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P60339 (EFTU2_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Elongation factor Tu-B
Short name=EF-Tu-B
Gene names
Name:tufB
Ordered Locus Names:TTHA0251
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus ›

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. HAMAP-Rule MF_00118_B

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm HAMAP-Rule MF_00118_B.

Post-translational modification

Phosphorylated on a threonine By similarity.

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
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference 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: HAMAP

GTPase activity

Inferred from electronic annotation. Source: InterPro

translation elongation factor activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 406405Elongation factor Tu-B HAMAP-Rule MF_00118_B
PRO_0000091424

Regions

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

Amino acid modifications

Modified residue3951Phosphothreonine By similarity

Secondary structure

1 ........................................................................ 406
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60339 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 38D5E2D8F1B645DD

FASTA40644,782
        10         20         30         40         50         60 
MAKGEFIRTK PHVNVGTIGH VDHGKTTLTA ALTFVTAAEN PNVEVKDYGD IDKAPEERAR 

        70         80         90        100        110        120 
GITINTAHVE YETAKRHYSH VDCPGHADYI KNMITGAAQM DGAILVVSAA DGPMPQTREH 

       130        140        150        160        170        180 
ILLARQVGVP YIVVFMNKVD MVDDPELLDL VEMEVRDLLN QYEFPGDEVP VIRGSALLAL 

       190        200        210        220        230        240 
EQMHRNPKTR RGENEWVDKI WELLDAIDEY IPTPVRDVDK PFLMPVEDVF TITGRGTVAT 

       250        260        270        280        290        300 
GRIERGKVKV GDEVEIVGLA PETRKTVVTG VEMHRKTLQE GIAGDNVGVL LRGVSREEVE 

       310        320        330        340        350        360 
RGQVLAKPGS ITPHTKFEAS VYVLKKEEGG RHTGFFSGYR PQFYFRTTDV TGVVQLPPGV 

       370        380        390        400 
EMVMPGDNVT FTVELIKPVA LEEGLRFAIR EGGRTVGAGV VTKILE

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, nucleotide sequence and expression of the tufB gene encoding elongation factor Tu from Thermus thermophilus HB8."
Satoh M., Tanaka T., Kushiro A., Hakoshima T., Tomita K.
FEBS Lett. 288:98-100(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X61957 Genomic DNA. Translation: CAA43956.1.
AP008226 Genomic DNA. Translation: BAD70074.1.
PIRS00229.
S17146.
RefSeqYP_143517.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C77X-ray1.60A2-405[»]
2P8Welectron microscopy11.30S36-70[»]
2P8Xelectron microscopy9.70S36-70[»]
2P8Zelectron microscopy8.90S36-70[»]
2XQDX-ray3.10Z2-406[»]
3DWUelectron microscopy12.60A21-66[»]
3FICelectron microscopy6.40Z2-406[»]
ProteinModelPortalP60339.
SMRP60339. Positions 4-406.
ModBaseSearch...

Protein-protein interaction databases

STRING300852.TTHA0251.

PTM databases

PhosSiteP12101832.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD70074; BAD70074; BAD70074.
GeneID3168327.
KEGGttj:TTHA0251.
PATRIC23955449. VBITheThe93045_0251.

Phylogenomic databases

eggNOGCOG0050.
HOGENOMHOG000229290.
KOK02358.
OMASSYSISH.
ProtClustDBPRK12735.

Family and domain databases

HAMAPMF_00118_B. EF_Tu_B.
InterProIPR000795. EF_GTP-bd_dom.
IPR005225. Small_GTP-bd_dom.
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.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50465. Elong_init_C. 1 hit.
SSF50447. Translat_factor. 1 hit.
TIGRFAMsTIGR00485. EF-Tu. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP60339.

Entry information

Entry nameEFTU2_THET8
AccessionPrimary (citable) accession number: P60339
Secondary accession number(s): P07157, Q5SLP2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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