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Q0K5Z9 (EFTU_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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
Synonyms:tufA
Ordered Locus Names:H16_A3491
AND
Name:tuf2
Synonyms:tufB
Ordered Locus Names:H16_A3505
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length396 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 – 396396Elongation factor Tu HAMAP-Rule MF_00118
PRO_0000337483

Regions

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

Sequences

Sequence LengthMass (Da)Tools
Q0K5Z9 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 265C1E13A2E0163B

FASTA39643,046
        10         20         30         40         50         60 
MAKEKFERTK PHVNVGTIGH VDHGKTTLTA AIATVLAAKF GGAAKKYDEI DAAPEEKARG 

        70         80         90        100        110        120 
ITINTAHVEY ETANRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI 

       130        140        150        160        170        180 
LLARQVGVPY IIVFLNKCDM VDDAELLELV EMEVRELLSK YEFPGDDTPI IKGSAKLALE 

       190        200        210        220        230        240 
GDKGELGEVA IMNLADALDT YIPTPERAVD GTFLMPVEDV FSISGRGTVV TGRIERGVVK 

       250        260        270        280        290        300 
VGEEIEIVGI KPTVKTTCTG VEMFRKLLDQ GQAGDNVGLL LRGTKREDVE RGQVLCKPGS 

       310        320        330        340        350        360 
IKPHTHFTGE VYILSKDEGG RHTPFFNNYR PQFYFRTTDV TGSIELPKDK EMVMPGDNVS 

       370        380        390 
ITVKLIAPIA MEEGLRFAIR EGGRTVGAGV VAKILD 

« Hide

References

[1]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260479 Genomic DNA. Translation: CAJ94559.1.
AM260479 Genomic DNA. Translation: CAJ94572.1.
RefSeqYP_727927.1. NC_008313.1.
YP_727940.1. NC_008313.1.

3D structure databases

ProteinModelPortalQ0K5Z9.
SMRQ0K5Z9. Positions 2-395.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381666.H16_A3505.

Proteomic databases

PRIDEQ0K5Z9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ94559; CAJ94559; H16_A3491.
CAJ94572; CAJ94572; H16_A3505.
GeneID4249009.
4249010.
KEGGreh:H16_A3491.
reh:H16_A3505.
PATRIC35236529. VBIRalEut6770_3885.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0050.
HOGENOMHOG000229290.
KOK02358.
OMADFKAYDQ.
OrthoDBEOG6R5C6X.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-3455-MONOMER.
CNEC381666:GJUJ-3469-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_CUPNH
AccessionPrimary (citable) accession number: Q0K5Z9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 3, 2006
Last modified: May 14, 2014
This is version 60 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