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Q5SHN6 (EFTU1_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. 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

Names and origin

Protein namesRecommended name:
Elongation factor Tu-A

Short name=EF-Tu-A
Gene names
Name:tufA
Synonyms:tuf
Ordered Locus Names:TTHA1694
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

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-Rule MF_00118

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00118

Subcellular location

Cytoplasm HAMAP-Rule MF_00118.

Post-translational modification

Phosphorylated on a threonine. Ref.4

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
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

GTPase activity

Inferred from electronic annotation. Source: InterPro

translation elongation factor activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP-Rule MF_00118
Chain2 – 406405Elongation factor Tu-A HAMAP-Rule MF_00118
PRO_0000091423

Regions

Nucleotide binding19 – 268GTP HAMAP-Rule MF_00118
Nucleotide binding82 – 865GTP HAMAP-Rule MF_00118
Nucleotide binding137 – 1404GTP HAMAP-Rule MF_00118

Amino acid modifications

Modified residue3951Phosphothreonine Probable

Experimental info

Sequence conflict3801A → G in CAA29397. Ref.1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5SHN6 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BA597518358269E4

FASTA40644,782
        10         20         30         40         50         60 
MAKGEFVRTK 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 
EQMHRNPKTR RGENEWVDKI WELLDAIDEY IPTPVRDVDK PFLMPVEDVF TITGRGTVAT 

       250        260        270        280        290        300 
GRIERGKVKV GDEVEIVGLA PETRRTVVTG VEMHRKTLQE GIAGDNVGVL LRGVSREEVE 

       310        320        330        340        350        360 
RGQVLAKPGS ITPHTKFEAS VYVLKKEEGG RHTGFFSGYR PQFYFRTTDV TGVVQLPPGV 

       370        380        390        400 
EMVMPGDNVT FTVELIKPVA LEEGLRFAIR EGGRTVGAGV VTKILE 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05977 Genomic DNA. Translation: CAA29397.1.
X06657 Genomic DNA. Translation: CAA29856.1.
AP008226 Genomic DNA. Translation: BAD71517.1.
PIRS00229.
S17146.
RefSeqYP_144960.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HA3X-ray2.00A/B2-406[»]
2C78X-ray1.40A2-405[»]
2WRNX-ray3.60Z1-406[»]
2WRQX-ray3.60Z1-406[»]
2Y0UX-ray3.10Z2-406[»]
2Y0WX-ray3.10Z2-406[»]
2Y0YX-ray3.10Z2-406[»]
2Y10X-ray3.10Z2-406[»]
2Y12X-ray3.10Z2-406[»]
2Y14X-ray3.10Z2-406[»]
2Y16X-ray3.10Z2-406[»]
2Y18X-ray3.10Z2-406[»]
4ABRX-ray3.10Z2-406[»]
ProteinModelPortalQ5SHN6.
SMRQ5SHN6. Positions 10-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA1694.

Proteomic databases

PRIDEQ5SHN6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD71517; BAD71517; BAD71517.
GeneID3167925.
KEGGttj:TTHA1694.
PATRIC23958343. VBITheThe93045_1664.

Phylogenomic databases

eggNOGCOG0050.
HOGENOMHOG000229290.
KOK02358.
OMAVTPHTEF.
OrthoDBEOG6R5C6X.
ProtClustDBPRK00049.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-1733-MONOMER.

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

EvolutionaryTraceQ5SHN6.

Entry information

Entry nameEFTU1_THET8
AccessionPrimary (citable) accession number: Q5SHN6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 78 of the entry and version 3 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