Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0A6P1

- EFTS_ECOLI

UniProt

P0A6P1 - EFTS_ECOLI

(max 400 entries)x

Your basket is currently empty.

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

Protein

Elongation factor Ts

Gene

tsf

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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.

GO - Molecular functioni

  1. guanyl-nucleotide exchange factor activity Source: EcoCyc
  2. translation elongation factor activity Source: UniProtKB-HAMAP
  3. zinc ion binding Source: EcoliWiki

GO - Biological processi

  1. positive regulation of GTPase activity Source: GOC
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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 241K → A: No change in binding to EF-Tu and in promoting GDP exchange. 1 Publication
Mutagenesisi81 – 811D → A: 2 to 3-fold less active in promoting GDP exchange and slightly lower binding constant for interaction with EF-Tu. 1 Publication
Mutagenesisi82 – 821F → A: 2 to 3-fold less active in promoting GDP exchange and 6-fold less active in binding to EF-Tu. 1 Publication
Mutagenesisi148 – 1481H → 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 identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 283282Elongation factor TsPRO_0000161117Add
BLAST

Proteomic databases

PaxDbiP0A6P1.
PRIDEiP0A6P1.

2D gel databases

SWISS-2DPAGEP0A6P1.

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

1
283
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1611Combined sources
Helixi20 – 2910Combined sources
Turni30 – 323Combined sources
Helixi34 – 5219Combined sources
Beta strandi59 – 679Combined sources
Beta strandi70 – 7910Combined sources
Helixi81 – 844Combined sources
Helixi87 – 10216Combined sources
Helixi108 – 12619Combined sources
Beta strandi131 – 1399Combined sources
Beta strandi141 – 1488Combined sources
Turni149 – 1513Combined sources
Beta strandi152 – 1609Combined sources
Helixi163 – 17614Combined sources
Beta strandi179 – 1824Combined sources
Helixi183 – 1853Combined sources
Helixi188 – 20417Combined sources
Helixi209 – 22719Combined sources
Turni229 – 2313Combined sources
Beta strandi232 – 2343Combined sources
Beta strandi237 – 2415Combined sources
Helixi242 – 2476Combined sources
Turni248 – 2503Combined sources
Beta strandi252 – 2609Combined sources
Turni261 – 2644Combined sources
Helixi272 – 2798Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EFUX-ray2.50B/D2-283[»]
3MMPX-ray2.50A/C1-283[»]
4Q7JX-ray2.90A/E2-283[»]
ProteinModelPortaliP0A6P1.
SMRiP0A6P1. Positions 2-283.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6P1.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the EF-Ts family.Curated

Phylogenomic databases

eggNOGiCOG0264.
HOGENOMiHOG000220986.
InParanoidiP0A6P1.
KOiK02357.
OMAiNFVRLEV.
OrthoDBiEOG66B42N.
PhylomeDBiP0A6P1.

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]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEITASLVK ELRERTGAGM MDCKKALTEA NGDIELAIEN MRKSGAIKAA
60 70 80 90 100
KKAGNVAADG VIKTKIDGNY GIILEVNCQT DFVAKDAGFQ AFADKVLDAA
110 120 130 140 150
VAGKITDVEV LKAQFEEERV ALVAKIGENI NIRRVAALEG DVLGSYQHGA
160 170 180 190 200
RIGVLVAAKG ADEELVKHIA MHVAASKPEF IKPEDVSAEV VEKEYQVQLD
210 220 230 240 250
IAMQSGKPKE IAEKMVEGRM KKFTGEVSLT GQPFVMEPSK TVGQLLKEHN
260 270 280
AEVTGFIRFE VGEGIEKVET DFAAEVAAMS KQS
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. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
PIRiA03525. EFECS.
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:
EMBLi
GenBanki
DDBJi
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 A03525. EFECS.
RefSeqi NP_414712.1. NC_000913.3.
YP_488472.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 [» ]
4Q7J X-ray 2.90 A/E 2-283 [» ]
ProteinModelPortali P0A6P1.
SMRi P0A6P1. Positions 2-283.
ModBasei Search...
MobiDBi 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-2DPAGE 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.
InParanoidi P0A6P1.
KOi K02357.
OMAi NFVRLEV.
OrthoDBi EOG66B42N.
PhylomeDBi P0A6P1.

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' publications
  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. 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. 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. 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 informationi

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: November 26, 2014
This is version 102 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3