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Protein

Elongation factor Tu

Gene

tuf

Organism
Thermus aquaticus
Status
Reviewed-Annotation score: Annotation score: 3 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

BRENDAi3.6.5.3. 6334.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor TuUniRule annotation
Short name:
EF-TuUniRule annotation
Gene namesi
Name:tufUniRule annotation
Synonyms:tufA
OrganismiThermus aquaticus
Taxonomic identifieri271 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 406405Elongation factor TuPRO_0000091420Add
BLAST

Proteomic databases

PRIDEiQ01698.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi498848.TaqDRAFT_4960.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 187Combined sources
Helixi25 – 3713Combined sources
Beta strandi41 – 433Combined sources
Helixi48 – 503Combined 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 – 12511Combined sources
Turni126 – 1283Combined sources
Beta strandi132 – 1376Combined sources
Helixi139 – 1413Combined sources
Helixi147 – 16014Combined sources
Turni161 – 1633Combined sources
Turni166 – 1683Combined sources
Beta strandi171 – 1733Combined sources
Helixi176 – 18510Combined sources
Turni191 – 1933Combined sources
Helixi195 – 21016Combined sources
Beta strandi218 – 2203Combined sources
Beta strandi223 – 23210Combined sources
Turni233 – 2353Combined sources
Beta strandi236 – 2427Combined sources
Beta strandi245 – 2495Combined sources
Beta strandi253 – 2564Combined sources
Beta strandi258 – 2625Combined sources
Beta strandi264 – 27310Combined sources
Beta strandi276 – 2827Combined sources
Beta strandi286 – 2916Combined sources
Turni296 – 2983Combined sources
Beta strandi304 – 3074Combined sources
Turni308 – 3103Combined sources
Beta strandi314 – 32310Combined sources
Helixi326 – 3283Combined sources
Beta strandi342 – 3454Combined sources
Beta strandi348 – 3558Combined sources
Beta strandi368 – 37912Combined 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
1B23X-ray2.60P2-406[»]
1EFTX-ray2.50A2-406[»]
1H1Umodel-B2-406[»]
1IPMmodel-I1-406[»]
1IPOmodel-G1-406[»]
1IPQmodel-F1-406[»]
1IPRmodel-G1-406[»]
1IPUmodel-H1-406[»]
1L1Umodel-11-406[»]
1MJ1electron microscopy13.00A2-406[»]
1OB5X-ray3.10A/C/E2-406[»]
1TTTX-ray2.70A/B/C2-406[»]
1TUIX-ray2.70A/B/C2-406[»]
ProteinModelPortaliQ01698.
SMRiQ01698. Positions 2-406.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01698.

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

eggNOGiENOG4105CGV. Bacteria.
COG0050. LUCA.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_B. EF_Tu_B.
InterProiIPR004161. EFTu-like_2.
IPR031157. 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.
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.

Q01698-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKGEFIRTK 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 EEMHKNPKTK RGENEWVDKI
210 220 230 240 250
WELLDAIDEY IPTPVRDVDK PFLMPVEDVF TITGRGTVAT GRIERGKVKV
260 270 280 290 300
GDEVEIVGLA PETRKTVVTG VEMHRKTLQE GIAGDNVGLL LRGVSREEVE
310 320 330 340 350
RGQVLAKPGS ITPHTKFEAS VYILKKEEGG RHTGFFTGYR PQFYFRTTDV
360 370 380 390 400
TGVVRLPQGV EMVMPGDNVT FTVELIKPVA LEEGLRFAIR EGGRTVGAGV

VTKILE
Length:406
Mass (Da):44,814
Last modified:January 23, 2007 - v2
Checksum:iA5E642800075E5D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66322 Genomic DNA. Translation: CAA46998.1.
PIRiS29293.
RefSeqiWP_003043841.1. NZ_LHCI01000106.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66322 Genomic DNA. Translation: CAA46998.1.
PIRiS29293.
RefSeqiWP_003043841.1. NZ_LHCI01000106.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B23X-ray2.60P2-406[»]
1EFTX-ray2.50A2-406[»]
1H1Umodel-B2-406[»]
1IPMmodel-I1-406[»]
1IPOmodel-G1-406[»]
1IPQmodel-F1-406[»]
1IPRmodel-G1-406[»]
1IPUmodel-H1-406[»]
1L1Umodel-11-406[»]
1MJ1electron microscopy13.00A2-406[»]
1OB5X-ray3.10A/C/E2-406[»]
1TTTX-ray2.70A/B/C2-406[»]
1TUIX-ray2.70A/B/C2-406[»]
ProteinModelPortaliQ01698.
SMRiQ01698. Positions 2-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi498848.TaqDRAFT_4960.

Proteomic databases

PRIDEiQ01698.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CGV. Bacteria.
COG0050. LUCA.

Enzyme and pathway databases

BRENDAi3.6.5.3. 6334.

Miscellaneous databases

EvolutionaryTraceiQ01698.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_B. EF_Tu_B.
InterProiIPR004161. EFTu-like_2.
IPR031157. 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.
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

  1. "Sequence of the tufA gene encoding elongation factor EF-Tu from Thermus aquaticus and overproduction of the protein in Escherichia coli."
    Voss R.H., Hartmann R.K., Lippmann C., Alexander C., Jahn O., Erdmann V.
    Eur. J. Biochem. 207:839-846(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-10.
    Strain: EP 00276.
  2. "The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation."
    Kjeldgaard M., Nissen P., Thirup S., Nyborg J.
    Structure 1:35-50(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    Strain: YT1.
  3. "Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog."
    Nissen P., Kjeldgaard M., Thirup S., Polekhina G., Reshetnikova L., Clark B.F.C., Nyborg J.
    Science 270:1464-1472(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    Strain: YT1.
  4. "Helix unwinding in the effector region of elongation factor EF-Tu-GDP."
    Polekhina G., Thirup S., Kjeldgaard M., Nissen P., Lippmann C., Nyborg J.
    Structure 4:1141-1151(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

Entry informationi

Entry nameiEFTU_THEAQ
AccessioniPrimary (citable) accession number: Q01698
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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

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 one 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.