A0A976UGG1 · A0A976UGG1_9LACO

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 site430Mg2+ 1 (UniProtKB | ChEBI); catalytic
Site455Interaction with DNA
Site458Interaction with DNA
Binding site503Mg2+ 2 (UniProtKB | ChEBI)
Binding site503Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site505Mg2+ 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
  • Organism
  • Strain
    • SNI3
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Lactiplantibacillus

Accessions

  • Primary accession
    A0A976UGG1

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 domain.

TypeIDPosition(s)Description
Domain33-179Histidine kinase/HSP90-like ATPase

Sequence similarities

Belongs to the type II topoisomerase GyrB family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    640
  • Mass (Da)
    71,134
  • Last updated
    2023-02-22 v1
  • Checksum
    54BCFE4725AF4976
KLEQAREYDASQIQVLEGLEAVRKRPGMYIGTTSSQGLHHLVWEIVDNGIDEALAGFANVIHVTVEKDNSITVTDNGRGIPVDIQEKTGKPALETVYTILHAGGKFGGGGYKVSGGLHGVGASVVNALSSTLDVKVTRNGHVYYMDFERGKVKTPMKIIGDAPDDAHGTAVHFVPDPDIFQETTTYDINILTTRIRELAFLNKGLRITIRDNRPDEPTEDDFLYEGGIRHYVEYLDKNKTVLFPEPIYVEGEQNGITVEVALQYTDDYHSNLMTFTNNIHTYEGGTHEEGFKRALTRVINDYARKNNLLKESDANLSGEDVREGMTAVVSVKHPDPQFEGQTKTKLGNSDARAAVDRLFSEHFSKYLMENPSVARKVVDKGLLASKARVAAKRAREVTRKKSGLEISNLPGKLADNSSKDPEISELFIVEGDSAGGSAKQGRSRLTQAILPIRGKILNVEKASIDKILANEEIRSLFTAMGTGFGGDFDLSKANYHKLIIMTDADVDGAHIRTLLLTLFYRYMRPLVDAGFVYIAQPPLYQVRQGKFVKYIDSDEELSEVMGQLAPSPKPVVQRYKGLGEMDAEQLWETTMDPDKRRLLRVRDEDAADADGVFSMLMGDQVKPRREFIEDNAKFVQDLDV

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MZ063535
EMBL· GenBank· DDBJ
UVH27480.1
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.
FeedbackHelp