Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A8LLG2 (EFTU_DINSH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:Dshi_0223
AND
Name:tuf2
Ordered Locus Names:Dshi_0274
OrganismDinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12) [Complete proteome] [HAMAP]
Taxonomic identifier398580 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeDinoroseobacter

Protein attributes

Sequence length391 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 – 391391Elongation factor Tu HAMAP-Rule MF_00118
PRO_0000337373

Regions

Nucleotide binding19 – 268GTP By similarity
Nucleotide binding76 – 805GTP By similarity
Nucleotide binding131 – 1344GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8LLG2 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: B701ECE5949571A1

FASTA39142,777
        10         20         30         40         50         60 
MAKEKFERSK PHVNIGTIGH VDHGKTTLTA AITKQFGDFK AYDEIDGAPE EKARGITIST 

        70         80         90        100        110        120 
AHVEYETDAR HYAHVDCPGH ADYVKNMITG AAQMDGAILV VNAADGPMPQ TREHILLGRQ 

       130        140        150        160        170        180 
VGIPYMVVFM NKVDQVDDEE LLELVEMEIR ELLSSYEYPG DDIPIIAGSA LAALEGRDPE 

       190        200        210        220        230        240 
IGEQKIAELM KAVDDYIPTP ARAVDQPFLM PIEDVFSISG RGTVVTGRVE RGVINVGDEI 

       250        260        270        280        290        300 
EIVGIRDTKK TTCTGVEMFR KLLDRGEAGD NIGALLRGVD REGVERGQVL CKPGSVTPHT 

       310        320        330        340        350        360 
KFEAEAYILT KEEGGRHTPF FANYRPQFYF RTTDVTGTVT LPEGTEMVMP GDNLKFGVEL 

       370        380        390 
IAPIAMEDGL RFAIREGGRT VGAGVVSKII E 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000830 Genomic DNA. Translation: ABV91972.1.
CP000830 Genomic DNA. Translation: ABV92023.1.
RefSeqYP_001531573.1. NC_009952.1.
YP_001531624.1. NC_009952.1.

3D structure databases

ProteinModelPortalA8LLG2.
SMRA8LLG2. Positions 2-390.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398580.Dshi_0274.

Proteomic databases

PRIDEA8LLG2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV91972; ABV91972; Dshi_0223.
ABV92023; ABV92023; Dshi_0274.
GeneID5711524.
5712148.
KEGGdsh:Dshi_0223.
dsh:Dshi_0274.
PATRIC21812891. VBIDinShi9476_0221.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0050.
HOGENOMHOG000229290.
KOK02358.
OMAISAPAAC.
OrthoDBEOG6R5C6X.

Enzyme and pathway databases

BioCycDSHI398580:GKEL-222-MONOMER.
DSHI398580:GKEL-274-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_DINSH
AccessionPrimary (citable) accession number: A8LLG2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 4, 2007
Last modified: May 14, 2014
This is version 45 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