A0A553IGR6 · A0A553IGR6_ACHLA

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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.

TypeIDPosition(s)Description
Binding site427Mg2+ 1 (UniProtKB | ChEBI); catalytic
Site452Interaction with DNA
Site455Interaction with DNA
Binding site500Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site500Mg2+ 2 (UniProtKB | ChEBI)
Binding site502Mg2+ 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
    • ORF names
      FNV44_06735

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • PG8REry
  • Taxonomic lineage
    Bacteria > Mycoplasmatota > Mollicutes > Acholeplasmatales > Acholeplasmataceae > Acholeplasma

Accessions

  • Primary accession
    A0A553IGR6

Proteomes

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
Domain421-535Toprim

Sequence similarities

Belongs to the type II topoisomerase GyrB family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    635
  • Mass (Da)
    71,204
  • Last updated
    2019-10-16 v1
  • Checksum
    A53993656710C785
MPNNNNSHYTADNIQILEGLEAVKKRPGMYIGSTGERGLHHLVWEIVDNSIDEALGGYADEITIEILKGEVIRVTDNGRGIPVDIHPKTKRPAVETILTTLHAGGKFDKGSYKVSGGLHGVGASVVNGLSEWFVVEIHKDGTIYEQKYERGIPAYDLKVKGSTDKSGTIISFQADPLIFTETVIYNYETLRTRIQQLAFLNKGLKLNLIDDRFEENKSESFHYEGGITEYVKFLNQSKSKIHNDIIYIDKEQDGITVELAMQFVDSYSPNLHSFTNNISTTEGGMHEDGFKMALTRVISKYADDLKMKKDDSISGEDTREGLTAIISVKHPEPQFEGQTKTKLGNPEVRAITSQITSEAIERFLMENPAQAKAIVEKVLLATRARVAAIKAKDLTRRKSPLDALGFASKLADCRSKDPEKSEIYIVEGDSAGGSAKQGRDSEFQAIMPLRGKVLNVEKSRLDKMLSNKEIVNLIQAMGTGISDEFDITKARYHKIVIMTDADVDGAHIRTLLLTFLFRHMRPLIDAGYVYAAQPPLYKISWGRNFQYSYNEQELNELLKTIETKPSIQRYKGLGEMDAEQLWDTTMDPAKRTLLQIKLEDAIEADQVFSMLMGEEVEPRKEFIQNNAQYATDIDA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VKID01000002
EMBL· GenBank· DDBJ
TRX99392.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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