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Q5M5I8 (EFTU_STRT2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Short name=EF-Tu
Gene names
Name:tuf
Ordered Locus Names:stu0487
OrganismStreptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) [Complete proteome] [HAMAP]
Taxonomic identifier264199 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis By similarity. HAMAP-Rule MF_00118

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00118

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00118.

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 termComplete 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

Chain1 – 398398Elongation factor Tu HAMAP-Rule MF_00118
PRO_1000015762

Regions

Nucleotide binding19 – 268GTP By similarity
Nucleotide binding84 – 885GTP By similarity
Nucleotide binding139 – 1424GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5M5I8 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: BB1F9107DB470CB2

FASTA39843,867
        10         20         30         40         50         60 
MAKEKYDRSK PHVNIGTIGH VDHGKTTLTA AITTVLARRL PSAVNTPKDY ASIDAAPEER 

        70         80         90        100        110        120 
ERGITINTAH VEYETEKRHY AHIDAPGHAD YVKNMITGAA QMDGAILVVA STDGPMPQTR 

       130        140        150        160        170        180 
EHILLSRQVG VKHLIVFMNK VDLVDDEELL ELVEMEIRDL LSEYDFPGDD IPVIQGSALK 

       190        200        210        220        230        240 
ALEGDSKYED IIMDLMNTVD EYIPEPERDT DKPLLLPVED VFSITGRGTV ASGRIDRGVV 

       250        260        270        280        290        300 
RVNDEVEIVG LKEESQKAVV TGVEMFRKQL DEGIAGDNVG VLLRGIQRDE IERGQVLAAP 

       310        320        330        340        350        360 
GSIKPHTKFK GEVYILTKEE GGRHTPFFNN YRPQFYFRTT DVTGSIELPA GTEMVMPGDN 

       370        380        390 
VTIDVELIHP IAVEKGTTFS IREGGRTVGS GIVTEIEA 

« Hide

References

[1]"Complete sequence and comparative genome analysis of the dairy bacterium Streptococcus thermophilus."
Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D., Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D., Hancy F. expand/collapse author list , Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.
Nat. Biotechnol. 22:1554-1558(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-250 / LMG 18311.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000023 Genomic DNA. Translation: AAV60197.1.
RefSeqYP_139012.1. NC_006448.1.

3D structure databases

ProteinModelPortalQ5M5I8.
SMRQ5M5I8. Positions 2-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264199.stu0487.

Proteomic databases

PRIDEQ5M5I8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV60197; AAV60197; stu0487.
GeneID3163862.
KEGGstl:stu0487.
PATRIC19802560. VBIStrThe97850_0490.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0050.
HOGENOMHOG000229290.
KOK02358.
OMAVTPHTEF.
OrthoDBEOG6R5C6X.
ProtClustDBPRK12736.

Enzyme and pathway databases

BioCycSTHE264199:GI6K-533-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...

Entry information

Entry nameEFTU_STRT2
AccessionPrimary (citable) accession number: Q5M5I8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 1, 2005
Last modified: April 16, 2014
This is version 68 of the entry and version 1 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