Reviewed,
UniProtKB/Swiss-Prot P0A6P1 (EFTS_ECOLI)
Last modified
November 3, 2009.
Version 57.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Elongation factor Ts Short name=EF-Ts | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 283 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 MF_00050 |
| Subunit structure | Heterotetramer composed of two EF-Ts.EF-Tu dimer complex. HAMAP MF_00050 |
| Subcellular location | |
| 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 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Molecular function | Elongation factor |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | translational elongation Inferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from direct assay. Source: UniProtKB membraneInferred from direct assay. Source: UniProtKB |
| Molecular function | protein binding Inferred from physical interaction. Source: IntAct translation elongation factor activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| dnaC | P0AEF0 | 1 | EBI-301164,EBI-549012 | |
| tufA | P0A6N1 | 2 | EBI-301164,EBI-301077 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.7 Ref.8 Ref.9 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Chain | 2 – 283 | 282 | Elongation factor Ts HAMAP MF_00050 | PRO_0000161117 | |||||||||||||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 80 – 83 | 4 | Involved in Mg(2+) ion dislocation from EF-Tu HAMAP MF_00050 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 24 | 1 | K → A: No change in binding to EF-Tu and in promoting GDP exchange. Ref.14 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 81 | 1 | D → A: 2 to 3-fold less active in promoting GDP exchange and slightly lower binding constant for interaction with EF-Tu. Ref.14 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 82 | 1 | F → A: 2 to 3-fold less active in promoting GDP exchange and 6-fold less active in binding to EF-Tu. Ref.14 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 148 | 1 | H → A: At least 100-fold decrease in affinity between EF-Ts and EF-Tu and only small amount of GDP exchange activity. Ref.14 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 6 – 16 | 11 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 20 – 29 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 30 – 32 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 34 – 52 | 19 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 59 – 67 | 9 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 70 – 79 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 81 – 84 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 87 – 102 | 16 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 108 – 126 | 19 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 131 – 139 | 9 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 141 – 148 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 149 – 151 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 152 – 160 | 9 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 163 – 176 | 14 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 179 – 182 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 183 – 185 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 188 – 204 | 17 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 209 – 227 | 19 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 229 – 231 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 232 – 234 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 237 – 241 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 242 – 247 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 248 – 250 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 252 – 260 | 9 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 261 – 264 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 272 – 279 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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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: 6272196] [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: 8202364] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 9298646] [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: 9600841] [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: 7615087] [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: 1447125] [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: 2661533] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-275. |
| [13] | "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: 8596629] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH EF-TU. |
| [14] | "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: 9468511] [Abstract] Cited for: MUTAGENESIS OF LYS-24; ASP-81; PHE-82 AND HIS-148. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 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. | |||||||||||||
| PIR | EFECS. A03525. | ||||||||||||
| RefSeq | AP_000830.1. NP_414712.1. | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | P0A6P1. 10 interactions. | ||||||||||||
| STRING | P0A6P1. | ||||||||||||
PTM databases | |||||||||||||
| PhosSite | P0A6P1. | ||||||||||||
2-D gel databases | |||||||||||||
| SWISS-2DPAGE | P0A6P1. | ||||||||||||
| 2DBase-Ecoli | P0A6P1. | ||||||||||||
| ECO2DBASE | C030.7. 6TH EDITION. C031.6. 6TH EDITION. | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 944866. | ||||||||||||
| GenomeReviews | Gene locus JW0165 in contig AP009048_GR. Gene locus b0170 in contig U00096_GR. | ||||||||||||
| KEGG | ecj:JW0165. eco:b0170. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB1026. | ||||||||||||
| EcoGene | EG11033. tsf. | ||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | P0A6P1. | ||||||||||||
| OMA | YLHGTRI. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:EG11033-MON. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P0A6P1. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00050. [Tree] | ||||||||||||
| InterPro | IPR001816. Transl_elong_EFTs/EF1B. IPR014039. Transl_elong_EFTs/EF1B_dimer. IPR018101. Transl_elong_Ts_CS. IPR000449. UBA/transl_elong_EF1B_N. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.30.479.20. Transl_elong_EFTs/EF1B_dimer. 2 hits. | ||||||||||||
| PANTHER | PTHR11741. Transl_elong_EFTs/EF1B. 1 hit. | ||||||||||||
| Pfam | PF00889. EF_TS. 1 hit. PF00627. UBA. 1 hit. [Graphical view] | ||||||||||||
| TIGRFAMs | TIGR00116. tsf. 1 hit. | ||||||||||||
| PROSITE | PS01126. EF_TS_1. 1 hit. PS01127. EF_TS_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | EFTS_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0A6P1 Secondary accession number(s): P02997 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


