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P0CE48 (EFTU2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation factor Tu 2

Short name=EF-Tu 2
Alternative name(s):
P-43
Gene names
Name:tufB
Ordered Locus Names:b3980, JW3943
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. HAMAP-Rule MF_00118

May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation. HAMAP-Rule MF_00118

Subunit structure

Monomer.

Subcellular location

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. Ref.8 Ref.10

Post-translational modification

The N-terminus is blocked. HAMAP-Rule MF_00118

Methylated in vivo on Lys-57 in response to nutrient starvation. Ref.5 Ref.6 Ref.8 Ref.12

Phosphorylated in vitro by phage protein doc on Thr-383. Ref.11 Ref.20 Ref.22 Ref.23

Phosphorylated in vitro by HipA on Thr-383 (Ref.20), this has since been reported not to occur in vivo (Ref.22). Ref.11 Ref.20 Ref.22 Ref.23

Miscellaneous

This chain is also used in bacteriophage Q-beta RNA polymerase.

Present with about 70,000 molecules/cell (Ref.10).

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.

Sequence similarities

Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6
Chain2 – 394393Elongation factor Tu 2 HAMAP-Rule MF_00118
PRO_0000392289

Regions

Nucleotide binding19 – 268GTP HAMAP-Rule MF_00118
Nucleotide binding81 – 855GTP HAMAP-Rule MF_00118
Nucleotide binding136 – 1394GTP HAMAP-Rule MF_00118

Amino acid modifications

Modified residue21N-acetylserine Ref.5 Ref.6
Modified residue381N6-succinyllysine Ref.21
Modified residue571N6,N6-dimethyllysine; alternate Ref.5 Ref.6 Ref.8 Ref.12
Modified residue571N6-methyllysine; alternate Ref.5 Ref.6 Ref.8 Ref.12
Modified residue1771N6-succinyllysine Ref.21
Modified residue2491N6-succinyllysine Ref.21
Modified residue2531N6-succinyllysine Ref.21
Modified residue2951N6-succinyllysine Ref.21
Modified residue3141N6-acetyllysine; alternate Ref.19
Modified residue3141N6-succinyllysine; alternate Ref.21
Modified residue3831Phosphothreonine Probable

Experimental info

Mutagenesis201H → A: No change in binding GDP and 3-fold reduction in binding EF-Ts. Ref.18
Mutagenesis1151Q → A: Weaker binding for GDP and for EF-Ts. Ref.18
Mutagenesis1371K → R, Q, E or I: Reduces affinity for GDP. Ref.14
Mutagenesis1391D → N: Reduces affinity for GDP; increases affinity for XDP. Ref.13
Mutagenesis2231G → D: Inhibits codon-induced conformational changes leading to GTPase activation on the ribosome.
Mutagenesis3491E → A: No change in binding GDP but higher binding constant for EF-Ts. Ref.18
Mutagenesis3831T → V: No longer phosphorylated by phage protein doc. Ref.23

Secondary structure

....................................................................... 394
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0CE48 [UniParc].

Last modified March 23, 2010. Version 1.
Checksum: 6EDA60255F43358F

FASTA39443,314
        10         20         30         40         50         60 
MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI DNAPEEKARG 

        70         80         90        100        110        120 
ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI 

       130        140        150        160        170        180 
LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE 

       190        200        210        220        230        240 
GDAEWEAKIL ELAGFLDSYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG 

       250        260        270        280        290        300 
EEVEIVGIKE TQKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGTIK 

       310        320        330        340        350        360 
PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV 

       370        380        390 
VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLS 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]Erratum
Kawashima T., Berthet-Colominas C., Wulff M., Cusack S., Leberman R.
Nature 381:172-172(1996)
[28]"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.
[29]"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).
[30]"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.
[31]"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.
[32]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIREFECT. A91478.
RefSeqNP_418407.1. NC_000913.3.
YP_491481.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP0CE48.
SMRP0CE48. Positions 9-394.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid852776. 1 interaction.
DIPDIP-60620N.
MINTMINT-1234073.

Proteomic databases

PRIDEP0CE48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76954; AAC76954; b3980.
BAE77340; BAE77340; BAE77340.
GeneID12932406.
948482.
KEGGecj:Y75_p3217.
eco:b3980.
PATRIC32123481. VBIEscCol129921_4093.

Organism-specific databases

EchoBASEEB1030.
EcoGeneEG11037. tufB.

Phylogenomic databases

KOK02358.
OMAGTEMCMP.
OrthoDBEOG6R5C6X.
PhylomeDBP0CE48.

Enzyme and pathway databases

BioCycEcoCyc:EG11037-MONOMER.

Gene expression databases

GenevestigatorP0A6N1.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00118_B. EF_Tu_B.
InterProIPR000795. 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]
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00485. EF-Tu. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0CE48.
PROP0CE48.

Entry information

Entry nameEFTU2_ECOLI
AccessionPrimary (citable) accession number: P0CE48
Secondary accession number(s): O68929 expand/collapse secondary AC list , P02990, P0A6N1, Q2M704, Q2M8R6, Q8X4S9, Q8XED3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 23, 2010
Last modified: July 9, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene