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Q0BKB8 (EFTU_FRATO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 52. 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:FTH_1691
OrganismFrancisella tularensis subsp. holarctica (strain OSU18) [Complete proteome] [HAMAP]
Taxonomic identifier393011 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length394 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 – 394394Elongation factor Tu HAMAP-Rule MF_00118
PRO_1000015663

Regions

Nucleotide binding19 – 268GTP By similarity
Nucleotide binding81 – 855GTP By similarity
Nucleotide binding136 – 1394GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0BKB8 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 53D2BBF0A229CD11

FASTA39443,391
        10         20         30         40         50         60 
MAKEKFERSK PHVNVGTIGH VDHGKTTLTA AITKVMAEKN GGMARKFDEI DSAPEEKARG 

        70         80         90        100        110        120 
ITINTSHVEY ESPNRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI 

       130        140        150        160        170        180 
LLSRQVGVPK IVVFLNKCDM VDDEELLELV EMEVRELLDQ YEFPGDDTPV IMGSALRAIE 

       190        200        210        220        230        240 
GDEAYVEKIV ELVQAMDDYI PAPERDTEKP FILPIEDVFS ISGRGTVVTG RIERGVVNVG 

       250        260        270        280        290        300 
DEVEVVGIRP TQKTTVTGVE MFRKLLDRGE AGDNVGILVR GLKRDDVERG QVLCKPGSIK 

       310        320        330        340        350        360 
PHTKFEAEVY VLSKEEGGRH TPFFKGYRPQ FYFRTTDITG AVELPEGVEM VMPGDNVKMT 

       370        380        390 
ITLINPIAMD EGLRFAIREG GRTVGAGVVA KIIE 

« Hide

References

[1]"Chromosome rearrangement and diversification of Francisella tularensis revealed by the type B (OSU18) genome sequence."
Petrosino J.F., Xiang Q., Karpathy S.E., Jiang H., Yerrapragada S., Liu Y., Gioia J., Hemphill L., Gonzalez A., Raghavan T.M., Uzman A., Fox G.E., Highlander S., Reichard M., Morton R.J., Clinkenbeard K.D., Weinstock G.M.
J. Bacteriol. 188:6977-6985(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OSU18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000437 Genomic DNA. Translation: ABI83466.1.
RefSeqYP_764103.1. NC_008369.1.

3D structure databases

ProteinModelPortalQ0BKB8.
SMRQ0BKB8. Positions 2-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393011.FTH_1691.

Proteomic databases

PRIDEQ0BKB8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI83466; ABI83466; FTH_1691.
GeneID4307427.
KEGGfth:FTH_1691.
PATRIC17953653. VBIFraTul3936_1946.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0050.
HOGENOMHOG000229290.
KOK02358.
OMASHIEYST.
OrthoDBEOG6R5C6X.
ProtClustDBPRK12735.

Enzyme and pathway databases

BioCycFTUL393011:GHFN-1731-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_FRATO
AccessionPrimary (citable) accession number: Q0BKB8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 52 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