fusA elongation factor G [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Gene symbol: fusA
Gene description: elongation factor G
Primary source: ASAP:ABE-0010914
Locus tag: b3340
See related: ECOCYC:EG10360
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: ECK3327; far; fus
Summary: Binds TrxA (Kumar, 2004). [More information is available at EcoGene: EG10360]. Elongation factor G is an essential protein that facilitates the translocation of the ribosome by one codon along the mRNA molecule. [More information is available at EcoCyc: EG10360].
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Genomic context

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Sequence:: NC_000913.3 (3471400..3473514, complement)

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?

Mutations in domain IV of elongation factor EF-G confer -1 frameshifting.
Title: Mutations in domain IV of elongation factor EF-G confer -1 frameshifting.
The cells with high EFG/RRF (or low RRF/EFG) ratios are more susceptible to fusidic acid than those with low EFG/RRF (or high RRF/EFG) ratios.
Title: Antimicrobial activity of fusidic acid in Escherichia coli is dependent on the relative levels of ribosome recycling factor and elongation factor G.
the CyaA(N600Y) mutant has a transcriptome indicative of increased CRP activity, pointing to an unknown role for CyaA and / or cAMP in gene expression..We show that the large scale transcriptomic changes in the topoisomerase I (FusA(A608E)-TopA(S180L)) mutant likely result from increased negative supercoiling in the cell.
Title: Modulation of Global Transcriptional Regulatory Networks as a Strategy for Increasing Kanamycin Resistance of the Translational Elongation Factor-G Mutants in Escherichia coli.
Kinetics of spontaneous and EF-G-accelerated rotation of ribosomal subunits has been presented.
Title: Kinetics of Spontaneous and EF-G-Accelerated Rotation of Ribosomal Subunits.
Ribosome recycling after peptide chain termination is a special case of the general RRF and EF-G function, which happens whenever fMet-tRNA is not available for triggering 70S scanning.
Title: The Termination Phase in Protein Synthesis is not Obligatorily Followed by the RRF/EF-G-Dependent Recycling Phase.
These results show that EF-G bound to GTP (EF-G-GTP) continuously samples both rotational states of the ribosome, binding with higher affinity to the rotated state.
Title: Coordinated conformational and compositional dynamics drive ribosome translocation.
These structures suggest that EF-G controls the translocation reaction by cycles of conformational rigidity and relaxation before and after GTP hydrolysis.
Title: Control of ribosomal subunit rotation by elongation factor G.
cryo-electron microscopy reconstruction of a fusidic-acid-stalled ribosomal 70S-tmRNA-SmpB-EF-G complex (carrying both of the large ligands, that is, EF-G and tmRNA) at 8.3 A resolution
Title: The complex of tmRNA-SmpB and EF-G on translocating ribosomes.
A central interdomain protein joint in elongation factor G regulates antibiotic sensitivity, GTP hydrolysis, and ribosome translocation
Title: A central interdomain protein joint in elongation factor G regulates antibiotic sensitivity, GTP hydrolysis, and ribosome translocation.
Collectively, the results support a central role of sw1 in driving the EF-G cycle during protein synthesis.
Title: Conformational changes in switch I of EF-G drive its directional cycling on and off the ribosome.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables GTP binding	IEA Inferred from Electronic Annotation more info
enables GTPase activity	IDA Inferred from Direct Assay more info	PubMed
enables GTPase activity	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 nucleotide binding	IEA Inferred from Electronic Annotation more info
enables translation elongation factor activity	IDA Inferred from Direct Assay more info	PubMed
enables translation elongation factor activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in ribosome disassembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in translation	IEA Inferred from Electronic Annotation more info
involved_in translational elongation	IDA Inferred from Direct Assay more info	PubMed
involved_in translational elongation	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: elongation factor G

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

NC_000913.3 Reference assembly

Range

3471400..3473514 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_417799.1 elongation factor G [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_417799.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A826YAG5

Conserved Domains (1) summary

PRK00007
Location:1 → 704

PRK00007; elongation factor G; Reviewed