Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A679A7E5 · A0A679A7E5_9BACE

Function

function

A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.

Miscellaneous

Few gyrases are as efficient as E.coli at forming negative supercoils. Not all organisms have 2 type II topoisomerases; in organisms with a single type II topoisomerase this enzyme also has to decatenate newly replicated chromosomes.

Catalytic activity

  • ATP-dependent breakage, passage and rejoining of double-stranded DNA.
    EC:5.6.2.2 (UniProtKB | ENZYME | Rhea)

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds two Mg2+ per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn2+ or Ca2+.

Features

Showing features for binding site, site.

Type
IDPosition(s)Description
Binding site436Mg2+ 1 (UniProtKB | ChEBI); catalytic
Site461Interaction with DNA
Site464Interaction with DNA
Binding site516Mg2+ 2 (UniProtKB | ChEBI)
Binding site516Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site518Mg2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchromosome
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular FunctionDNA binding
Molecular FunctionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
Molecular Functionmetal ion binding
Biological ProcessDNA topological change
Biological ProcessDNA-templated DNA replication

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA gyrase subunit B
  • EC number

Gene names

    • Name
      gyrB

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Bacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides > environmental samples

Accessions

  • Primary accession
    A0A679A7E5

Subcellular Location

Keywords

Interaction

Subunit

Heterotetramer, composed of two GyrA and two GyrB chains. In the heterotetramer, GyrA contains the active site tyrosine that forms a transient covalent intermediate with DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region401-421Disordered
Domain430-551Toprim

Sequence similarities

Belongs to the type II topoisomerase GyrB family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    654
  • Mass (Da)
    72,803
  • Last updated
    2020-06-17 v1
  • MD5 Checksum
    1DED5B67FF7F8C847558BCDA2D99D4D3
MSEEEKQNGGSNYSASNIQVLEGLEAVRKRPAMYIGDISEKGLHHLVYEVVDNSIDEALAGYCDHIEVTINEDNSITVQDNGRGIPVDFHEKEKKSALEVVMTVLHAGGKFDKGSYKVSGGLHGVGVSCVNALSTHMTTNVYRNGKIYQQEYACGKPLYSVKEVGTSNLTGTKQTFWPDGSIFTVTEYKYDILQARMRELAYLNKGIRITLTDRRVKNEDGSFKCETFHSEEGVKEFVRFLNRNNEPLINDVIYLNTEKNGTPIECAIMYNTGYRESLHSYVNNINTIEGGTHEAGFRMALTRVLKKYAEDTKALEKAKVEINGEDFREGLIAVISVKVSEPQFEGQTKTKLGNNEVSGAVNQAVGEALTNYLEEHPKEAKLIVDKVILAATARIAARKARESVQRKSPMGGGGMPGKLADCSSRNPEECELFLVEGDSAGGSAKQGRSRATQAILPLRGKILNVEKAMWHKAFESDEVNNIITALGVRFGVEGSEDSKKANIDKLRYNKVIIMTDADVDGSHIDTLIMTLFYRYMPEVIEGGHLYIANPPLYKCSKGKISEYCYTDEARQAFIQKYADGQENGIHTQRYKGLGEMNPEQLWETTMNPETRILKQVSIENAANVDYIFSMLMGDDVAPRREFIEQNATYANIDA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MG725355
EMBL· GenBank· DDBJ
AZZ79597.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help