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Q7VA05 (EFTU_PROMA) 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:tuf
Ordered Locus Names:Pro_1664
OrganismProchlorococcus marinus (strain SARG / CCMP1375 / SS120) [Reference proteome] [HAMAP]
Taxonomic identifier167539 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length399 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
Reference 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 – 399399Elongation factor Tu HAMAP-Rule MF_00118
PRO_1000015728

Regions

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

Sequences

Sequence LengthMass (Da)Tools
Q7VA05 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: E11DE93F93A71AA0

FASTA39943,548
        10         20         30         40         50         60 
MAREKFERNK PHVNIGTIGH VDHGKTTLTA AITNVLAKKG QAQAQDYGDI DGAPEERERG 

        70         80         90        100        110        120 
ITINTAHVEY ETDGRHYAHV DCPGHADYVK NMITGAAQMD GAILVCAATD GPMAQTKEHI 

       130        140        150        160        170        180 
LLAKQVGVPA LVVALNKCDM VDDPEIIELV EMEIRELLDS YDFPGDEIPI VQVSGLKALE 

       190        200        210        220        230        240 
GDSEWEGKVE ELMKAVDASI PEPEREVDKP FLMAVEDVFS ITGRGTVATG RIERGKVTVG 

       250        260        270        280        290        300 
EEVEIVGIRD TRLTTVTGVE MFRKLLDEGM AGDNVGLLLR GIQKEDIERG MVLVKKGSIT 

       310        320        330        340        350        360 
PHTQFEGEVY VLKKEEGGRH TPFFAGYRPQ FYIRTTDVTG QITAFTADDG SSVEMVMPGD 

       370        380        390 
RIKMTGELIC PVAIEQGMRF AIREGGRTIG AGVVSKIIK 

« Hide

References

[1]"Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a nearly minimal oxyphototrophic genome."
Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M., Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J., Tandeau de Marsac N., Weissenbach J. expand/collapse author list , Wincker P., Wolf Y.I., Hess W.R.
Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SARG / CCMP1375 / SS120.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017126 Genomic DNA. Translation: AAQ00708.1.
RefSeqNP_876055.1. NC_005042.1.

3D structure databases

ProteinModelPortalQ7VA05.
SMRQ7VA05. Positions 2-398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167539.Pro1664.

Proteomic databases

PRIDEQ7VA05.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ00708; AAQ00708; Pro_1664.
GeneID1463046.
KEGGpma:Pro_1664.
PATRIC23030155. VBIProMar8617_1758.

Phylogenomic databases

eggNOGCOG0050.
KOK02358.
OMATGQITAF.
OrthoDBEOG6R5C6X.
ProtClustDBPRK00049.

Enzyme and pathway databases

BioCycPMAR167539:GJN2-1701-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_PROMA
AccessionPrimary (citable) accession number: Q7VA05
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2003
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