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P0A6N3

- EFTU_ECO57

UniProt

P0A6N3 - EFTU_ECO57

Protein

Elongation factor Tu

Gene

tufA

more
Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 2 (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.UniRule annotation
    May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi19 – 268GTPUniRule annotation
    Nucleotide bindingi81 – 855GTPUniRule annotation
    Nucleotide bindingi136 – 1394GTPUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. response to antibiotic Source: UniProtKB-KW

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Antibiotic resistance, Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciECOL386585:GJFA-4159-MONOMER.
    ECOL386585:GJFA-4902-MONOMER.
    ECOO157:TUFA-MONOMER.
    ECOO157:TUFB-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor TuUniRule annotation
    Short name:
    EF-TuUniRule annotation
    Alternative name(s):
    P-43
    Gene namesi
    Name:tufAUniRule annotation
    Ordered Locus Names:Z4697, ECs4190
    AND
    Name:tufBUniRule annotation
    Ordered Locus Names:Z5553, ECs4903
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 394393Elongation factor TuPRO_0000091321Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei57 – 571N6-methylated lysineBy similarity
    Modified residuei314 – 3141N6-acetyllysineBy similarity
    Modified residuei383 – 3831PhosphothreonineBy similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    PRIDEiP0A6N3.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    MINTiMINT-1234032.
    STRINGi155864.Z4697.

    Structurei

    Secondary structure

    1
    394
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 209
    Helixi21 – 233
    Helixi25 – 3915
    Beta strandi68 – 714
    Beta strandi76 – 816
    Helixi85 – 939
    Beta strandi94 – 963
    Beta strandi100 – 1078
    Turni108 – 1103
    Helixi116 – 12611
    Beta strandi131 – 1366
    Helixi138 – 1403
    Helixi144 – 16017
    Turni165 – 1673
    Beta strandi170 – 1723
    Turni176 – 1805
    Helixi183 – 19816
    Helixi206 – 2083
    Beta strandi212 – 2143
    Beta strandi217 – 2215
    Turni222 – 2243
    Beta strandi225 – 2317
    Beta strandi234 – 2385
    Beta strandi242 – 2509
    Beta strandi252 – 2609
    Beta strandi265 – 2706
    Beta strandi274 – 2818
    Helixi284 – 2863
    Beta strandi292 – 2954
    Turni296 – 2983
    Beta strandi301 – 31111
    Helixi314 – 3163
    Beta strandi330 – 3323
    Beta strandi334 – 3363
    Beta strandi337 – 3437
    Beta strandi358 – 36811
    Beta strandi374 – 3796
    Beta strandi382 – 39211

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3AGPX-ray2.80A1-394[»]
    3AGQX-ray3.22A1-394[»]
    3AVTX-ray2.61A1-394[»]
    3AVUX-ray2.91A1-394[»]
    3AVVX-ray3.12A1-394[»]
    3AVWX-ray2.60A1-394[»]
    3AVXX-ray2.41A1-394[»]
    3AVYX-ray2.62A1-394[»]
    3VNUX-ray3.20A1-394[»]
    3VNVX-ray2.60A1-394[»]
    4FWTX-ray3.20A1-394[»]
    ProteinModelPortaliP0A6N3.
    SMRiP0A6N3. Positions 9-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6N3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 204195tr-type GAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni19 – 268G1By similarity
    Regioni60 – 645G2By similarity
    Regioni81 – 844G3By similarity
    Regioni136 – 1394G4By similarity
    Regioni174 – 1763G5By 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.

    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.

    P0A6N3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI    50
    DNAPEEKARG ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD 100
    GAILVVAATD GPMPQTREHI LLGRQVGVPY IIVFLNKCDM VDDEELLELV 150
    EMEVRELLSQ YDFPGDDTPI VRGSALKALE GDAEWEAKIL ELAGFLDSYI 200
    PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG EEVEIVGIKE 250
    TQKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGTIK 300
    PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM 350
    VMPGDNIKMV VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLS 394
    Length:394
    Mass (Da):43,314
    Last modified:January 23, 2007 - v2
    Checksum:i6EDA60255F43358F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti394 – 3941S → G in tufA.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG58446.1.
    AE005174 Genomic DNA. Translation: AAG59176.1.
    BA000007 Genomic DNA. Translation: BAB37613.1.
    BA000007 Genomic DNA. Translation: BAB38326.1.
    PIRiB85998.
    G91241.
    RefSeqiNP_289886.1. NC_002655.2.
    NP_290611.1. NC_002655.2.
    NP_312217.1. NC_002695.1.
    NP_312930.1. NC_002695.1.

    Genome annotation databases

    EnsemblBacteriaiAAG58446; AAG58446; Z4697.
    AAG59176; AAG59176; Z5553.
    BAB37613; BAB37613; BAB37613.
    BAB38326; BAB38326; BAB38326.
    GeneIDi914959.
    915957.
    958801.
    960150.
    KEGGiece:Z4697.
    ece:Z5553.
    ecs:ECs4190.
    ecs:ECs4903.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG58446.1 .
    AE005174 Genomic DNA. Translation: AAG59176.1 .
    BA000007 Genomic DNA. Translation: BAB37613.1 .
    BA000007 Genomic DNA. Translation: BAB38326.1 .
    PIRi B85998.
    G91241.
    RefSeqi NP_289886.1. NC_002655.2.
    NP_290611.1. NC_002655.2.
    NP_312217.1. NC_002695.1.
    NP_312930.1. NC_002695.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3AGP X-ray 2.80 A 1-394 [» ]
    3AGQ X-ray 3.22 A 1-394 [» ]
    3AVT X-ray 2.61 A 1-394 [» ]
    3AVU X-ray 2.91 A 1-394 [» ]
    3AVV X-ray 3.12 A 1-394 [» ]
    3AVW X-ray 2.60 A 1-394 [» ]
    3AVX X-ray 2.41 A 1-394 [» ]
    3AVY X-ray 2.62 A 1-394 [» ]
    3VNU X-ray 3.20 A 1-394 [» ]
    3VNV X-ray 2.60 A 1-394 [» ]
    4FWT X-ray 3.20 A 1-394 [» ]
    ProteinModelPortali P0A6N3.
    SMRi P0A6N3. Positions 9-394.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1234032.
    STRINGi 155864.Z4697.

    Proteomic databases

    PRIDEi P0A6N3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG58446 ; AAG58446 ; Z4697 .
    AAG59176 ; AAG59176 ; Z5553 .
    BAB37613 ; BAB37613 ; BAB37613 .
    BAB38326 ; BAB38326 ; BAB38326 .
    GeneIDi 914959.
    915957.
    958801.
    960150.
    KEGGi ece:Z4697.
    ece:Z5553.
    ecs:ECs4190.
    ecs:ECs4903.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci ECOL386585:GJFA-4159-MONOMER.
    ECOL386585:GJFA-4902-MONOMER.
    ECOO157:TUFA-MONOMER.
    ECOO157:TUFB-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A6N3.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TUFA AND TUFB).
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TUFA AND TUFB).
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

    Entry informationi

    Entry nameiEFTU_ECO57
    AccessioniPrimary (citable) accession number: P0A6N3
    Secondary accession number(s): O68929
    , P02990, Q8X4S9, Q8XED3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 78 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This chain is also used in bacteriophage Q-beta RNA polymerase.By similarity
    The antibiotic kirromycin inhibits protein biosynthesis by inhibiting the release of EF-Tu from the ribosome.By similarity
    The antibiotic pulvomycin inhibits protein biosynthesis by disrupting the allosteric control mechanism of EF-Tu.By similarity
    The sequence of the tufB gene is shown. TufA differs in a single position By similarity.By similarity

    Keywords - Technical termi

    3D-structure, Complete 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