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P0A6P1 (EFTS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation factor Ts

Short name=EF-Ts
Gene names
Name:tsf
Ordered Locus Names:b0170, JW0165
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00050

Subunit structure

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

Subcellular location

Cytoplasm HAMAP-Rule MF_00050.

Sequence similarities

Belongs to the EF-Ts family.

Mass spectrometry

Molecular mass is 30294±6 Da from positions 2 - 283. Determined by ESI. Ref.10

Binary interactions

With

Entry

#Exp.

IntAct

Notes

tufAP0CE477EBI-301164,EBI-301077

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7 Ref.8 Ref.9
Chain2 – 283282Elongation factor Ts HAMAP-Rule MF_00050
PRO_0000161117

Regions

Region80 – 834Involved in Mg(2+) ion dislocation from EF-Tu HAMAP-Rule MF_00050

Experimental info

Mutagenesis241K → A: No change in binding to EF-Tu and in promoting GDP exchange. Ref.15
Mutagenesis811D → A: 2 to 3-fold less active in promoting GDP exchange and slightly lower binding constant for interaction with EF-Tu. Ref.15
Mutagenesis821F → A: 2 to 3-fold less active in promoting GDP exchange and 6-fold less active in binding to EF-Tu. Ref.15
Mutagenesis1481H → A: At least 100-fold decrease in affinity between EF-Ts and EF-Tu and only small amount of GDP exchange activity. Ref.15

Secondary structure

............................................. 283
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6P1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0B9D21E928A5051C

FASTA28330,423
        10         20         30         40         50         60 
MAEITASLVK ELRERTGAGM MDCKKALTEA NGDIELAIEN MRKSGAIKAA KKAGNVAADG 

        70         80         90        100        110        120 
VIKTKIDGNY GIILEVNCQT DFVAKDAGFQ AFADKVLDAA VAGKITDVEV LKAQFEEERV 

       130        140        150        160        170        180 
ALVAKIGENI NIRRVAALEG DVLGSYQHGA RIGVLVAAKG ADEELVKHIA MHVAASKPEF 

       190        200        210        220        230        240 
IKPEDVSAEV VEKEYQVQLD IAMQSGKPKE IAEKMVEGRM KKFTGEVSLT GQPFVMEPSK 

       250        260        270        280 
TVGQLLKEHN AEVTGFIRFE VGEGIEKVET DFAAEVAAMS KQS 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIREFECS. A03525.
RefSeqNP_414712.1. NC_000913.3.
YP_488472.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EFUX-ray2.50B/D2-283[»]
3MMPX-ray2.50A/C1-283[»]
ProteinModelPortalP0A6P1.
SMRP0A6P1. Positions 2-283.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-31835N.
IntActP0A6P1. 10 interactions.
MINTMINT-1273899.
STRING511145.b0170.

PTM databases

PhosSiteP0810442.

2D gel databases

SWISS-2DPAGEP0A6P1.

Proteomic databases

PaxDbP0A6P1.
PRIDEP0A6P1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73281; AAC73281; b0170.
BAB96746; BAB96746; BAB96746.
GeneID12931801.
944866.
KEGGecj:Y75_p0166.
eco:b0170.
PATRIC32115449. VBIEscCol129921_0176.

Organism-specific databases

EchoBASEEB1026.
EcoGeneEG11033. tsf.

Phylogenomic databases

eggNOGCOG0264.
HOGENOMHOG000220986.
KOK02357.
OMAADCSKEW.
OrthoDBEOG66B42N.
PhylomeDBP0A6P1.
ProtClustDBPRK09377.

Enzyme and pathway databases

BioCycEcoCyc:EG11033-MONOMER.
ECOL316407:JW0165-MONOMER.

Gene expression databases

GenevestigatorP0A6P1.

Family and domain databases

Gene3D3.30.479.20. 2 hits.
HAMAPMF_00050. EF_Ts.
InterProIPR001816. Transl_elong_EFTs/EF1B.
IPR014039. Transl_elong_EFTs/EF1B_dimer.
IPR018101. Transl_elong_Ts_CS.
IPR009060. UBA-like.
IPR000449. UBA/Ts_N.
[Graphical view]
PANTHERPTHR11741. PTHR11741. 1 hit.
PfamPF00889. EF_TS. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
SSF54713. SSF54713. 2 hits.
TIGRFAMsTIGR00116. tsf. 1 hit.
PROSITEPS01126. EF_TS_1. 1 hit.
PS01127. EF_TS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A6P1.
PROP0A6P1.

Entry information

Entry nameEFTS_ECOLI
AccessionPrimary (citable) accession number: P0A6P1
Secondary accession number(s): P02997
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene