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Escherichia coli K-12 substr. MG1655 Polypeptide: elongation factor Tu



Gene: tufB Accession Numbers: EG11037 (EcoCyc), b3980, ECK3971

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.

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

Citations: [Weijland92]

Gene Citations: [Neidhardt96, vanDelft87, Lee81a]

Locations: cytosol, inner membrane

Map Position: [4,173,967 -> 4,175,151] (89.96 centisomes)
Length: 1185 bp / 394 aa

Molecular Weight of Polypeptide: 43.314 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0013020 , CGSC:60 , EchoBASE:EB1030 , EcoGene:EG11037 , EcoliWiki:b3980 , Mint:MINT-1234073 , ModBase:P02990 , OU-Microarray:b3980 , PortEco:tufB , Pride:P0CE48 , Protein Model Portal:P0CE48 , RefSeq:NP_418407 , RegulonDB:EG11037 , SMR:P0CE48 , UniProt:P0CE48

Relationship Links: EcoO157Cyc:Homolog:TUFB , EcoO157Cyc:Homolog:TUFB-MONOMER , 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:1DG1 , PDB:Structure:1EFM , PDB:Structure:1EFU , PDB:Structure:1LS2 , PDB:Structure:1OB2 , PDB:Structure:1QZD , PDB:Structure:2BVN , PDB:Structure:3FIH , PDB:Structure:3IZV , PDB:Structure:3IZW , PDB:Structure:3MMP , 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 [UniProtGOA11]
GO:0006414 - translational elongation Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0046677 - response to antibiotic Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Zheng11]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0003746 - translation elongation factor activity Inferred by computational analysis [UniProtGOA11, GOA06, GOA01]
GO:0003924 - GTPase activity Inferred by computational analysis [GOA01]
GO:0005525 - GTP binding Inferred by computational analysis [UniProtGOA11, GOA06, GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Zhang07]
GO:0005622 - intracellular Inferred by computational analysis [GOA01]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11a, UniProtGOA11]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]

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
[UniProt10a]
UniProt: N-acetylserine;
Chain 2 -> 394
[UniProt10]
UniProt: Elongation factor Tu 2;
Nucleotide-Phosphate-Binding-Region 19 -> 26
[UniProt10a]
UniProt: GTP;
Mutagenesis-Variant 20
[Zhang98e, UniProt11]
Alternate sequence: H → A; UniProt: No change in binding GDP and 3-fold reduction in binding EF-Ts.
N6-succinyllysine-Modification 38
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
Modified-Residue 57
[Young91, LItalien79, UniProt11a]
UniProt: N6,N6-dimethyllysine; alternate.
Nucleotide-Phosphate-Binding-Region 81 -> 85
[UniProt10a]
UniProt: GTP;
Mutagenesis-Variant 115
[Zhang98e, UniProt11]
Alternate sequence: Q → A; UniProt: Weaker binding for GDP and for EF- Ts.
Nucleotide-Phosphate-Binding-Region 136 -> 139
[UniProt10a]
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.
N6-succinyllysine-Modification 177
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
Acetylation-Modification 177
[Yu08]
 
Acetylation-Modification 188
[Yu08]
 
Acetylation-Modification 209
[Yu08]
 
Mutagenesis-Variant 223
[UniProt10a]
Alternate sequence: G → D; UniProt: Inhibits codon-induced conformational changes leading to GTPase activation on the ribosome;
N6-succinyllysine-Modification 249
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
N6-succinyllysine-Modification 253
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
N6-succinyllysine-Modification 295
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
N6-succinyllysine-Modification 314
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine; alternate.
Acetylation-Modification 314
[Zhang09, UniProt12a]
UniProt: N6-acetyllysine; alternate.
Mutagenesis-Variant 349
[Zhang98e, UniProt11]
Alternate sequence: E → A; UniProt: No change in binding GDP but higher binding constant for EF-Ts.
Phosphorylation-Modification 383
[Lippmann93, UniProt11]
UniProt: Phosphothreonine.
Acetylation-Modification 391
[Yu08]
 


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b3980 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11037.


References

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

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

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

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

Lee81a: Lee JS, An G, Friesen JD, Fill NP (1981). "Location of the tufB promoter of E. coli: cotranscription of tufB with four transfer RNA genes." Cell 25(1);251-8. PMID: 6168388

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

Neidhardt96: Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low Jr KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE "Escherichia coli and Salmonella, Cellular and Molecular Biology, Second Edition." American Society for Microbiology, Washington, D.C., 1996.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 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.

UniProt12a: UniProt Consortium (2012). "UniProt version 2012-09 released on 2012-09-12 00:00:00." Database.

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

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

vanDelft87: van Delft JH, Marinon B, Schmidt DS, Bosch L (1987). "Transcription of the tRNA-tufB operon of Escherichia coli: activation, termination and antitermination." Nucleic Acids Res 15(22);9515-30. PMID: 3317280

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

Zhang07: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111

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

Zhang11: Zhang Z, Tan M, Xie Z, Dai L, Chen Y, Zhao Y (2011). "Identification of lysine succinylation as a new post-translational modification." Nat Chem Biol 7(1);58-63. PMID: 21151122

Zhang98e: 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

Zheng11: Zheng C, Yang L, Hoopmann MR, Eng JK, Tang X, Weisbrod CR, Bruce JE (2011). "Cross-linking measurements of in vivo protein complex topologies." Mol Cell Proteomics 10(10);M110.006841. PMID: 21697552

Other References Related to Gene Regulation

Bosch90: Bosch L, Nilsson L, Vijgenboom E, Verbeek H (1990). "FIS-dependent trans-activation of tRNA and rRNA operons of Escherichia coli." Biochim Biophys Acta 1050(1-3);293-301. PMID: 2145039

Hengen97: Hengen PN, Bartram SL, Stewart LE, Schneider TD (1997). "Information analysis of Fis binding sites." Nucleic Acids Res 25(24);4994-5002. PMID: 9396807

Nilsson90: Nilsson L, Vanet A, Vijgenboom E, Bosch L (1990). "The role of FIS in trans activation of stable RNA operons of E. coli." EMBO J 9(3);727-34. PMID: 1690124


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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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