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P60339

- EFTU2_THET8

UniProt

P60339 - EFTU2_THET8

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Protein
Elongation factor Tu-B
Gene
tufB, TTHA0251
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 268GTP By similarity
Nucleotide bindingi82 – 865GTP By similarity
Nucleotide bindingi137 – 1404GTP By similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-HAMAP
  2. GTPase activity Source: InterPro
  3. translation elongation factor activity Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-261-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor Tu-B
Short name:
EF-Tu-B
Gene namesi
Name:tufB
Ordered Locus Names:TTHA0251
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 406405Elongation factor Tu-BUniRule annotation
PRO_0000091424Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei395 – 3951Phosphothreonine By similarity

Post-translational modificationi

Phosphorylated on a threonine By similarity.UniRule annotation

Keywords - PTMi

Phosphoprotein

PTM databases

PhosSiteiP12101832.

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi300852.TTHA0251.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 187
Helixi25 – 3915
Helixi48 – 514
Helixi55 – 606
Beta strandi67 – 726
Beta strandi77 – 826
Helixi87 – 893
Helixi90 – 978
Beta strandi101 – 1088
Turni109 – 1113
Helixi115 – 12713
Beta strandi132 – 1376
Helixi139 – 1413
Helixi145 – 16117
Turni166 – 1683
Beta strandi171 – 1733
Helixi176 – 18510
Beta strandi191 – 1944
Helixi195 – 21016
Beta strandi218 – 2203
Beta strandi223 – 2253
Beta strandi228 – 2325
Turni233 – 2353
Beta strandi236 – 2427
Beta strandi245 – 2484
Beta strandi253 – 26210
Beta strandi264 – 27310
Beta strandi286 – 2938
Helixi296 – 2983
Beta strandi304 – 3074
Beta strandi310 – 32314
Helixi326 – 3283
Beta strandi330 – 3334
Beta strandi342 – 3454
Beta strandi348 – 3558
Beta strandi368 – 38114
Beta strandi386 – 3916
Beta strandi394 – 40411

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C77X-ray1.60A2-406[»]
2P8Welectron microscopy11.30S36-70[»]
2P8Xelectron microscopy9.70S36-70[»]
2P8Zelectron microscopy8.90S36-70[»]
2XQDX-ray3.10Z2-406[»]
3DWUelectron microscopy12.60A21-66[»]
3FICelectron microscopy6.40Z2-406[»]
ProteinModelPortaliP60339.
SMRiP60339. Positions 4-406.

Miscellaneous databases

EvolutionaryTraceiP60339.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 215206tr-type G
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 268G1 By similarity
Regioni61 – 655G2 By similarity
Regioni82 – 854G3 By similarity
Regioni137 – 1404G4 By similarity
Regioni175 – 1773G5 By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0050.
HOGENOMiHOG000229290.
KOiK02358.
OMAiSSYSISH.
OrthoDBiEOG6R5C6X.
PhylomeDBiP60339.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_B. EF_Tu_B.
InterProiIPR000795. 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]
PfamiPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00485. EF-Tu. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P60339-1 [UniParc]FASTAAdd to Basket

« Hide

MAKGEFIRTK PHVNVGTIGH VDHGKTTLTA ALTFVTAAEN PNVEVKDYGD    50
IDKAPEERAR GITINTAHVE YETAKRHYSH VDCPGHADYI KNMITGAAQM 100
DGAILVVSAA DGPMPQTREH ILLARQVGVP YIVVFMNKVD MVDDPELLDL 150
VEMEVRDLLN QYEFPGDEVP VIRGSALLAL EQMHRNPKTR RGENEWVDKI 200
WELLDAIDEY IPTPVRDVDK PFLMPVEDVF TITGRGTVAT GRIERGKVKV 250
GDEVEIVGLA PETRKTVVTG VEMHRKTLQE GIAGDNVGVL LRGVSREEVE 300
RGQVLAKPGS ITPHTKFEAS VYVLKKEEGG RHTGFFSGYR PQFYFRTTDV 350
TGVVQLPPGV EMVMPGDNVT FTVELIKPVA LEEGLRFAIR EGGRTVGAGV 400
VTKILE 406
Length:406
Mass (Da):44,782
Last modified:January 23, 2007 - v2
Checksum:i38D5E2D8F1B645DD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X61957 Genomic DNA. Translation: CAA43956.1.
AP008226 Genomic DNA. Translation: BAD70074.1.
PIRiS00229.
S17146.
RefSeqiWP_011227805.1. NC_006461.1.
YP_143517.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70074; BAD70074; BAD70074.
GeneIDi3168327.
KEGGittj:TTHA0251.
PATRICi23955449. VBITheThe93045_0251.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X61957 Genomic DNA. Translation: CAA43956.1 .
AP008226 Genomic DNA. Translation: BAD70074.1 .
PIRi S00229.
S17146.
RefSeqi WP_011227805.1. NC_006461.1.
YP_143517.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C77 X-ray 1.60 A 2-406 [» ]
2P8W electron microscopy 11.30 S 36-70 [» ]
2P8X electron microscopy 9.70 S 36-70 [» ]
2P8Z electron microscopy 8.90 S 36-70 [» ]
2XQD X-ray 3.10 Z 2-406 [» ]
3DWU electron microscopy 12.60 A 21-66 [» ]
3FIC electron microscopy 6.40 Z 2-406 [» ]
ProteinModelPortali P60339.
SMRi P60339. Positions 4-406.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHA0251.

PTM databases

PhosSitei P12101832.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD70074 ; BAD70074 ; BAD70074 .
GeneIDi 3168327.
KEGGi ttj:TTHA0251.
PATRICi 23955449. VBITheThe93045_0251.

Phylogenomic databases

eggNOGi COG0050.
HOGENOMi HOG000229290.
KOi K02358.
OMAi SSYSISH.
OrthoDBi EOG6R5C6X.
PhylomeDBi P60339.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-261-MONOMER.

Miscellaneous databases

EvolutionaryTracei P60339.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00118_B. EF_Tu_B.
InterProi IPR000795. 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 ]
Pfami PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view ]
PRINTSi PR00315. ELONGATNFCT.
SUPFAMi SSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00485. EF-Tu. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEi PS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiEFTU2_THET8
AccessioniPrimary (citable) accession number: P60339
Secondary accession number(s): P07157, Q5SLP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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