gyrB DNA gyrase subunit B [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: gyrB
Official Full Name: DNA gyrase subunit B
Primary source: ECOCYC:EG10424
Locus tag: b3699
See related: ASAP:ABE-0012093
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: acrB; Cou; ECK3691; himB; hisU; hopA; nalC; parA; pcbA; pcpA
Summary: gyrB is an essential gene. [More information is available at EcoGene: EG10424]. The GyrB subunit of DNA gyrase is required for the ATPase activity of the enzyme. [More information is available at EcoCyc: EG10424].
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Genomic context

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Sequence:: NC_000913.3 (3877705..3880119, 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?

Single-molecule dynamics of DNA gyrase in evolutionarily distant bacteria Mycobacterium tuberculosis and Escherichia coli.
Title: Single-molecule dynamics of DNA gyrase in evolutionarily distant bacteria Mycobacterium tuberculosis and Escherichia coli.
Among nalidixic acid resistant isolates...1 (2%) isolate showed gyrB (A660-T660) SNP.
Title: Characterization of enteropathogenic Escherichia coli of clinical origin from the pediatric population in Pakistan.
SecA defects are accompanied by dysregulation of MukB, gyrB, chromosome partitioning and DNA superhelicity.
Title: SecA defects are accompanied by dysregulation of MukB, DNA gyrase, chromosome partitioning and DNA superhelicity in Escherichia coli.
Data indicate the existence of interactions between the fluoroquinolone C-7 ring and both GyrA and GyrB.
Title: Fluoroquinolone-gyrase-DNA complexes: two modes of drug binding.
ParB complexes P1 plasmids, ParA-ATP stimulates this interaction and ParA-ADP inhibits ParB pairing activity in a parS-independent manner.
Title: ParAB-mediated intermolecular association of plasmid P1 parS sites.
The GyrB subunit from Escherichia coli has been investigated, namely the ATP binding pocket both considering the protein without ligands and bound with the inhibitors clorobiocin, novobiocin and 5'-adenylyl-beta-gamma-imidodiphosphate.
Title: Exploring the conformational changes of the ATP binding site of gyrase B from Escherichia coli complexed with different established inhibitors by using molecular dynamics simulation: protein-ligand interactions in the light of the alanine scanning and free energy decomposition methods.
ParA binds DNA non-specifically in the presence of ATP.
Title: ATP control of dynamic P1 ParA-DNA interactions: a key role for the nucleoid in plasmid partition.
The insert domain of gyrB may have two functions, acting as a steric buttress to pre-configure the primary DNA-binding site, and serving as a relay that may help coordinate communication between different functional domains.
Title: A domain insertion in Escherichia coli GyrB adopts a novel fold that plays a critical role in gyrase function.
These results reveal an important function for Par systems in plasmid DNA segregation that is likely to be conserved in bacteria.
Title: Intracellular mobility of plasmid DNA is limited by the ParA family of partitioning systems.
N-terminus verified by Edman degradation on mature peptide
Title: DNA sequence of the E. coli gyrB gene: application of a new sequencing strategy.

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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 ATP binding	IDA Inferred from Direct Assay more info	PubMed
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP-dependent activity, acting on DNA	IDA Inferred from Direct Assay more info	PubMed
enables DNA binding	IDA Inferred from Direct Assay more info	PubMed
enables DNA binding	IEA Inferred from Electronic Annotation more info
enables DNA binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables DNA negative supercoiling activity	IDA Inferred from Direct Assay more info	PubMed
enables DNA negative supercoiling activity	IEA Inferred from Electronic Annotation more info
enables DNA topoisomerase activity	IEA Inferred from Electronic Annotation more info
enables DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity	IBA Inferred from Biological aspect of Ancestor more info
enables DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity	IDA Inferred from Direct Assay more info	PubMed
enables DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in DNA topological change	IBA Inferred from Biological aspect of Ancestor more info
involved_in DNA topological change	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within DNA topological change	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in DNA-templated DNA replication	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within DNA-templated transcription	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in chromosome organization	IEA Inferred from Electronic Annotation more info
involved_in response to antibiotic	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within response to xenobiotic stimulus	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
part_of DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex	IDA Inferred from Direct Assay more info	PubMed
located_in chromosome	IEA Inferred from Electronic Annotation more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed