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Q0I1U9 (EFTU_HISS1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. 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:HS_0195
AND
Name:tuf2
Synonyms:tufA
Ordered Locus Names:HS_1644
OrganismHistophilus somni (strain 129Pt) (Haemophilus somnus) [Complete proteome] [HAMAP]
Taxonomic identifier205914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

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_0000337400

Regions

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

Sequences

Sequence LengthMass (Da)Tools
Q0I1U9 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 066D3F62731942B4

FASTA39443,386
        10         20         30         40         50         60 
MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLSKHF GGAARAFDQI DNAPEEKARG 

        70         80         90        100        110        120 
ITINTSHVEY DTATRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI 

       130        140        150        160        170        180 
LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALQALN 

       190        200        210        220        230        240 
GVAEWEEKIL ELASHLDNYI PEPERAIDQP FLLPIEDVFS ISGRGTVVTG RVERGIIRTG 

       250        260        270        280        290        300 
EEVEIVGIKE TTKTTVTGVE MFRKLLDEGR AGENIGALLR GTKREEIERG QVLAKPGSIT 

       310        320        330        340        350        360 
PHTDFESEVY VLSKEEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMT 

       370        380        390 
VSLIHPIAMD QGLRFAIREG GRTVGAGVVA KIIK 

« Hide

References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129Pt.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000436 Genomic DNA. Translation: ABI24473.1.
CP000436 Genomic DNA. Translation: ABI25912.1.
RefSeqYP_718402.1. NC_008309.1.
YP_719849.1. NC_008309.1.

3D structure databases

ProteinModelPortalQ0I1U9.
SMRQ0I1U9. Positions 4-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205914.HS_1644.

Proteomic databases

PRIDEQ0I1U9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI24473; ABI24473; HS_0195.
ABI25912; ABI25912; HS_1644.
GeneID4239706.
4241171.
KEGGhso:HS_0195.
hso:HS_1644.
PATRIC20280298. VBIHaeSom53361_0207.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0050.
HOGENOMHOG000229290.
KOK02358.
OMAVTPHTEF.
OrthoDBEOG6R5C6X.
ProtClustDBPRK00049.

Enzyme and pathway databases

BioCycHSOM205914:GJ7V-1725-MONOMER.
HSOM205914:GJ7V-201-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_HISS1
AccessionPrimary (citable) accession number: Q0I1U9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 3, 2006
Last modified: April 16, 2014
This is version 61 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