Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0A6N2

- EFTU_ECOL6

UniProt

P0A6N2 - EFTU_ECOL6

Protein

Elongation factor Tu

Gene

tufA

more
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    BioCyciECOL199310:C4935-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:c4111
    AND
    Name:tufBUniRule annotation
    Ordered Locus Names:c4935
    OrganismiEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
    Taxonomic identifieri199310 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000001410: 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_0000091322Add
    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

    PRIDEiP0A6N2.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi199310.c4111.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A6N2.
    SMRiP0A6N2. Positions 9-394.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    HOGENOMiHOG000229290.
    KOiK02358.
    OMAiKEECENH.
    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.

    P0A6N2-1 [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

    Sequence cautioni

    The sequence AAN82549.1 differs from that shown. Reason: Erroneous initiation.

    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
    AE014075 Genomic DNA. Translation: AAN82549.1. Different initiation.
    AE014075 Genomic DNA. Translation: AAN83363.1.
    RefSeqiNP_755975.2. NC_004431.1.
    NP_756789.1. NC_004431.1.

    Genome annotation databases

    EnsemblBacteriaiAAN82549; AAN82549; c4111.
    AAN83363; AAN83363; c4935.
    GeneIDi1036191.
    1039881.
    KEGGiecc:c4111.
    ecc:c4935.
    PATRICi18285976. VBIEscCol75197_3864.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014075 Genomic DNA. Translation: AAN82549.1 . Different initiation.
    AE014075 Genomic DNA. Translation: AAN83363.1 .
    RefSeqi NP_755975.2. NC_004431.1.
    NP_756789.1. NC_004431.1.

    3D structure databases

    ProteinModelPortali P0A6N2.
    SMRi P0A6N2. Positions 9-394.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 199310.c4111.

    Proteomic databases

    PRIDEi P0A6N2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN82549 ; AAN82549 ; c4111 .
    AAN83363 ; AAN83363 ; c4935 .
    GeneIDi 1036191.
    1039881.
    KEGGi ecc:c4111.
    ecc:c4935.
    PATRICi 18285976. VBIEscCol75197_3864.

    Phylogenomic databases

    HOGENOMi HOG000229290.
    KOi K02358.
    OMAi KEECENH.
    OrthoDBi EOG6R5C6X.

    Enzyme and pathway databases

    BioCyci ECOL199310:C4935-MONOMER.

    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: CFT073 / ATCC 700928 / UPEC.

    Entry informationi

    Entry nameiEFTU_ECOL6
    AccessioniPrimary (citable) accession number: P0A6N2
    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 77 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

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3