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P0CE48

- EFTU2_ECOLI

UniProt

P0CE48 - EFTU2_ECOLI

Protein

Elongation factor Tu 2

Gene

tufB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 39 (01 Oct 2014)
      Sequence version 1 (23 Mar 2010)
      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.
    May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.

    Regions

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

    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

    BioCyciEcoCyc:EG11037-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor Tu 2UniRule annotation
    Short name:
    EF-Tu 2UniRule annotation
    Alternative name(s):
    P-43
    Gene namesi
    Name:tufBUniRule annotation
    Ordered Locus Names:b3980, JW3943
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11037. tufB.

    Subcellular locationi

    Cytoplasm. Cell inner membrane; Peripheral membrane protein
    Note: Between 50-80% of the protein is associated with the cell inner membrane. Localization to the membrane has been suggested to follow nutrient stress.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi20 – 201H → A: No change in binding GDP and 3-fold reduction in binding EF-Ts. 2 Publications
    Mutagenesisi115 – 1151Q → A: Weaker binding for GDP and for EF-Ts. 2 Publications
    Mutagenesisi137 – 1371K → R, Q, E or I: Reduces affinity for GDP. 2 Publications
    Mutagenesisi139 – 1391D → N: Reduces affinity for GDP; increases affinity for XDP. 2 Publications
    Mutagenesisi223 – 2231G → D: Inhibits codon-induced conformational changes leading to GTPase activation on the ribosome. 1 Publication
    Mutagenesisi349 – 3491E → A: No change in binding GDP but higher binding constant for EF-Ts. 2 Publications
    Mutagenesisi383 – 3831T → V: No longer phosphorylated by phage protein doc. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 394393Elongation factor Tu 2PRO_0000392289Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei38 – 381N6-succinyllysine1 Publication
    Modified residuei57 – 571N6,N6-dimethyllysine; alternate4 Publications
    Modified residuei57 – 571N6-methyllysine; alternate4 Publications
    Modified residuei177 – 1771N6-succinyllysine1 Publication
    Modified residuei249 – 2491N6-succinyllysine1 Publication
    Modified residuei253 – 2531N6-succinyllysine1 Publication
    Modified residuei295 – 2951N6-succinyllysine1 Publication
    Modified residuei314 – 3141N6-acetyllysine; alternate1 Publication
    Modified residuei314 – 3141N6-succinyllysine; alternate1 Publication
    Modified residuei383 – 3831Phosphothreonine3 Publications

    Post-translational modificationi

    The N-terminus is blocked.
    Methylated in vivo on Lys-57 in response to nutrient starvation.4 Publications
    Phosphorylated in vitro by phage protein doc on Thr-383.3 Publications
    Phosphorylated in vitro by HipA on Thr-383 (PubMed:19150849), this has since been reported not to occur in vivo (PubMed:24095282).4 Publications

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    PRIDEiP0CE48.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A6N1.

    Interactioni

    Subunit structurei

    Monomer.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    BioGridi852776. 1 interaction.
    DIPiDIP-60620N.
    MINTiMINT-1234073.

    Structurei

    Secondary structure

    1
    394
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 187
    Helixi25 – 4016
    Helixi47 – 515
    Beta strandi55 – 584
    Beta strandi61 – 644
    Beta strandi66 – 716
    Beta strandi76 – 816
    Helixi85 – 9410
    Beta strandi100 – 1078
    Turni108 – 1103
    Helixi114 – 12613
    Beta strandi130 – 1367
    Turni138 – 1403
    Helixi144 – 16017
    Helixi165 – 1673
    Beta strandi170 – 1723
    Helixi175 – 1806
    Helixi183 – 19917
    Helixi206 – 2083
    Beta strandi212 – 2143
    Beta strandi217 – 2215
    Turni222 – 2243
    Beta strandi225 – 2317
    Beta strandi234 – 2385
    Beta strandi242 – 2509
    Beta strandi252 – 26110
    Beta strandi264 – 2707
    Beta strandi274 – 2818
    Helixi284 – 2863
    Beta strandi292 – 2943
    Beta strandi301 – 31111
    Helixi314 – 3163
    Beta strandi330 – 3334
    Beta strandi336 – 3438
    Beta strandi356 – 36813
    Beta strandi374 – 3796
    Beta strandi382 – 39413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DG1X-ray2.50G/H1-394[»]
    1EFMX-ray2.70A2-394[»]
    1EFUX-ray2.50A/C10-394[»]
    1LS2electron microscopy16.80A2-394[»]
    1OB2X-ray3.35A3-394[»]
    1QZDelectron microscopy-A2-394[»]
    2BVNX-ray2.30A/B2-394[»]
    3FIHelectron microscopy6.70Z2-394[»]
    3IZVelectron microscopy-C2-394[»]
    3IZWelectron microscopy-C2-394[»]
    3MMPX-ray2.50A/C1-394[»]
    ProteinModelPortaliP0CE48.
    SMRiP0CE48. Positions 9-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0CE48.

    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

    KOiK02358.
    OMAiGTEMCMP.
    OrthoDBiEOG6R5C6X.
    PhylomeDBiP0CE48.

    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.

    P0CE48-1 [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:March 23, 2010 - v1
    Checksum:i6EDA60255F43358F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57091 Genomic DNA. Translation: CAA40370.1.
    J01717 Genomic DNA. Translation: AAA24669.1.
    U00006 Genomic DNA. Translation: AAC43078.1.
    U00096 Genomic DNA. Translation: AAC76954.1.
    AP009048 Genomic DNA. Translation: BAE77340.1.
    PIRiA91478. EFECT.
    RefSeqiNP_418407.1. NC_000913.3.
    YP_491481.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76954; AAC76954; b3980.
    BAE77340; BAE77340; BAE77340.
    GeneIDi12932406.
    948482.
    KEGGiecj:Y75_p3217.
    eco:b3980.
    PATRICi32123481. VBIEscCol129921_4093.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57091 Genomic DNA. Translation: CAA40370.1 .
    J01717 Genomic DNA. Translation: AAA24669.1 .
    U00006 Genomic DNA. Translation: AAC43078.1 .
    U00096 Genomic DNA. Translation: AAC76954.1 .
    AP009048 Genomic DNA. Translation: BAE77340.1 .
    PIRi A91478. EFECT.
    RefSeqi NP_418407.1. NC_000913.3.
    YP_491481.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DG1 X-ray 2.50 G/H 1-394 [» ]
    1EFM X-ray 2.70 A 2-394 [» ]
    1EFU X-ray 2.50 A/C 10-394 [» ]
    1LS2 electron microscopy 16.80 A 2-394 [» ]
    1OB2 X-ray 3.35 A 3-394 [» ]
    1QZD electron microscopy - A 2-394 [» ]
    2BVN X-ray 2.30 A/B 2-394 [» ]
    3FIH electron microscopy 6.70 Z 2-394 [» ]
    3IZV electron microscopy - C 2-394 [» ]
    3IZW electron microscopy - C 2-394 [» ]
    3MMP X-ray 2.50 A/C 1-394 [» ]
    ProteinModelPortali P0CE48.
    SMRi P0CE48. Positions 9-394.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 852776. 1 interaction.
    DIPi DIP-60620N.
    MINTi MINT-1234073.

    Proteomic databases

    PRIDEi P0CE48.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76954 ; AAC76954 ; b3980 .
    BAE77340 ; BAE77340 ; BAE77340 .
    GeneIDi 12932406.
    948482.
    KEGGi ecj:Y75_p3217.
    eco:b3980.
    PATRICi 32123481. VBIEscCol129921_4093.

    Organism-specific databases

    EchoBASEi EB1030.
    EcoGenei EG11037. tufB.

    Phylogenomic databases

    KOi K02358.
    OMAi GTEMCMP.
    OrthoDBi EOG6R5C6X.
    PhylomeDBi P0CE48.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG11037-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0CE48.
    PROi P0CE48.

    Gene expression databases

    Genevestigatori P0A6N1.

    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. "The nucleotide sequence of tufB and four nearby tRNA structural genes of Escherichia coli."
      An G., Friesen J.D.
      Gene 12:33-39(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "The complete amino-acid sequence of elongation factor Tu from Escherichia coli."
      Jones M.D., Petersen T.E., Nielsen K.M., Magnusson S., Sottrup-Jensen L., Gausing K., Clark B.F.C.
      Eur. J. Biochem. 108:507-526(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-394, ACETYLATION AT SER-2, METHYLATION AT LYS-57.
      Strain: B.
    6. "The amino acid sequence of elongation factor Tu of Escherichia coli. The complete sequence."
      Laursen R.A., L'Italien J.J., Nagarkatti S., Miller D.L.
      J. Biol. Chem. 256:8102-8109(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-394, ACETYLATION AT SER-2, METHYLATION AT LYS-57.
    7. "Transcription of the E. coli tufB gene: cotranscription with four tRNA genes and inhibition by guanosine-5'-diphosphate-3'-diphosphate."
      Miyajima A., Shibuya M., Kuchino Y., Kaziro Y.
      Mol. Gen. Genet. 183:13-19(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
    8. "Elongation factor Tu is methylated in response to nutrient deprivation in Escherichia coli."
      Young C.C., Bernlohr R.W.
      J. Bacteriol. 173:3096-3100(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 153-176 AND 262-290, METHYLATION AT LYS-57 IN RESPONSE TO NUTRIENT STARVATION, SUBCELLULAR LOCATION.
      Strain: B/R.
    9. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 311-322, BLOCKAGE OF N-TERMINUS.
      Strain: K12 / EMG2.
    10. "Abundance and membrane association of elongation factor Tu in E. coli."
      Jacobson G.R., Rosenbusch J.P.
      Nature 261:23-26(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: BLOCKAGE OF N-TERMINUS, SUBCELLULAR LOCATION.
      Strain: K12 / BHB 960.
    11. "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 AT THR-383, PROTEIN SEQUENCE OF 290-304 AND 383-391.
    12. "Location of the site of methylation in elongation factor Tu."
      L'Italien J.J., Laursen R.A.
      FEBS Lett. 107:359-362(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-57.
    13. "A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP regulatory protein."
      Hwang Y.-W., Miller D.L.
      J. Biol. Chem. 262:13081-13085(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-139.
    14. "Mutagenesis of bacterial elongation factor Tu at lysine 136. A conserved amino acid in GTP regulatory proteins."
      Hwang Y.-W., Sanchez A., Miller D.L.
      J. Biol. Chem. 264:8304-8309(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-137.
    15. "Site-directed mutagenesis of the GDP binding domain of bacterial elongation factor Tu."
      Hwang Y.-W., McCabe P.G., Innis M.A., Miller D.L.
      Arch. Biochem. Biophys. 274:394-403(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    16. "The G222D mutation in elongation factor Tu inhibits the codon-induced conformational changes leading to GTPase activation on the ribosome."
      Vorstenbosch E., Pape T., Rodnina M.V., Kraal B., Wintermeyer W.
      EMBO J. 15:6766-6774(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF MUTANT ASP-223.
    17. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    18. "Mutational analysis of the roles of residues in Escherichia coli elongation factor Ts in the interaction with elongation factor Tu."
      Zhang Y., Yu N.-J., Spremulli L.L.
      J. Biol. Chem. 273:4556-4562(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-20; GLN-115 AND GLU-349.
    19. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-314, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    20. "Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB."
      Schumacher M.A., Piro K.M., Xu W., Hansen S., Lewis K., Brennan R.G.
      Science 323:396-401(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-383 BY HIPA.
    21. "Identification of lysine succinylation as a new post-translational modification."
      Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
      Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION AT LYS-38; LYS-177; LYS-249; LYS-253; LYS-295 AND LYS-314.
      Strain: K12.
    22. "Molecular mechanism of bacterial persistence by HipA."
      Germain E., Castro-Roa D., Zenkin N., Gerdes K.
      Mol. Cell 52:248-254(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: LACK OF PHOSPHORYLATION BY HIPA.
      Strain: K12 / MG1655 / ATCC 47076.
    23. "The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu."
      Castro-Roa D., Garcia-Pino A., De Gieter S., van Nuland N.A., Loris R., Zenkin N.
      Nat. Chem. Biol. 9:811-817(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-383 BY DOC, MUTAGENESIS OF THR-383.
    24. "Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins."
      Jurnak F.
      Science 230:32-36(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-394 OF A TRYPSIN-MODIFIED EF-TU-GDP.
    25. "Refined structure of elongation factor EF-Tu from Escherichia coli."
      Kjeldgaard M., Nyborg J.
      J. Mol. Biol. 223:721-742(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
    26. "The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5-A resolution."
      Kawashima T., Berthet-Colominas C., Wulff M., Cusack S., Leberman R.
      Nature 379:511-518(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 10-394 IN COMPLEX WITH EF-TS.
    27. "An alpha to beta conformational switch in EF-Tu."
      Abel K., Yoder M.D., Hilgenfeld R., Jurnak F.
      Structure 4:1153-1159(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GDP AND ANTIBIOTIC GE2270A.
    28. "Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05-A resolution."
      Song H., Parsons M.R., Rowsell S., Leonard G., Phillips S.E.V.
      J. Mol. Biol. 285:1245-1256(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
    29. "Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process."
      Valle M., Sengupta J., Swami N.K., Grassucci R.A., Burkhardt N., Nierhaus K.H., Agrawal R.K., Frank J.
      EMBO J. 21:3557-3567(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (16.8 ANGSTROMS) OF 2-393 IN THE 70S RIBOSOME.
    30. "Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy."
      Valle M., Zavialov A., Li W., Stagg S.M., Sengupta J., Nielsen R.C., Nissen P., Harvey S.C., Ehrenberg M., Frank J.
      Nat. Struct. Biol. 10:899-906(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 3-394, STRUCTURE BY ELECTRON MICROSCOPY (10.0 ANGSTROMS) OF 2-393 IN COMPLEX WITH THE 70S RIBOSOME.
    31. "Enacyloxin IIa pinpoints a binding pocket of elongation factor Tu for development of novel antibiotics."
      Parmeggiani A., Krab I.M., Watanabe T., Nielsen R.C., Dahlberg C., Nyborg J., Nissen P.
      J. Biol. Chem. 281:2893-2900(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-394 OF EF-TU-GUANYLYL IMINODIPHOSPHATE (GDPNP) ENACYLOXIN IIA COMPLEX.

    Entry informationi

    Entry nameiEFTU2_ECOLI
    AccessioniPrimary (citable) accession number: P0CE48
    Secondary accession number(s): O68929
    , P02990, P0A6N1, Q2M704, Q2M8R6, Q8X4S9, Q8XED3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 23, 2010
    Last sequence update: March 23, 2010
    Last modified: October 1, 2014
    This is version 39 of the entry and version 1 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.
    Present with about 70,000 molecules/cell.1 Publication
    The antibiotic kirromycin inhibits protein biosynthesis by inhibiting the release of EF-Tu from the ribosome. TufA resistance to kirromycin is conferred by mutations to Gln-125, Gly-317 and Ala-376. This has not been formally proven for tufB, but is certainly correct.
    The antibiotic pulvomycin inhibits protein biosynthesis by disrupting the allosteric control mechanism of EF-Tu TufA resistance to pulvomycin is conferred by Arg-231, Arg-334 and Thr-335. This has not been formally proven for tufB, but is certainly correct.

    Caution

    EF-Tu 1 and EF-Tu 2 differ in a single position and are no longer merged. However, many papers are found in both entries as it is not always possible to determine for each paper which of EF-Tu 1 or EF-Tu 2 was being worked upon.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3