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Protein

Elongation factor Tu-A

Gene

tufA

Organism
Thermus thermophilus
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

BRENDAi3.6.5.3. 2305.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor Tu-AUniRule annotation
Short name:
EF-Tu-AUniRule annotation
Gene namesi
Name:tufAUniRule annotation
Synonyms:tuf
OrganismiThermus thermophilus
Taxonomic identifieri274 [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 methionineiRemoved
Chaini2 – 406405Elongation factor Tu-APRO_0000091422Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei395 – 3951PhosphothreonineBy similarity

Post-translational modificationi

Phosphorylated on a threonine.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP60338.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

DIPiDIP-61168N.
IntActiP60338. 1 interaction.
STRINGi262724.TTC1734.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 187Combined sources
Helixi21 – 233Combined sources
Helixi25 – 3915Combined 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
Turni191 – 1933Combined sources
Helixi195 – 21016Combined sources
Beta strandi218 – 2203Combined 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 strandi279 – 2824Combined sources
Beta strandi286 – 2916Combined sources
Turni296 – 2983Combined sources
Beta strandi304 – 3074Combined 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
1AIPX-ray3.00A/B/E/F2-406[»]
1EXMX-ray1.70A2-406[»]
4H9GX-ray1.93A2-406[»]
4LBVX-ray2.03A3-406[»]
4LBWX-ray1.74A3-406[»]
4LBYX-ray2.69A3-406[»]
4LBZX-ray2.22A3-406[»]
4LC0X-ray2.22A3-406[»]
ProteinModelPortaliP60338.
SMRiP60338. Positions 10-406.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60338.

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.

P60338-1 [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 - v2
Checksum:iBA597518358269E4
GO

Sequence databases

PIRiS00229.
S17146.

Cross-referencesi

Sequence databases

PIRiS00229.
S17146.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AIPX-ray3.00A/B/E/F2-406[»]
1EXMX-ray1.70A2-406[»]
4H9GX-ray1.93A2-406[»]
4LBVX-ray2.03A3-406[»]
4LBWX-ray1.74A3-406[»]
4LBYX-ray2.69A3-406[»]
4LBZX-ray2.22A3-406[»]
4LC0X-ray2.22A3-406[»]
ProteinModelPortaliP60338.
SMRiP60338. Positions 10-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61168N.
IntActiP60338. 1 interaction.
STRINGi262724.TTC1734.

Proteomic databases

PRIDEiP60338.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CGV. Bacteria.
COG0050. LUCA.

Enzyme and pathway databases

BRENDAi3.6.5.3. 2305.

Miscellaneous databases

EvolutionaryTraceiP60338.

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. "Crystal structure of active elongation factor Tu reveals major domain rearrangements."
    Berchtold H., Reshetnikova L., Reiser C.O.A., Schirmer N.K., Sprinzl M., Hilgenfeld R.
    Nature 365:126-132(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  2. "Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus."
    Wang Y., Jiang Y., Meyering-Voss M., Sprinzl M., Sigler P.B.
    Nat. Struct. Biol. 4:650-656(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH EF-TS.
  3. "The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA."
    Nissen P., Thirup S., Kjeldgaard M., Nyborg J.
    Structure 7:143-156(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Entry informationi

Entry nameiEFTU1_THETH
AccessioniPrimary (citable) accession number: P60338
Secondary accession number(s): P07157
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The sequence shown here has been extracted from PDB entry 1EXM.Curated

Keywords - Technical termi

3D-structure

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.