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P60339

- EFTU2_THET8

UniProt

P60339 - EFTU2_THET8

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Protein

Elongation factor Tu-B

Gene

tufB

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 268GTPUniRule annotation
Nucleotide bindingi82 – 865GTPUniRule annotation
Nucleotide bindingi137 – 1404GTPUniRule annotation

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-HAMAP
  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-BUniRule annotation
Short name:
EF-Tu-BUniRule annotation
Gene namesi
Name:tufBUniRule annotation
Ordered Locus Names:TTHA0251
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 406405Elongation factor Tu-BPRO_0000091424Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Phosphorylated on a threonine.By similarity

Keywords - PTMi

Phosphoprotein

PTM databases

PhosSiteiP12101832.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi300852.TTHA0251.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 187Combined sources
Helixi25 – 3915Combined sources
Helixi48 – 514Combined sources
Helixi55 – 606Combined sources
Beta strandi67 – 726Combined sources
Beta strandi77 – 826Combined sources
Helixi87 – 893Combined sources
Helixi90 – 978Combined sources
Beta strandi101 – 1088Combined sources
Turni109 – 1113Combined sources
Helixi115 – 12713Combined sources
Beta strandi132 – 1376Combined sources
Helixi139 – 1413Combined sources
Helixi145 – 16117Combined sources
Turni166 – 1683Combined sources
Beta strandi171 – 1733Combined sources
Helixi176 – 18510Combined sources
Beta strandi191 – 1944Combined sources
Helixi195 – 21016Combined sources
Beta strandi218 – 2203Combined sources
Beta strandi223 – 2253Combined sources
Beta strandi228 – 2325Combined sources
Turni233 – 2353Combined sources
Beta strandi236 – 2427Combined sources
Beta strandi245 – 2484Combined sources
Beta strandi253 – 26210Combined sources
Beta strandi264 – 27310Combined sources
Beta strandi286 – 2938Combined sources
Helixi296 – 2983Combined sources
Beta strandi304 – 3074Combined sources
Beta strandi310 – 32314Combined sources
Helixi326 – 3283Combined sources
Beta strandi330 – 3334Combined sources
Beta strandi342 – 3454Combined sources
Beta strandi348 – 3558Combined sources
Beta strandi368 – 38114Combined sources
Beta strandi386 – 3916Combined sources
Beta strandi394 – 40411Combined sources

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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60339.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 268G1By similarity
Regioni61 – 655G2By similarity
Regioni82 – 854G3By similarity
Regioni137 – 1404G4By similarity
Regioni175 – 1773G5By similarity

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.UniRule annotation

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

        10         20         30         40         50
MAKGEFIRTK PHVNVGTIGH VDHGKTTLTA ALTFVTAAEN PNVEVKDYGD
60 70 80 90 100
IDKAPEERAR GITINTAHVE YETAKRHYSH VDCPGHADYI KNMITGAAQM
110 120 130 140 150
DGAILVVSAA DGPMPQTREH ILLARQVGVP YIVVFMNKVD MVDDPELLDL
160 170 180 190 200
VEMEVRDLLN QYEFPGDEVP VIRGSALLAL EQMHRNPKTR RGENEWVDKI
210 220 230 240 250
WELLDAIDEY IPTPVRDVDK PFLMPVEDVF TITGRGTVAT GRIERGKVKV
260 270 280 290 300
GDEVEIVGLA PETRKTVVTG VEMHRKTLQE GIAGDNVGVL LRGVSREEVE
310 320 330 340 350
RGQVLAKPGS ITPHTKFEAS VYVLKKEEGG RHTGFFSGYR PQFYFRTTDV
360 370 380 390 400
TGVVQLPPGV EMVMPGDNVT FTVELIKPVA LEEGLRFAIR EGGRTVGAGV

VTKILE
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: October 29, 2014
This is version 88 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