Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q01698 (EFTU_THEAQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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
Short name=EF-Tu
Gene names
Name:tuf
Synonyms:tufA
OrganismThermus aquaticus
Taxonomic identifier271 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length406 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 MF_00118_B

Subunit structure

Monomer By similarity. HAMAP MF_00118_B

Subcellular location

Cytoplasm HAMAP MF_00118_B.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Nucleotide-binding
   Molecular functionElongation factor
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: InterPro

translation elongation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 406405Elongation factor Tu HAMAP MF_00118_B
PRO_0000091420

Regions

Nucleotide binding19 – 268GTP HAMAP MF_00118_B
Nucleotide binding82 – 865GTP HAMAP MF_00118_B
Nucleotide binding137 – 1404GTP HAMAP MF_00118_B

Secondary structure

1 ...................................................................... 406
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01698 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A5E642800075E5D1

FASTA40644,814
        10         20         30         40         50         60 
MAKGEFIRTK PHVNVGTIGH VDHGKTTLTA ALTYVAAAEN PNVEVKDYGD IDKAPEERAR 

        70         80         90        100        110        120 
GITINTAHVE YETAKRHYSH VDCPGHADYI KNMITGAAQM DGAILVVSAA DGPMPQTREH 

       130        140        150        160        170        180 
ILLARQVGVP YIVVFMNKVD MVDDPELLDL VEMEVRDLLN QYEFPGDEVP VIRGSALLAL 

       190        200        210        220        230        240 
EEMHKNPKTK RGENEWVDKI WELLDAIDEY IPTPVRDVDK PFLMPVEDVF TITGRGTVAT 

       250        260        270        280        290        300 
GRIERGKVKV GDEVEIVGLA PETRKTVVTG VEMHRKTLQE GIAGDNVGLL LRGVSREEVE 

       310        320        330        340        350        360 
RGQVLAKPGS ITPHTKFEAS VYILKKEEGG RHTGFFTGYR PQFYFRTTDV TGVVRLPQGV 

       370        380        390        400 
EMVMPGDNVT FTVELIKPVA LEEGLRFAIR EGGRTVGAGV VTKILE

« Hide

References

[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: 1499561] [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: 8069622] [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: 7491491] [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: 8939739] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X66322 Genomic DNA. Translation: CAA46998.1.
PIRS29293.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B23X-ray2.60P2-405[»]
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[»]
1OB5X-ray3.10A/C/E2-405[»]
1TTTX-ray2.70A/B/C2-406[»]
1TUIX-ray2.70A/B/C2-406[»]
ProteinModelPortalQ01698.
SMRQ01698. Positions 2-406.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00118_B. EF_Tu_B.
[Tree]
InterProIPR000795. ProtSyn_GTP-bd.
IPR005225. Small_GTP-bd_dom.
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.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]
PANTHERPTHR23115:SF31. Transl_elong_EFTu/EF1A_bac/org. 1 hit.
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50465. Elong_init_C. 1 hit.
SSF50447. Translat_factor. 1 hit.
TIGRFAMsTIGR00485. EF-Tu. 1 hit.
TIGR00231. Small_GTP. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEFTU_THEAQ
AccessionPrimary (citable) accession number: Q01698
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: May 31, 2011
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents