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P0CE48

- EFTU2_ECOLI

UniProt

P0CE48 - EFTU2_ECOLI

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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

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
Complete GO annotation...

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-HAMAP
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

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. 1 Publication
Mutagenesisi115 – 1151Q → A: Weaker binding for GDP and for EF-Ts. 1 Publication
Mutagenesisi137 – 1371K → R, Q, E or I: Reduces affinity for GDP. 1 Publication
Mutagenesisi139 – 1391D → N: Reduces affinity for GDP; increases affinity for XDP. 1 Publication
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. 1 Publication
Mutagenesisi383 – 3831T → V: No longer phosphorylated by phage protein doc. 1 Publication

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 – 187Combined sources
Helixi25 – 4016Combined sources
Helixi47 – 515Combined sources
Beta strandi55 – 584Combined sources
Helixi61 – 633Combined sources
Beta strandi67 – 715Combined sources
Beta strandi76 – 816Combined sources
Helixi86 – 883Combined sources
Helixi89 – 968Combined sources
Beta strandi102 – 1076Combined sources
Turni108 – 1103Combined sources
Helixi114 – 12613Combined sources
Beta strandi131 – 1366Combined sources
Helixi138 – 1403Combined sources
Helixi144 – 16017Combined sources
Turni165 – 1673Combined sources
Beta strandi170 – 1723Combined sources
Helixi175 – 1795Combined sources
Helixi183 – 19917Combined sources
Helixi206 – 2083Combined sources
Beta strandi212 – 2143Combined sources
Beta strandi218 – 2214Combined sources
Turni222 – 2243Combined sources
Beta strandi225 – 2317Combined sources
Beta strandi234 – 2385Combined sources
Beta strandi242 – 2498Combined sources
Beta strandi252 – 26110Combined sources
Beta strandi264 – 2707Combined sources
Beta strandi274 – 2818Combined sources
Helixi284 – 2863Combined sources
Beta strandi292 – 2954Combined sources
Beta strandi300 – 31112Combined sources
Helixi314 – 3163Combined sources
Beta strandi330 – 3334Combined sources
Beta strandi336 – 3438Combined sources
Beta strandi356 – 36914Combined sources
Beta strandi374 – 3796Combined sources
Beta strandi382 – 39211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

InParanoidiP0CE48.
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

        10         20         30         40         50
MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI
60 70 80 90 100
DNAPEEKARG ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD
110 120 130 140 150
GAILVVAATD GPMPQTREHI LLGRQVGVPY IIVFLNKCDM VDDEELLELV
160 170 180 190 200
EMEVRELLSQ YDFPGDDTPI VRGSALKALE GDAEWEAKIL ELAGFLDSYI
210 220 230 240 250
PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG EEVEIVGIKE
260 270 280 290 300
TQKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGTIK
310 320 330 340 350
PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM
360 370 380 390
VMPGDNIKMV VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLS
Length:394
Mass (Da):43,314
Last modified:March 23, 2010 - v1
Checksum:i6EDA60255F43358F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

InParanoidi P0CE48.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 41 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