A0A2V0N1C3 · A0A2V0N1C3_9MYCO

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 site459Mg2+ 1 (UniProtKB | ChEBI); catalytic
Site484Interaction with DNA
Site487Interaction with DNA
Binding site532Mg2+ 2 (UniProtKB | ChEBI)
Binding site532Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site534Mg2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchromosome
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular FunctionDNA binding
Molecular FunctionDNA negative supercoiling 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
      MFM001_04510

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MFM001
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium

Accessions

  • Primary accession
    A0A2V0N1C3

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 region, compositional bias, domain.

TypeIDPosition(s)Description
Region226-246Disordered
Compositional bias228-246Basic and acidic residues
Domain453-567Toprim

Sequence similarities

Belongs to the type II topoisomerase GyrB family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    675
  • Mass (Da)
    74,574
  • Last updated
    2018-09-12 v1
  • Checksum
    1D97E5FE3EF33C67
MAAQKKSTKQYGAESITVLEGLEAVRKRPGMYIGSTGERGLHHLIWEVVDNAVDEAMAGYATEVDVKILEDGGVQVTDNGRGIPVAMHATGMPTVDVVMTQLHAGGKFGGDDSAYAVSGGLHGVGVSVVNALSTRLEVEISTDGYEWFQHYDRSVPGTLKQGEKTKTTGTTVRFWADPDIFETTDYDFETVARRLQEMAFLNKGLTINLTDQRVRNEEVVDEVVSDTADAPKTAREEAEERSTQKVKHRTFHYPGGLVDFVKHINRTKNPIHSSIVDFSGKGPGHEVEIAMQWNAGYSESVHTFANTINTHEGGTHEEGFRAALTSVVNKYAKDRKLLKDKDPNLTGDDIREGLAAVISVKVSEPQFEGQTKTKLGNTEVKSFVQKVCNEQLTHWFEANPSDAKTVVNKAVSSAQARIAARKARELVRRKSATDLGGLPGKLADCRSTDPRKSELYVVEGDSAGGSAKSGRDSMFQAILPLRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDITKLRYHKIVLMADADVDGQHISTLLLTLLFRFMRPLIENGHVFLAQPPLYKLKWQRSDPEFAYSDRERDGLLEAGQKAGKKINKDDGIQRYKGLGEMDAKELWETTMDPSVRVLRQVTLDDAAAADELFSILMGEDVDARRSFITRNAKDVRFLDV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias228-246Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BFAB01000001
EMBL· GenBank· DDBJ
GBE63989.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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