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A2BYN4 (EFTU_PROM5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:P9515_16881
OrganismProchlorococcus marinus (strain MIT 9515) [Complete proteome] [HAMAP]
Taxonomic identifier167542 [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
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from electronic annotation. Source: GOC

   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_1000015726

Regions

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

Sequences

Sequence LengthMass (Da)Tools
A2BYN4 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 9AE4516E0512CC97

FASTA39943,678
        10         20         30         40         50         60 
MAREKFERNK PHVNIGTIGH VDHGKTTLTA AITNVLAKKG QAQAQDYGDI DGAPEERERG 

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

       130        140        150        160        170        180 
LLAKQVGVPA LVVALNKCDM VDDEEIIELV EMEIRELLDS YDFPGDDIPI VQVSGLKALE 

       190        200        210        220        230        240 
GDSNWESKIE ELMKAVDASI PEPEREIDKP FLMAIEDVFS ITGRGTVATG RIERGKVKVG 

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

       310        320        330        340        350        360 
PHTKFEGEVY VLKKEEGGRH TPFFAGYRPQ FYIRTTDVTG QITAFTSDDG ANVEMVMPGD 

       370        380        390 
RIKMTGELIC PVAIEQGMRF AIREGGRTIG AGVVSKIIE 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9515.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000552 Genomic DNA. Translation: ABM72895.1.
RefSeqYP_001012002.1. NC_008817.1.

3D structure databases

ProteinModelPortalA2BYN4.
SMRA2BYN4. Positions 2-398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167542.P9515_16881.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM72895; ABM72895; P9515_16881.
GeneID4720197.
KEGGpmc:P9515_16881.
PATRIC23017046. VBIProMar113831_1735.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0050.
HOGENOMHOG000229290.
KOK02358.
OMATGQITAF.
OrthoDBEOG6R5C6X.
ProtClustDBPRK00049.

Enzyme and pathway databases

BioCycPMAR167542:GI3N-1736-MONOMER.

Family and domain databases

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_PROM5
AccessionPrimary (citable) accession number: A2BYN4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 20, 2007
Last modified: February 19, 2014
This is version 48 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