SubmitCancel

Skip Header

P0A6P1

- EFTS_ECOLI

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here

Protein
Elongation factor Ts
Gene
tsf, b0170, JW0165

Gene:

tsf, b0170, JW0165
Organism
Escherichia coli (strain K12)
Status
Reviewed - - Experimental evidence at protein leveli

UniProt

P0A6P1 - EFTS_ECOLI

Protein:

Elongation factor Ts
Protein Existence: Experimental evidence at protein level

Functioni

Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.UniRule annotation

GO - Molecular functioni

  1. guanyl-nucleotide exchange factor activityInferred from direct assayi PubMed 11772013 Source: EcoCyc
  2. translation elongation factor activityInferred from electronic annotationi Source: UniProtKB-HAMAP
  3. zinc ion bindingInferred from direct assayi PubMed 11985624 Source: EcoliWiki
Complete GO annotation...

GO - Biological processi

  1. guanyl-nucleotide exchange factor activityInferred from direct assayi PubMed 11772013 Source: EcoCyc
  2. translation elongation factor activityInferred from electronic annotationi Source: UniProtKB-HAMAP
  3. zinc ion bindingInferred from direct assayi PubMed 11985624 Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG11033-MONOMER.
ECOL316407:JW0165-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor Ts
Short name:
EF-Ts
Gene namesi
Name:tsf
Ordered Locus Names:b0170, JW0165
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11033. tsf.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasmInferred from direct assayi PubMed 16858726 Source: UniProtKB
  2. membraneInferred from direct assayi PubMed 16858726 Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Mutagenesisi241K → A: No change in binding to EF-Tu and in promoting GDP exchange. 1 Publication
Mutagenesisi811D → A: 2 to 3-fold less active in promoting GDP exchange and slightly lower binding constant for interaction with EF-Tu. 1 Publication
Mutagenesisi821F → A: 2 to 3-fold less active in promoting GDP exchange and 6-fold less active in binding to EF-Tu. 1 Publication
Mutagenesisi1481H → A: At least 100-fold decrease in affinity between EF-Ts and EF-Tu and only small amount of GDP exchange activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Initiator methioninei11Removed3 Publications
Chaini2 – 283282Elongation factor TsUniRule annotation
PRO_0000161117

Proteomic databases

PaxDbiP0A6P1.
PRIDEiP0A6P1.

2D gel databases

SWISS-2DPAGEiP0A6P1.

PTM databases

PhosSiteiP0810442.

Expressioni

Gene expression databases

GenevestigatoriP0A6P1.

Interactioni

Subunit structurei

Heterotetramer composed of two EF-Ts.EF-Tu dimer complexes.

Binary interactionsi

WithEntry#Exp.IntActNotes
tufAP0CE477EBI-301164,EBI-301077

Protein-protein interaction databases

DIPiDIP-31835N.
IntActiP0A6P1. 10 interactions.
MINTiMINT-1273899.
STRINGi511145.b0170.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Helixi6 – 1611
Helixi20 – 2910
Turni30 – 323
Helixi34 – 5219
Beta strandi59 – 679
Beta strandi70 – 7910
Helixi81 – 844
Helixi87 – 10216
Helixi108 – 12619
Beta strandi131 – 1399
Beta strandi141 – 1488
Turni149 – 1513
Beta strandi152 – 1609
Helixi163 – 17614
Beta strandi179 – 1824
Helixi183 – 1853
Helixi188 – 20417
Helixi209 – 22719
Turni229 – 2313
Beta strandi232 – 2343
Beta strandi237 – 2415
Helixi242 – 2476
Turni248 – 2503
Beta strandi252 – 2609
Turni261 – 2644
Helixi272 – 2798

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EFUX-ray2.50B/D2-283[»]
3MMPX-ray2.50A/C1-283[»]
ProteinModelPortaliP0A6P1.
SMRiP0A6P1. Positions 2-283.

Miscellaneous databases

EvolutionaryTraceiP0A6P1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Regioni80 – 834Involved in Mg(2+) ion dislocation from EF-TuUniRule annotation

Sequence similaritiesi

Belongs to the EF-Ts family.

Phylogenomic databases

eggNOGiCOG0264.
HOGENOMiHOG000220986.
KOiK02357.
OMAiADCSKEW.
OrthoDBiEOG66B42N.
ProtClustDBiPRK09377.

Family and domain databases

Gene3Di3.30.479.20. 2 hits.
HAMAPiMF_00050. EF_Ts.
InterProiIPR001816. Transl_elong_EFTs/EF1B.
IPR014039. Transl_elong_EFTs/EF1B_dimer.
IPR018101. Transl_elong_Ts_CS.
IPR009060. UBA-like.
IPR000449. UBA/Ts_N.
[Graphical view]
PANTHERiPTHR11741. PTHR11741. 1 hit.
PfamiPF00889. EF_TS. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54713. SSF54713. 2 hits.
TIGRFAMsiTIGR00116. tsf. 1 hit.
PROSITEiPS01126. EF_TS_1. 1 hit.
PS01127. EF_TS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A6P1-1 [UniParc]FASTA

« Hide

MAEITASLVK ELRERTGAGM MDCKKALTEA NGDIELAIEN MRKSGAIKAA    50
KKAGNVAADG VIKTKIDGNY GIILEVNCQT DFVAKDAGFQ AFADKVLDAA 100
VAGKITDVEV LKAQFEEERV ALVAKIGENI NIRRVAALEG DVLGSYQHGA 150
RIGVLVAAKG ADEELVKHIA MHVAASKPEF IKPEDVSAEV VEKEYQVQLD 200
IAMQSGKPKE IAEKMVEGRM KKFTGEVSLT GQPFVMEPSK TVGQLLKEHN 250
AEVTGFIRFE VGEGIEKVET DFAAEVAAMS KQS 283
Length:283
Mass (Da):30,423
Last modified:January 23, 2007 - v2
Checksum:i0B9D21E928A5051C
GO

Mass spectrometryi

Molecular mass is 30294±6 Da from positions 2 - 283. Determined by ESI.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V00343 Genomic DNA. Translation: CAA23632.1.
D13334 Genomic DNA. Translation: BAA02597.1.
U00096 Genomic DNA. Translation: AAC73281.1.
AP009048 Genomic DNA. Translation: BAB96746.1.
U70214 Genomic DNA. Translation: AAB08599.1.
PIRiEFECS. A03525.
RefSeqiNP_414712.1. NC_000913.3.
YP_488472.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73281; AAC73281; b0170.
BAB96746; BAB96746; BAB96746.
GeneIDi12931801.
944866.
KEGGiecj:Y75_p0166.
eco:b0170.
PATRICi32115449. VBIEscCol129921_0176.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V00343 Genomic DNA. Translation: CAA23632.1 .
D13334 Genomic DNA. Translation: BAA02597.1 .
U00096 Genomic DNA. Translation: AAC73281.1 .
AP009048 Genomic DNA. Translation: BAB96746.1 .
U70214 Genomic DNA. Translation: AAB08599.1 .
PIRi EFECS. A03525.
RefSeqi NP_414712.1. NC_000913.3.
YP_488472.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EFU X-ray 2.50 B/D 2-283 [» ]
3MMP X-ray 2.50 A/C 1-283 [» ]
ProteinModelPortali P0A6P1.
SMRi P0A6P1. Positions 2-283.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-31835N.
IntActi P0A6P1. 10 interactions.
MINTi MINT-1273899.
STRINGi 511145.b0170.

PTM databases

PhosSitei P0810442.

2D gel databases

SWISS-2DPAGEi P0A6P1.

Proteomic databases

PaxDbi P0A6P1.
PRIDEi P0A6P1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73281 ; AAC73281 ; b0170 .
BAB96746 ; BAB96746 ; BAB96746 .
GeneIDi 12931801.
944866.
KEGGi ecj:Y75_p0166.
eco:b0170.
PATRICi 32115449. VBIEscCol129921_0176.

Organism-specific databases

EchoBASEi EB1026.
EcoGenei EG11033. tsf.

Phylogenomic databases

eggNOGi COG0264.
HOGENOMi HOG000220986.
KOi K02357.
OMAi ADCSKEW.
OrthoDBi EOG66B42N.
ProtClustDBi PRK09377.

Enzyme and pathway databases

BioCyci EcoCyc:EG11033-MONOMER.
ECOL316407:JW0165-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A6P1.
PROi P0A6P1.

Gene expression databases

Genevestigatori P0A6P1.

Family and domain databases

Gene3Di 3.30.479.20. 2 hits.
HAMAPi MF_00050. EF_Ts.
InterProi IPR001816. Transl_elong_EFTs/EF1B.
IPR014039. Transl_elong_EFTs/EF1B_dimer.
IPR018101. Transl_elong_Ts_CS.
IPR009060. UBA-like.
IPR000449. UBA/Ts_N.
[Graphical view ]
PANTHERi PTHR11741. PTHR11741. 1 hit.
Pfami PF00889. EF_TS. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
SSF54713. SSF54713. 2 hits.
TIGRFAMsi TIGR00116. tsf. 1 hit.
PROSITEi PS01126. EF_TS_1. 1 hit.
PS01127. EF_TS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publicationsDownload
  1. "Organization and nucleotide sequence of a new ribosomal operon in Escherichia coli containing the genes for ribosomal protein S2 and elongation factor Ts."
    An G., Bendiak D.S., Mamelak L.A., Friesen J.D.
    Nucleic Acids Res. 9:4163-4172(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
    Fujita N., Mori H., Yura T., Ishihama A.
    Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
    Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "The complete genome sequence of Escherichia coli K-12."
    Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
    Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.
    Submitted (SEP-1994) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-14.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-22.
    Strain: K12 / EMG2.
  9. "Protein identification with N and C-terminal sequence tags in proteome projects."
    Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.
    J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-5.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  10. "Analysis and crystallization of a 25 kDa C-terminal fragment of cloned elongation factor Ts from Escherichia coli."
    Boegestrand S., Wiborg O., Thirup S., Nyborg J.
    FEBS Lett. 368:49-54(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 52-56, MASS SPECTROMETRY.
  11. "Identification and characterization of the smbA gene, a suppressor of the mukB null mutant of Escherichia coli."
    Yamanaka K., Ogura T., Niki H., Hiraga S.
    J. Bacteriol. 174:7517-7526(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 179-283.
  12. "Localization of the ribosome-releasing factor gene in the Escherichia coli chromosome."
    Ichikawa S., Ryoji M., Siegfried Z., Kaji A.
    J. Bacteriol. 171:3689-3695(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-275.
  13. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  14. "The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5-A resolution."
    Kawashima T., Berthet-Colominas C., Wulff M., Cusack S., Leberman R.
    Nature 379:511-518(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH EF-TU.
  15. "Mutational analysis of the roles of residues in Escherichia coli elongation factor Ts in the interaction with elongation factor Tu."
    Zhang Y., Yu N.-J., Spremulli L.L.
    J. Biol. Chem. 273:4556-4562(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-24; ASP-81; PHE-82 AND HIS-148.

Entry nameiEFTS_ECOLI
AccessioniPrimary (citable) accession number: P0A6P1
Secondary accession number(s): P02997
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 96 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene

Similar proteinsi