEVP KQVQEKLIKG Q 691
    Length:691
    Mass (Da):76,879
    Last modified:December 21, 2004 - v1
    Checksum:i8F0063EE8123470E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16278 Genomic DNA. Translation: CAA34354.1.
    AP008226 Genomic DNA. Translation: BAD71518.1.
    X52165 Genomic DNA. Translation: CAA36420.1.
    PIRiS15928. EFTWG.
    RefSeqiWP_011228848.1. NC_006461.1.
    YP_144961.1. NC_006461.1.

    Genome annotation databases

    EnsemblBacteriaiBAD71518; BAD71518; BAD71518.
    GeneIDi3169680.
    KEGGittj:TTHA1695.
    PATRICi23958345. VBITheThe93045_1665.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16278 Genomic DNA. Translation: CAA34354.1 .
    AP008226 Genomic DNA. Translation: BAD71518.1 .
    X52165 Genomic DNA. Translation: CAA36420.1 .
    PIRi S15928. EFTWG.
    RefSeqi WP_011228848.1. NC_006461.1.
    YP_144961.1. NC_006461.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DAR X-ray 2.40 A 1-691 [» ]
    1EFG X-ray 2.70 A 1-691 [» ]
    1ELO X-ray 2.80 A 1-691 [» ]
    1ZN0 electron microscopy 15.50 B 6-688 [» ]
    2EFG X-ray 2.60 A 1-691 [» ]
    2WRI X-ray 3.60 Y 1-691 [» ]
    2WRK X-ray 3.60 Y 1-691 [» ]
    2XSY electron microscopy 7.80 Y 1-691 [» ]
    2XUY electron microscopy 7.60 Y 1-691 [» ]
    4B8F X-ray 3.70 Y 1-691 [» ]
    4B8H X-ray 3.70 Y 1-691 [» ]
    4CR1 X-ray 2.95 Y 1-691 [» ]
    4JUW X-ray 2.86 Y 10-689 [» ]
    ProteinModelPortali Q5SHN5.
    SMRi Q5SHN5. Positions 4-689.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 300852.TTHA1695.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD71518 ; BAD71518 ; BAD71518 .
    GeneIDi 3169680.
    KEGGi ttj:TTHA1695.
    PATRICi 23958345. VBITheThe93045_1665.

    Phylogenomic databases

    eggNOGi COG0480.
    HOGENOMi HOG000231587.
    KOi K02355.
    OMAi SGVQPQT.
    OrthoDBi EOG6X6RBF.
    PhylomeDBi Q5SHN5.

    Enzyme and pathway databases

    BioCyci TTHE300852:GH8R-1734-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q5SHN5.
    PROi Q5SHN5.

    Family and domain databases

    Gene3Di 3.30.230.10. 1 hit.
    3.30.70.240. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPi MF_00054_B. EF_G_EF_2_B.
    InterProi IPR000795. EF_GTP-bd_dom.
    IPR009022. EFG_III-V.
    IPR000640. EFG_V.
    IPR027417. P-loop_NTPase.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR005225. Small_GTP-bd_dom.
    IPR009000. Transl_B-barrel.
    IPR004540. Transl_elong_EFG/EF2.
    IPR005517. Transl_elong_EFG/EF2_IV.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    [Graphical view ]
    Pfami PF00679. EFG_C. 1 hit.
    PF14492. EFG_II. 1 hit.
    PF03764. EFG_IV. 1 hit.
    PF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    [Graphical view ]
    PRINTSi PR00315. ELONGATNFCT.
    SMARTi SM00838. EFG_C. 1 hit.
    SM00889. EFG_IV. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50447. SSF50447. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF54980. SSF54980. 2 hits.
    TIGRFAMsi TIGR00484. EF-G. 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. "Nucleotide sequence of the Thermus thermophilus HB8 gene coding for elongation factor G."
      Yakhnin A.V., Vorozheykina D.P., Matvienko N.I.
      Nucleic Acids Res. 17:8863-8863(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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.
    3. "Nucleotide sequence of the Thermus thermophilus HB8 rps12 and rps7 genes coding for the ribosomal proteins S12 and S7."
      Yakhnin A.V., Vorozheykina D.P., Matvienko N.I.
      Nucleic Acids Res. 18:3659-3659(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
    4. "The crystal structure of elongation factor G complexed with GDP, at 2.7-A resolution."
      Czworkowski J., Wang J., Steitz T.A., Moore P.B.
      EMBO J. 13:3661-3668(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    5. "Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus."
      Aevarsson A., Brazhnikov E., Garber M., Zheltonosova J., Chirgadze Y., Al-Karadaghi S., Svensson L.A., Liljas A.
      EMBO J. 13:3669-3677(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS).

    Entry informationi

    Entry nameiEFG_THET8
    AccessioniPrimary (citable) accession number: Q5SHN5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2005
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 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