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Protein

Elongation factor Tu-A

Gene

tufA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 268GTP
Nucleotide bindingi82 – 865GTP
Nucleotide bindingi137 – 1404GTP

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1733-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor Tu-AUniRule annotation
Short name:
EF-Tu-AUniRule annotation
Gene namesi
Name:tufAUniRule annotation
Synonyms:tuf
Ordered Locus Names:TTHA1694
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 406405Elongation factor Tu-APRO_0000091423Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei395 – 3951Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated on a threonine.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ5SHN6.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi300852.TTHA1694.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 187Combined sources
Helixi25 – 3814Combined sources
Helixi48 – 514Combined sources
Helixi55 – 606Combined sources
Beta strandi67 – 726Combined sources
Beta strandi77 – 826Combined sources
Helixi87 – 893Combined sources
Helixi90 – 978Combined sources
Beta strandi101 – 1088Combined sources
Turni109 – 1113Combined sources
Helixi115 – 12612Combined sources
Beta strandi132 – 1376Combined sources
Helixi139 – 1413Combined sources
Helixi145 – 16117Combined sources
Turni166 – 1683Combined sources
Beta strandi171 – 1733Combined sources
Helixi176 – 18510Combined sources
Helixi195 – 21016Combined sources
Beta strandi223 – 2253Combined sources
Beta strandi228 – 2325Combined sources
Turni233 – 2353Combined sources
Beta strandi236 – 2427Combined sources
Beta strandi245 – 2495Combined sources
Beta strandi253 – 26210Combined sources
Beta strandi264 – 27310Combined sources
Beta strandi276 – 2827Combined sources
Beta strandi286 – 2938Combined sources
Turni296 – 2983Combined sources
Beta strandi304 – 3074Combined sources
Beta strandi310 – 32314Combined sources
Helixi326 – 3283Combined sources
Beta strandi342 – 3454Combined sources
Beta strandi348 – 3558Combined sources
Beta strandi368 – 38114Combined sources
Beta strandi386 – 3916Combined sources
Beta strandi394 – 40411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HA3X-ray2.00A/B2-406[»]
2C78X-ray1.40A2-406[»]
4V5GX-ray3.60AZ/CZ1-406[»]
4V5PX-ray3.10AZ/CZ2-406[»]
4V5QX-ray3.10AZ/CZ2-406[»]
4V5RX-ray3.10AZ/CZ2-406[»]
4V5SX-ray3.10AZ/CZ2-406[»]
4V8QX-ray3.10BZ2-406[»]
ProteinModelPortaliQ5SHN6.
SMRiQ5SHN6. Positions 10-406.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SHN6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 215206tr-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 268G1By similarity
Regioni61 – 655G2By similarity
Regioni82 – 854G3By similarity
Regioni137 – 1404G4By similarity
Regioni175 – 1773G5By 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

eggNOGiCOG0050.
HOGENOMiHOG000229290.
KOiK02358.
OMAiDEGGRHN.
OrthoDBiEOG6R5C6X.
PhylomeDBiQ5SHN6.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_B. EF_Tu_B.
InterProiIPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_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]
PfamiPF03144. 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.

Q5SHN6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKGEFVRTK PHVNVGTIGH VDHGKTTLTA ALTYVAAAEN PNVEVKDYGD
60 70 80 90 100
IDKAPEERAR GITINTAHVE YETAKRHYSH VDCPGHADYI KNMITGAAQM
110 120 130 140 150
DGAILVVSAA DGPMPQTREH ILLARQVGVP YIVVFMNKVD MVDDPELLDL
160 170 180 190 200
VEMEVRDLLN QYEFPGDEVP VIRGSALLAL EQMHRNPKTR RGENEWVDKI
210 220 230 240 250
WELLDAIDEY IPTPVRDVDK PFLMPVEDVF TITGRGTVAT GRIERGKVKV
260 270 280 290 300
GDEVEIVGLA PETRRTVVTG VEMHRKTLQE GIAGDNVGVL LRGVSREEVE
310 320 330 340 350
RGQVLAKPGS ITPHTKFEAS VYVLKKEEGG RHTGFFSGYR PQFYFRTTDV
360 370 380 390 400
TGVVQLPPGV EMVMPGDNVT FTVELIKPVA LEEGLRFAIR EGGRTVGAGV

VTKILE
Length:406
Mass (Da):44,782
Last modified:January 23, 2007 - v3
Checksum:iBA597518358269E4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti380 – 3801A → G in CAA29397 (PubMed:3317278).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05977 Genomic DNA. Translation: CAA29397.1.
X06657 Genomic DNA. Translation: CAA29856.1.
AP008226 Genomic DNA. Translation: BAD71517.1.
PIRiS00229.
S17146.
RefSeqiWP_011228847.1. NC_006461.1.
YP_144960.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71517; BAD71517; BAD71517.
GeneIDi3167925.
KEGGittj:TTHA1694.
PATRICi23958343. VBITheThe93045_1664.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05977 Genomic DNA. Translation: CAA29397.1.
X06657 Genomic DNA. Translation: CAA29856.1.
AP008226 Genomic DNA. Translation: BAD71517.1.
PIRiS00229.
S17146.
RefSeqiWP_011228847.1. NC_006461.1.
YP_144960.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HA3X-ray2.00A/B2-406[»]
2C78X-ray1.40A2-406[»]
4V5GX-ray3.60AZ/CZ1-406[»]
4V5PX-ray3.10AZ/CZ2-406[»]
4V5QX-ray3.10AZ/CZ2-406[»]
4V5RX-ray3.10AZ/CZ2-406[»]
4V5SX-ray3.10AZ/CZ2-406[»]
4V8QX-ray3.10BZ2-406[»]
ProteinModelPortaliQ5SHN6.
SMRiQ5SHN6. Positions 10-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1694.

Proteomic databases

PRIDEiQ5SHN6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71517; BAD71517; BAD71517.
GeneIDi3167925.
KEGGittj:TTHA1694.
PATRICi23958343. VBITheThe93045_1664.

Phylogenomic databases

eggNOGiCOG0050.
HOGENOMiHOG000229290.
KOiK02358.
OMAiDEGGRHN.
OrthoDBiEOG6R5C6X.
PhylomeDBiQ5SHN6.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1733-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SHN6.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_B. EF_Tu_B.
InterProiIPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_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]
PfamiPF03144. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and identification of the nucleotide binding site for the elongation factor Tu from Thermus thermophilus HB8."
    Seidler L., Peter M., Meissner F., Sprinzl M.
    Nucleic Acids Res. 15:9263-9277(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular cloning and sequence determination of the tuf gene coding for the elongation factor Tu of Thermus thermophilus HB8."
    Kushiro A., Shimizu M., Tomita K.
    Eur. J. Biochem. 170:93-98(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  4. "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.
  5. "Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox."
    Vogeley L., Palm G.J., Mesters J.R., Hilgenfeld R.
    J. Biol. Chem. 276:17149-17155(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF COMPLEX WITH GDP AND AURODOX.

Entry informationi

Entry nameiEFTU1_THET8
AccessioniPrimary (citable) accession number: Q5SHN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 90 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.