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Q2W2H3 (EFTU_MAGSA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 71. 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:amb3132
AND
Name:tuf2
Ordered Locus Names:amb3148
OrganismMagnetospirillum magneticum (strain AMB-1 / ATCC 700264) [Complete proteome] [HAMAP]
Taxonomic identifier342108 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeMagnetospirillum

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_0000337427

Regions

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

Sequences

Sequence LengthMass (Da)Tools
Q2W2H3 [UniParc].

Last modified January 10, 2006. Version 1.
Checksum: 9BA6343579D588CA

FASTA39643,053
        10         20         30         40         50         60 
MAKAKFERNK PHCNIGTIGH VDHGKTSLTA AITKILAETG GATFTAYDQI DKAPEEKARG 

        70         80         90        100        110        120 
ITISTAHVEY ETSNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI 

       130        140        150        160        170        180 
LLARQVGVPA LVVFMNKCDM VDDPELLDLV ELEVRELLSS YDFPGDDIPI VRGSALCALE 

       190        200        210        220        230        240 
DKQPEIGRDA ILKLMAEVDA YIPQPERPKD KPFLMPIEDV FSISGRGTVV TGRVERGVVK 

       250        260        270        280        290        300 
VGEEVEIVGI KNTVKTTCTG VEMFRKLLDQ GEAGDNIGAL LRGTKREDVE RGQVLAAPGS 

       310        320        330        340        350        360 
ITPHTDFEAE AYILNKEEGG RHTPFFTNYR PQFYFRTTDV TGVVALPEGT EMVMPGDNVK 

       370        380        390 
MIVTLIAPIA MDQGLRFAIR EGGRTVGAGV VAKIIK 

« Hide

References

[1]"Complete genome sequence of the facultative anaerobic magnetotactic bacterium Magnetospirillum sp. strain AMB-1."
Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.
DNA Res. 12:157-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AMB-1 / ATCC 700264.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007255 Genomic DNA. Translation: BAE51936.1.
AP007255 Genomic DNA. Translation: BAE51952.1.
RefSeqYP_422495.1. NC_007626.1.
YP_422511.1. NC_007626.1.

3D structure databases

ProteinModelPortalQ2W2H3.
SMRQ2W2H3. Positions 2-395.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342108.amb3148.

Proteomic databases

PRIDEQ2W2H3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE51936; BAE51936; amb3132.
BAE51952; BAE51952; amb3148.
GeneID3804789.
3804890.
KEGGmag:amb3132.
mag:amb3148.
PATRIC22440559. VBIMagMag129836_3113.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0050.
HOGENOMHOG000229290.
KOK02358.
OMAGTEMCMP.
OrthoDBEOG6R5C6X.

Enzyme and pathway databases

BioCycMMAG342108:GJNU-3167-MONOMER.
MMAG342108:GJNU-3184-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_MAGSA
AccessionPrimary (citable) accession number: Q2W2H3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 10, 2006
Last modified: May 14, 2014
This is version 71 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