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Q5SHN6

- EFTU1_THET8

UniProt

Q5SHN6 - EFTU1_THET8

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Protein
Elongation factor Tu-A
Gene
tufA, tuf, TTHA1694
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 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 – 268GTPUniRule annotation
Nucleotide bindingi82 – 865GTPUniRule annotation
Nucleotide bindingi137 – 1404GTPUniRule annotation

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-1733-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor Tu-A
Short name:
EF-Tu-A
Gene namesi
Name:tufA
Synonyms:tuf
Ordered Locus Names:TTHA1694
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 – 11RemovedUniRule annotation
Chaini2 – 406405Elongation factor Tu-AUniRule annotation
PRO_0000091423Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Phosphorylated on a threonine.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ5SHN6.

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi300852.TTHA1694.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 187
Beta strandi20 – 245
Helixi25 – 3814
Helixi48 – 514
Helixi55 – 606
Beta strandi67 – 726
Beta strandi77 – 826
Helixi87 – 893
Helixi90 – 978
Beta strandi101 – 1088
Turni109 – 1113
Helixi115 – 12612
Beta strandi132 – 1376
Helixi139 – 1413
Helixi145 – 16117
Turni166 – 1683
Beta strandi171 – 1733
Helixi176 – 18510
Beta strandi191 – 1933
Helixi195 – 21016
Beta strandi218 – 2203
Beta strandi223 – 2253
Beta strandi228 – 2325
Turni233 – 2353
Beta strandi236 – 2427
Beta strandi245 – 2495
Beta strandi253 – 26210
Beta strandi264 – 27310
Beta strandi276 – 2827
Beta strandi286 – 2938
Turni296 – 2983
Beta strandi304 – 3074
Beta strandi310 – 32314
Helixi326 – 3283
Beta strandi342 – 3454
Beta strandi348 – 3558
Beta strandi357 – 3593
Beta strandi365 – 3673
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
1HA3X-ray2.00A/B2-406[»]
2C78X-ray1.40A2-406[»]
2WRNX-ray3.60Z1-406[»]
2WRQX-ray3.60Z1-406[»]
2Y0UX-ray3.10Z2-406[»]
2Y0WX-ray3.10Z2-406[»]
2Y0YX-ray3.10Z2-406[»]
2Y10X-ray3.10Z2-406[»]
2Y12X-ray3.10Z2-406[»]
2Y14X-ray3.10Z2-406[»]
2Y16X-ray3.10Z2-406[»]
2Y18X-ray3.10Z2-406[»]
4ABRX-ray3.10Z2-406[»]
ProteinModelPortaliQ5SHN6.
SMRiQ5SHN6. Positions 10-406.

Miscellaneous databases

EvolutionaryTraceiQ5SHN6.

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.
OMAiGTEMCMP.
OrthoDBiEOG6R5C6X.
PhylomeDBiQ5SHN6.

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.

Q5SHN6-1 [UniParc]FASTAAdd to Basket

« Hide

MAKGEFVRTK PHVNVGTIGH VDHGKTTLTA ALTYVAAAEN 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 PETRRTVVTG 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 - v3
Checksum:iBA597518358269E4
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti380 – 3801A → G in CAA29397. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05977 Genomic DNA. Translation: CAA29397.1.
X06657 Genomic DNA. Translation: CAA29856.1.
AP008226 Genomic DNA. Translation: BAD71517.1.
PIRiS00229.
S17146.
RefSeqiWP_011228847.1. NC_006461.1.
YP_144960.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71517; BAD71517; BAD71517.
GeneIDi3167925.
KEGGittj:TTHA1694.
PATRICi23958343. VBITheThe93045_1664.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05977 Genomic DNA. Translation: CAA29397.1 .
X06657 Genomic DNA. Translation: CAA29856.1 .
AP008226 Genomic DNA. Translation: BAD71517.1 .
PIRi S00229.
S17146.
RefSeqi WP_011228847.1. NC_006461.1.
YP_144960.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HA3 X-ray 2.00 A/B 2-406 [» ]
2C78 X-ray 1.40 A 2-406 [» ]
2WRN X-ray 3.60 Z 1-406 [» ]
2WRQ X-ray 3.60 Z 1-406 [» ]
2Y0U X-ray 3.10 Z 2-406 [» ]
2Y0W X-ray 3.10 Z 2-406 [» ]
2Y0Y X-ray 3.10 Z 2-406 [» ]
2Y10 X-ray 3.10 Z 2-406 [» ]
2Y12 X-ray 3.10 Z 2-406 [» ]
2Y14 X-ray 3.10 Z 2-406 [» ]
2Y16 X-ray 3.10 Z 2-406 [» ]
2Y18 X-ray 3.10 Z 2-406 [» ]
4ABR X-ray 3.10 Z 2-406 [» ]
ProteinModelPortali Q5SHN6.
SMRi Q5SHN6. Positions 10-406.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHA1694.

Proteomic databases

PRIDEi Q5SHN6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD71517 ; BAD71517 ; BAD71517 .
GeneIDi 3167925.
KEGGi ttj:TTHA1694.
PATRICi 23958343. VBITheThe93045_1664.

Phylogenomic databases

eggNOGi COG0050.
HOGENOMi HOG000229290.
KOi K02358.
OMAi GTEMCMP.
OrthoDBi EOG6R5C6X.
PhylomeDBi Q5SHN6.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-1733-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q5SHN6.

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. "Sequence and identification of the nucleotide binding site for the elongation factor Tu from Thermus thermophilus HB8."
    Seidler L., Peter M., Meissner F., Sprinzl M.
    Nucleic Acids Res. 15:9263-9277(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular cloning and sequence determination of the tuf gene coding for the elongation factor Tu of Thermus thermophilus HB8."
    Kushiro A., Shimizu M., Tomita K.
    Eur. J. Biochem. 170:93-98(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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.
  4. "Prokaryotic elongation factor Tu is phosphorylated in vivo."
    Lippmann C., Lindschau C., Vijgenboom E., Schroeder W., Bosch L., Erdmann V.A.
    J. Biol. Chem. 268:601-607(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  5. "Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox."
    Vogeley L., Palm G.J., Mesters J.R., Hilgenfeld R.
    J. Biol. Chem. 276:17149-17155(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF COMPLEX WITH GDP AND AURODOX.

Entry informationi

Entry nameiEFTU1_THET8
AccessioniPrimary (citable) accession number: Q5SHN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 81 of the entry and version 3 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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