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tufA translation elongation factor Tu 1 [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947838, updated on 3-Dec-2024

Summary

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Official Symbol
tufA
Official Full Name
translation elongation factor Tu 1
Primary source
ECOCYC:EG11036
Locus tag
b3339
See related
ASAP:ABE-0010912
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK3326; kirT; pulT
Summary
Elongation factor Tu (EF-Tu) is the most abundant protein in Escherichia coli. [More information is available at EcoCyc: EG11036].
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Genomic context

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Sequence:
NC_000913.3 (3470145..3471329, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene bacterioferritin-associated ferredoxin Neighboring gene endochitinase Neighboring gene elongation factor G Neighboring gene 30S ribosomal subunit protein S7

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. An alpha to beta conformational switch in EF-Tu. Abel K, et al. Structure, 1996 Oct 15. PMID 8939740
  2. A secondary promoter for elongation factor Tu synthesis in the str ribosomal protein operon of Escherichia coli. Zengel JM, et al. Mol Gen Genet, 1982. PMID 6285146
  3. Evidence for an internal promoter preceding tufA in the str operon of Escherichia coli. An G, et al. J Bacteriol, 1982 Feb. PMID 6276361, Free PMC Article
  4. Mapping of two promoters for elongation factor Tu within the structural gene for elongation factor G. Zengel JM, et al. Biochim Biophys Acta, 1990 Aug 27. PMID 2207161
  5. Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 A resolution. Song H, et al. J Mol Biol, 1999 Jan 22. PMID 9918724

See all (200) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Conformational changes in EF-Tu coordinate the rate-limiting passage of aa-tRNA through the accommodation corridor en route to the peptidyl transferase center of the large ribosomal subunit.
    Title: Elongation factor-Tu can repetitively engage aminoacyl-tRNA within the ribosome during the proofreading stage of tRNA selection.
  2. By analyzing incorporation of near- and non-cognate amino acids in a model protein EF-Tu, we show that most of missense errors are too rare to detect by conventional methods, such as DDA, and are estimated to be between <10-7-10-5 by QRAS.
    Title: Broad range of missense error frequencies in cellular proteins.
  3. Data show that tRNA, selenocysteine- (tRNASec) variant (tRNAUTuX) facilitates peptide elongation factor EF-Tu dependent selenocysteine (Sec) insertion in response to UAG codons.
    Title: A synthetic tRNA for EF-Tu mediated selenocysteine incorporation in vivo and in vitro.
  4. Disruption of the TF/DnaK chaperone pathway is rescued by overexpression of the redox-regulated chaperone Hsp33.
    Title: Hsp33 controls elongation factor-Tu stability and allows Escherichia coli growth in the absence of the major DnaK and trigger factor chaperones.
  5. EF-Tu in Qbeta replicase modulates RNA elongation processes in a distinct manner from its established function in protein synthesis.
    Title: Molecular basis for RNA polymerization by Qβ replicase.
  6. Data suggest that the identity of the esterified amino acid and three base pairs in the T stem of tRNA combine to define the affinity of each aa-tRNA for EF-Tu, both off and on the ribosome.
    Title: Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decoding.
  7. N-terminus verified by Edman degradation on mature peptide
    Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
  8. P-loop and domain movements have roles in EF-Tu for guanine nucleotide exchange
    Title: The importance of P-loop and domain movements in EF-Tu for guanine nucleotide exchange.
Submit: New GeneRIF Correction

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables GTP binding IEA
Inferred from Electronic Annotation
more info
  
enables GTPase activity IEA
Inferred from Electronic Annotation
more info
  
enables RNA binding IEA
Inferred from Electronic Annotation
more info
  
enables guanosine tetraphosphate binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables guanosine tetraphosphate binding IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables translation elongation factor activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables translation elongation factor activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in response to antibiotic IEA
Inferred from Electronic Annotation
more info
  
involved_in translation IEA
Inferred from Electronic Annotation
more info
  
involved_in translational elongation IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in translational elongation IEA
Inferred from Electronic Annotation
more info
  
involved_in translational elongation NAS
Non-traceable Author Statement
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm HDA PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
part_of guanyl-nucleotide exchange factor complex IPI
Inferred from Physical Interaction
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
translation elongation factor Tu 1

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    3470145..3471329 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417798.1 translation elongation factor Tu 1 [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_417798.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A5B9ASQ8
    Conserved Domains (1) summary
    PRK00049
    Location:1 → 393
    PRK00049; elongation factor Tu; Reviewed
Nucleotide Protein
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