tufB translation elongation factor Tu 2 [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: tufB
Official Full Name: translation elongation factor Tu 2
Primary source: ECOCYC:EG11037
Locus tag: b3980
See related: ASAP:ABE-0013020
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: ECK3971; kirT; pulT
Summary: Elongation factor Tu (EF-Tu) is the most abundant protein in Escherichia coli. [More information is available at EcoCyc: EG11037].
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Genomic context

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Sequence:: NC_000913.3 (4175944..4177128)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

we engineered an approximately 700-million-year-old inferred ancestral variant of tufB, an essential gene encoding elongation factor Tu, and inserted it in a modern Escherichia coli genome in place of the native tufB gene. We subsequently evolved replicate hybrid bacterial populations for 2000 generations and examined the adaptive response via fitness assays, whole genome sequencing, proteomics, and biochemical assays.
Title: Experimental Evolution of Escherichia coli Harboring an Ancient Translation Protein.
Comparison of DeltaDeltaG(o) values for binding EF-Tu to aa-tRNA show that the majority of the interface residues stabilize the ternary complex and their thermodynamic contribution can depend on the tRNA species that is used.
Title: The interface between Escherichia coli elongation factor Tu and aminoacyl-tRNA.
Fusidic acid increases traps the ribosome EF-G complex in a preexisting conformation formed during translation. Only the 0.3 state is observed when poly(Phe) synthesis is prevented by omission of EF-Tu.
Title: Single-molecule structural dynamics of EF-G--ribosome interaction during translocation.
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.
Ecdomains 2+3 suppressed the GTPase activity of the E coli domain 1, whereas those of Bacillut thuringensis EF-Tu stimulated the Bstdomain 1 GTPase.
Title: Opposite roles of domains 2+3 of Escherichia coli EF-Tu and Bacillus stearothermophilus EF-Tu in the regulation of EF-Tu GTPase activity.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

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 hydrolase activity	IEA Inferred from Electronic Annotation more info
enables magnesium ion binding	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables nucleotide 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	IEA Inferred from Electronic Annotation more info
part_of guanyl-nucleotide exchange factor complex	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