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Q0SN31 (EFTU_BORAP) 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:tuf
Ordered Locus Names:BAPKO_0504, BafPKo_0493
OrganismBorrelia afzelii (strain PKo) [Complete proteome] [HAMAP]
Taxonomic identifier390236 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group

Protein attributes

Sequence length394 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 – 394394Elongation factor Tu HAMAP-Rule MF_00118
PRO_1000015619

Regions

Nucleotide binding19 – 268GTP By similarity
Nucleotide binding82 – 865GTP By similarity
Nucleotide binding137 – 1404GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0SN31 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 90CEEA2B0499A948

FASTA39443,354
        10         20         30         40         50         60 
MAKEVFQRTK PHMNVGTIGH VDHGKTTLTA AISIYCSKLN KDAKALKYED IDNAPEEKAR 

        70         80         90        100        110        120 
GITINARHIE YETANRHYAH VDCPGHADYI KNMITGAAQM DAAILLVAAD SGAEPQTKEH 

       130        140        150        160        170        180 
LLLAQRMGIK KIIVFLNKLD LADPELVELV EVEVLELVEK YGFSANTPII KGSAFGAMSN 

       190        200        210        220        230        240 
PEDPEATKCV KELLESMDNY FDLPERDIDK PFLLAVEDVF SISGRGTVAT GRIERGVIKV 

       250        260        270        280        290        300 
GQEVEIVGIK ETRKTTVTGV EMFQKILEQG QAGDNVGLLL RGVDKKDIER GQVLSAPGTI 

       310        320        330        340        350        360 
TPHKKFKASI YCLTKEEGGR HKPFFPGYRP QFFFRTTDVT GVVALEGKEM VMPGDNVDIV 

       370        380        390 
VELISSIAMD KNVEFAVREG GRTVASGRIL EILE 

« Hide

References

[1]"Comparative genome analysis: selection pressure on the Borrelia vls cassettes is essential for infectivity."
Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J., Wilske B., Platzer M.
BMC Genomics 7:211-211(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PKo.
[2]"Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii Lyme disease agent isolates."
Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J., Fraser-Liggett C.M., Schutzer S.E.
J. Bacteriol. 193:6995-6996(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PKo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000395 Genomic DNA. Translation: ABH01747.1.
CP002933 Genomic DNA. Translation: AEL69701.1.
RefSeqYP_005592691.1. NC_017238.1.
YP_709923.1. NC_008277.1.

3D structure databases

ProteinModelPortalQ0SN31.
SMRQ0SN31. Positions 2-394.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390236.BAPKO_0504.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABH01747; ABH01747; BAPKO_0504.
AEL69701; AEL69701; BafPKo_0493.
GeneID12159441.
4227955.
KEGGbaf:BAPKO_0504.
bafz:BafPKo_0493.
PATRIC37189281. VBIBorAfz3878_0540.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0050.
HOGENOMHOG000229290.
KOK02358.
OMAGTEMCMP.
OrthoDBEOG6R5C6X.

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_BORAP
AccessionPrimary (citable) accession number: Q0SN31
Secondary accession number(s): G0ISC0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 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