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F0N2W4

- F0N2W4_NEIMO

UniProt

F0N2W4 - F0N2W4_NEIMO

Protein

Elongation factor Tu

Gene

tuf

Organism
Neisseria meningitidis serogroup B (strain M04-240196)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 19 (01 Oct 2014)
      Sequence version 1 (03 May 2011)
      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

    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

    Keywords - Molecular functioni

    Elongation factorUniRule annotationImported

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    GTP-bindingUniRule annotation, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciNMEN935593:GLHT-130-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor TuUniRule annotation
    Short name:
    EF-TuUniRule annotation
    Gene namesi
    Name:tufUniRule annotation
    Ordered Locus Names:NMBM04240196_0130Imported
    OrganismiNeisseria meningitidis serogroup B (strain M04-240196)Imported
    Taxonomic identifieri935593 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
    ProteomesiUP000007481: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    CytoplasmUniRule annotation

    PTM / Processingi

    Proteomic databases

    PRIDEiF0N2W4.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliF0N2W4.
    SMRiF0N2W4. Positions 2-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK02358.

    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. EFACTOR_GTP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    F0N2W4-1 [UniParc]FASTAAdd to Basket

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    MAKEKFERSK PHVNVGTIGH VDHGKTTLTA ALTTILAKKF GGAAKAYDQI    50
    DNAPEEKARG ITINTSHVEY ETETRHYAHV DCPGHADYVK NMITGAAQMD 100
    GAILVCSAAD GPMPQTREHI LLARQVGVPY IIVFMNKCDM VDDAELLELV 150
    EMEIRDLLSS YDFPGDDCPI VQGSALKALE GDAAYEEKIF ELAAALDSYI 200
    PTPERAVDKP FLLPIEDVFS ISGRGTVVTG RVERGIIHVG DEIEIVGLKE 250
    TQKTTCTGVE MFRKLLDEGQ AGDNVGVLLR GTKREDVERG QVLAKPGTIT 300
    PHTKFKAEVY VLSKEEGGRH TPFFANYRPQ FYFRTTDVTG AVTLEEGVEM 350
    VMPGENVTIT VELIAPIAME EGLRFAIREG GRTVGAGVVS SVIA 394
    Length:394
    Mass (Da):42,909
    Last modified:May 3, 2011 - v1
    Checksum:i0C571C3D20CBE944
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002423 Genomic DNA. Translation: ADZ00670.1.
    RefSeqiYP_005896909.1. NC_017515.1.

    Genome annotation databases

    EnsemblBacteriaiADZ00670; ADZ00670; NMBM04240196_0130.
    GeneIDi12487193.
    KEGGinmq:NMBM04240196_0130.
    PATRICi47166390. VBINeiMen179694_0156.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002423 Genomic DNA. Translation: ADZ00670.1 .
    RefSeqi YP_005896909.1. NC_017515.1.

    3D structure databases

    ProteinModelPortali F0N2W4.
    SMRi F0N2W4. Positions 2-394.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi F0N2W4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADZ00670 ; ADZ00670 ; NMBM04240196_0130 .
    GeneIDi 12487193.
    KEGGi nmq:NMBM04240196_0130.
    PATRICi 47166390. VBINeiMen179694_0156.

    Phylogenomic databases

    KOi K02358.

    Enzyme and pathway databases

    BioCyci NMEN935593:GLHT-130-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. EFACTOR_GTP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Neisseria meningitidis is structured in clades associated with restriction modification systems that modulate homologous recombination."
      Budroni S., Siena E., Hotopp J.C., Seib K.L., Serruto D., Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.
      Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: M04-240196Imported.

    Entry informationi

    Entry nameiF0N2W4_NEIMO
    AccessioniPrimary (citable) accession number: F0N2W4
    Entry historyi
    Integrated into UniProtKB/TrEMBL: May 3, 2011
    Last sequence update: May 3, 2011
    Last modified: October 1, 2014
    This is version 19 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteomeImported

    External Data

    Dasty 3