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Q3YRK7 (EFTU_EHRCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. 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:tuf1
Ordered Locus Names:Ecaj_0162
AND
Name:tuf2
Ordered Locus Names:Ecaj_0614
OrganismEhrlichia canis (strain Jake) [Complete proteome] [HAMAP]
Taxonomic identifier269484 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia

Protein attributes

Sequence length395 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 – 395395Elongation factor Tu HAMAP-Rule MF_00118
PRO_0000337374

Regions

Nucleotide binding15 – 228GTP By similarity
Nucleotide binding80 – 845GTP By similarity
Nucleotide binding135 – 1384GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3YRK7 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 9530194A1407386D

FASTA39543,481
        10         20         30         40         50         60 
MVEERKPHIN VGTIGHVDHG KTTLTAALTT VLAKRLSGEG NKSVKYDEID KAPEEKARGI 

        70         80         90        100        110        120 
TISTAHVEYE TENRHYAHVD CPGHADYIKN MITGAAQMDA AILVVSATDG AMPQTREHIL 

       130        140        150        160        170        180 
LAKQVGVKDI VVWMNKCDVV DDEEMLSLVE MEIRELLSKY GYPGDDIDVV RGSAVKALEE 

       190        200        210        220        230        240 
ETGSGVWSEK IMELMNALEK ISLPVREKDK PFLMSIEDVF SIPGRGTVVT GRIERGVIRV 

       250        260        270        280        290        300 
GDKIEIVGLR EIQSTVCTGV EMFHKALDAG EAGDNAGILL RGIKKEDVER GQVLSAPGQI 

       310        320        330        340        350        360 
HSYKRFKAEV YILKKEEGGR HTPFFSNYQP QFYVRTTDVT GNIKLPEGVE MVMPGDNINI 

       370        380        390 
EVSLDKPVAI DQGLRFAIRE GGRTVGSGII TEILE 

« Hide

References

[1]"The genome of the obligately intracellular bacterium Ehrlichia canis reveals themes of complex membrane structure and immune evasion strategies."
Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.
J. Bacteriol. 188:4015-4023(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Jake.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000107 Genomic DNA. Translation: AAZ68213.1.
CP000107 Genomic DNA. Translation: AAZ68648.1.
RefSeqYP_302811.1. NC_007354.1.
YP_303246.1. NC_007354.1.

3D structure databases

ProteinModelPortalQ3YRK7.
SMRQ3YRK7. Positions 3-394.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269484.Ecaj_0614.

Proteomic databases

PRIDEQ3YRK7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ68213; AAZ68213; Ecaj_0162.
AAZ68648; AAZ68648; Ecaj_0614.
GeneID3618072.
3618360.
KEGGecn:Ecaj_0162.
ecn:Ecaj_0614.
PATRIC20573812. VBIEhrCan118076_0178.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycECAN269484:GI02-172-MONOMER.
ECAN269484:GI02-645-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_EHRCJ
AccessionPrimary (citable) accession number: Q3YRK7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 27, 2005
Last modified: April 16, 2014
This is version 70 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