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BioCyc websites down
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discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Escherichia coli K-12 substr. MG1655 Polypeptide: elongation factor Tu



Gene: tufA Accession Numbers: EG11036 (EcoCyc), b3339, ECK3326

Synonyms: pulT, kirT, EF-Tu

Regulation Summary Diagram: ?

Summary:
Elongation factor Tu (EF-Tu) is the most abundant protein in E. coli. In its GTP-bound (active) form, EF-Tu binds aminoacylated tRNAs. At the decoding site of the ribosome, this ternary complex is "tested" for a codon-anticodon match; if the proper aminoacyl-tRNA has been found, GTP is hydrolyzed and EF-Tu and GDP dissociate from the ribosome, while the aminoacyl-tRNA remains bound to the ribosome.

Proteomic analyses indicate that EF-Tu is maximally expressed during stress response [Muela08].

In E. coli, EF-Tu is encoded by two genes, tufA and tufB.

Citations: [Weijland92]

Gene Citations: [Zengel90, Johanson92, Saito94, Post78]

Locations: cytosol, inner membrane

Map Position: [3,468,167 <- 3,469,351] (74.75 centisomes)
Length: 1185 bp / 394 aa

Molecular Weight of Polypeptide: 43.284 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0010912 , CGSC:61 , EchoBASE:EB1029 , EcoGene:EG11036 , EcoliWiki:b3339 , ModBase:P0A6N1 , OU-Microarray:b3339 , PortEco:tufA , PR:PRO_000024141 , Pride:P0CE47 , Protein Model Portal:P0CE47 , RefSeq:NP_417798 , RegulonDB:EG11036 , SMR:P0CE47 , UniProt:P0CE47

Relationship Links: InterPro:IN-FAMILY:IPR000795 , InterPro:IN-FAMILY:IPR004160 , InterPro:IN-FAMILY:IPR004161 , InterPro:IN-FAMILY:IPR004541 , InterPro:IN-FAMILY:IPR005225 , InterPro:IN-FAMILY:IPR009000 , InterPro:IN-FAMILY:IPR009001 , InterPro:IN-FAMILY:IPR027417 , PDB:Structure:1D8T , PDB:Structure:1EFC , PDB:Structure:1ETU , PDB:Structure:1MJ1 , PDB:Structure:2FX3 , PDB:Structure:2HCJ , PDB:Structure:2HDN , PDB:Structure:3EP2 , PDB:Structure:3EQ3 , PDB:Structure:3EQ4 , PDB:Structure:3U2Q , PDB:Structure:3U6B , PDB:Structure:3U6K , PDB:Structure:4G5G , Pfam:IN-FAMILY:PF00009 , Pfam:IN-FAMILY:PF03143 , Pfam:IN-FAMILY:PF03144 , Prints:IN-FAMILY:PR00315 , Prosite:IN-FAMILY:PS00301

In Paralogous Gene Group: 77 (16 members)

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006184 - GTP catabolic process Inferred by computational analysis [GOA01]
GO:0006412 - translation Inferred by computational analysis [UniProtGOA11a]
GO:0006414 - translational elongation Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0046677 - response to antibiotic Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Lasserre06, Arifuzzaman06, Kawashima96, Butland05]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0003746 - translation elongation factor activity Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01]
GO:0003924 - GTPase activity Inferred by computational analysis [GOA01]
GO:0005525 - GTP binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, Lasserre06]
GO:0005622 - intracellular Inferred by computational analysis [GOA01]
GO:0005829 - cytosol
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell processes adaptations osmotic pressure
information transfer protein related translation


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Laursen81, Jones80, UniProt11a]
UniProt: Removed.
Acetylation-Modification 2
[UniProt10]
UniProt: N-acetylserine;
Chain 2 -> 394
[UniProt10a]
UniProt: Elongation factor Tu 1;
Nucleotide-Phosphate-Binding-Region 19 -> 26
[UniProt10]
UniProt: GTP;
Mutagenesis-Variant 20
[Zhang98a, UniProt11]
Alternate sequence: H → A; UniProt: No change in binding GDP and 3-fold reduction in binding EF-Ts.
Mutagenesis-Variant 21
[Jacquet89, UniProt11]
Alternate sequence: V → G; UniProt: Lowers GTPase activity 5 to 10- fold.
Modified-Residue 57
[Young91, LItalien79, UniProt11a]
UniProt: N6,N6-dimethyllysine; alternate.
Nucleotide-Phosphate-Binding-Region 81 -> 85
[UniProt10]
UniProt: GTP;
Mutagenesis-Variant 83
[Cool90, UniProt11]
Alternate sequence: P → T; UniProt: Loss of GTPase activity and creation of an autophosphorylation site.
Mutagenesis-Variant 115
[Zhang98a, UniProt11]
Alternate sequence: Q → A; UniProt: Weaker binding for GDP and for EF- Ts.
Mutagenesis-Variant 125
[UniProt10]
Alternate sequence: Q → K; UniProt: Kirromycin resistant;
Nucleotide-Phosphate-Binding-Region 136 -> 139
[UniProt10]
UniProt: GTP;
Mutagenesis-Variant 137
[Hwang89, UniProt11]
Alternate sequence: K → I; UniProt: Reduces affinity for GDP.
Alternate sequence: K → E; UniProt: Reduces affinity for GDP.
Alternate sequence: K → Q; UniProt: Reduces affinity for GDP.
Alternate sequence: K → R; UniProt: Reduces affinity for GDP.
Mutagenesis-Variant 139
[Hwang87, UniProt11]
Alternate sequence: D → N; UniProt: Reduces affinity for GDP; increases affinity for XDP.
Acetylation-Modification 177
[Yu08]
 
Acetylation-Modification 188
[Yu08]
 
Acetylation-Modification 209
[Yu08]
 
Mutagenesis-Variant 223
[UniProt10]
Alternate sequence: G → D; UniProt: Inhibits codon-induced conformational changes leading to GTPase activation on the ribosome;
Mutagenesis-Variant 231
[UniProt10]
Alternate sequence: R → C; UniProt: Pulvomycin resistant;
Acetylation-Modification 314
[Zhang09, UniProt11]
UniProt: N6-acetyllysine.
Mutagenesis-Variant 317
[UniProt10]
Alternate sequence: G → D; UniProt: Kirromycin resistant;
Mutagenesis-Variant 334
[UniProt10]
Alternate sequence: R → C; UniProt: Pulvomycin resistant;
Mutagenesis-Variant 335
[UniProt10]
Alternate sequence: T → A; UniProt: Pulvomycin resistant;
Mutagenesis-Variant 349
[Zhang98a, UniProt11]
Alternate sequence: E → A; UniProt: No change in binding GDP but higher binding constant for EF-Ts.
Mutagenesis-Variant 376
[UniProt10]
Alternate sequence: A → V; UniProt: Kirromycin resistant;
Alternate sequence: A → T; UniProt: Kirromycin resistant;
Phosphorylation-Modification 383
[Lippmann93, UniProt11]
UniProt: Phosphothreonine.


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
1/26/1998 (pkarp) Merged genes G7976/tufA and EG11036/tufA


References

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Cool90: Cool RH, Jensen M, Jonak J, Clark BF, Parmeggiani A (1990). "Substitution of proline 82 by threonine induces autophosphorylating activity in GTP-binding domain of elongation factor Tu." J Biol Chem 265(12);6744-9. PMID: 2157708

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Hwang87: Hwang YW, Miller DL (1987). "A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP regulatory protein." J Biol Chem 262(27);13081-5. PMID: 3308869

Hwang89: Hwang YW, Sanchez A, Miller DL (1989). "Mutagenesis of bacterial elongation factor Tu at lysine 136. A conserved amino acid in GTP regulatory proteins." J Biol Chem 264(14);8304-9. PMID: 2498311

Jacquet89: Jacquet E, Parmeggiani A (1989). "Substitution of Val20 by Gly in elongation factor Tu. Effects on the interaction with elongation factors Ts, aminoacyl-tRNA and ribosomes." Eur J Biochem 185(2);341-6. PMID: 2684669

Johanson92: Johanson U, Hughes D (1992). "Comparison of the complete sequence of the str operon in Salmonella typhimurium and Escherichia coli." Gene 1992;120(1);93-8. PMID: 1398129

Jones80: Jones MD, Petersen TE, Nielsen KM, Magnusson S, Sottrup-Jensen L, Gausing K, Clark BF (1980). "The complete amino-acid sequence of elongation factor Tu from Escherichia coli." Eur J Biochem 108(2);507-26. PMID: 6997043

Kawashima96: Kawashima T, Berthet-Colominas C, Wulff M, Cusack S, Leberman R (1996). "The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution." Nature 379(6565);511-8. PMID: 8596629

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Laursen81: Laursen RA, L'Italien JJ, Nagarkatti S, Miller DL (1981). "The amino acid sequence of elongation factor Tu of Escherichia coli. The complete sequence." J Biol Chem 256(15);8102-9. PMID: 7021545

Lippmann93: Lippmann C, Lindschau C, Vijgenboom E, Schroder W, Bosch L, Erdmann VA (1993). "Prokaryotic elongation factor Tu is phosphorylated in vivo." J Biol Chem 268(1);601-7. PMID: 8416965

LItalien79: L'Italien JJ, Laursen RA (1979). "Location of the site of methylation in elongation factor Tu." FEBS Lett 107(2);359-62. PMID: 389663

Muela08: Muela A, Seco C, Camafeita E, Arana I, Orruno M, Lopez JA, Barcina I (2008). "Changes in Escherichia coli outer membrane subproteome under environmental conditions inducing the viable but nonculturable state." FEMS Microbiol Ecol 64(1);28-36. PMID: 18318713

Post78: Post LE, Arfsten AE, Reusser F, Nomura M (1978). "DNA sequences of promoter regions for the str and spc ribosomal protein operons in E. coli." Cell 15(1);215-29. PMID: 151587

Saito94: Saito K, Mattheakis LC, Nomura M (1994). "Post-transcriptional regulation of the str operon in Escherichia coli. Ribosomal protein S7 inhibits coupled translation of S7 but not its independent translation." J Mol Biol 1994;235(1);111-24. PMID: 7507167

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Weijland92: Weijland A, Harmark K, Cool RH, Anborgh PH, Parmeggiani A (1992). "Elongation factor Tu: a molecular switch in protein biosynthesis." Mol Microbiol 6(6);683-8. PMID: 1573997

Young91: Young CC, Bernlohr RW (1991). "Elongation factor Tu is methylated in response to nutrient deprivation in Escherichia coli." J Bacteriol 173(10);3096-100. PMID: 2022614

Yu08: Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG (2008). "The diversity of lysine-acetylated proteins in Escherichia coli." J Microbiol Biotechnol 18(9);1529-36. PMID: 18852508

Zengel90: Zengel JM, Lindahl L (1990). "Mapping of two promoters for elongation factor Tu within the structural gene for elongation factor G." Biochim Biophys Acta 1050(1-3);317-22. PMID: 2207161

Zhang09: Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8(2);215-25. PMID: 18723842

Zhang98a: Zhang Y, Yu NJ, Spremulli LL (1998). "Mutational analysis of the roles of residues in Escherichia coli elongation factor Ts in the interaction with elongation factor Tu." J Biol Chem 273(8);4556-62. PMID: 9468511

Other References Related to Gene Regulation

Dean81: Dean D, Yates JL, Nomura M (1981). "Identification of ribosomal protein S7 as a repressor of translation within the str operon of E. coli." Cell 24(2);413-9. PMID: 7016341

Golovin06: Golovin A, Spiridonova V, Kopylov A (2006). "Mapping contacts of the S12-S7 intercistronic region of str operon mRNA with ribosomal protein S7 of E. coli." FEBS Lett 580(25);5858-62. PMID: 17027976

Lemke11: Lemke JJ, Sanchez-Vazquez P, Burgos HL, Hedberg G, Ross W, Gourse RL (2011). "Direct regulation of Escherichia coli ribosomal protein promoters by the transcription factors ppGpp and DksA." Proc Natl Acad Sci U S A 108(14);5712-7. PMID: 21402902

Post78a: Post LE, Arfsten AE, Nomura M, Jaskunas SR (1978). "Isolation and characterization of a promoter mutant in the str ribosomal protein operon in E. coli." Cell 1978;15(1);231-6. PMID: 359165

Rezuchova03: Rezuchova B, Miticka H, Homerova D, Roberts M, Kormanec J (2003). "New members of the Escherichia coli sigmaE regulon identified by a two-plasmid system." FEMS Microbiol Lett 225(1);1-7. PMID: 12900013

Rhodius05: Rhodius VA, Suh WC, Nonaka G, West J, Gross CA (2005). "Conserved and variable functions of the sigmaE stress response in related genomes." PLoS Biol 4(1);e2. PMID: 16336047

Salmon03: Salmon K, Hung SP, Mekjian K, Baldi P, Hatfield GW, Gunsalus RP (2003). "Global gene expression profiling in Escherichia coli K12. The effects of oxygen availability and FNR." J Biol Chem 278(32);29837-55. PMID: 12754220

Zaslaver06: Zaslaver A, Bren A, Ronen M, Itzkovitz S, Kikoin I, Shavit S, Liebermeister W, Surette MG, Alon U (2006). "A comprehensive library of fluorescent transcriptional reporters for Escherichia coli." Nat Methods 3(8);623-8. PMID: 16862137

Zengel84: Zengel JM, Archer RH, Lindahl L (1984). "The nucleotide sequence of the Escherichia coli fus gene, coding for elongation factor G." Nucleic Acids Res 12(4);2181-92. PMID: 6322136


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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