P21557 · GYRA_HALL2

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

Mutations in DNA gyrase result in novobiocin resistance in halophilic archaebacteria.
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)

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site133O-(5'-phospho-DNA)-tyrosine intermediate

GO annotations

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

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA gyrase subunit A
  • EC number

Gene names

    • Name
      gyrA
    • ORF names
      C456_09158

Organism names

Accessions

  • Primary accession
    P21557
  • Secondary accessions
    • M0GQR6
    • Q47968

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001452731-858DNA gyrase subunit A

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.

Structure

Family & Domains

Features

Showing features for domain, motif, region, compositional bias.

TypeIDPosition(s)Description
Domain45-517Topo IIA-type catalytic
Motif544-550GyrA-box
Region833-858Disordered
Compositional bias834-858Acidic residues

Sequence similarities

Belongs to the type II topoisomerase GyrA/ParC subunit family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    858
  • Mass (Da)
    94,437
  • Last updated
    2014-05-14 v2
  • Checksum
    0D59C30C3C757155
MSSDAPDSFEPGAGIAAEVKNARIEDEMEQSYIDYAMSVIAGRALPDVRDGLKPVHRRILYAMHQAGVTSNSSHRKSSSIVGETMGDYHPHGDSAIYDTLARMAQDFSMRYPLVDGQGNFGSVDGDPPAAMRYTEARMSPIAEELLDDIDKDTVDFQSNYDDRKQEPTVLPSSFPNLLVNGSSGIAVGMSTNIPPHNLGEVVDATVELIENPDATVADLMEHIKGPDFPTGANIVGRNAVHKAYKTGRGRVRVRADYDVFEEEGRIVINELPYQENKARLIERIADDVNEGKIEGIRDIRDESDRDGIRVVIELKRGAMAEVVKNQLLDNHLESTFGVINLALVDGQPQVLTLKETLEHYLDHRRDVVRRRSEYELAEAEDRAHILDGRLKALDNIDDVVETIRNSESRDDAKAALRGEVEVEVDGEPLPTFDFSEEQANHIVSMQLGSLTSMEAAEIEAEYEDVQATIERLETILGDQSELDAVIESELLDIKDEYADDRRTSFVANTGEVTRADLIPEEDVVVVVSEDDYIKRMPVSRFRAQHRGGKGIIGTDLKEGDNVSSVFVTNTHDDLLCFTNHGQVYQLKAYQVPEMSRTARGKSAVNLLDFDDGEEITAVVNCDDLEDIEGYLTMVTRNGYIKRTGTDRFQNILSTGIIATKLDEGDELVDVEVTDGESDLVIGTERGMSIRFDEDEVRAMGRSARGVRGIKLEGDDVVAGVAAIDEAHHSWILTVTENGYGKRTDLDAYRTQSRNGKGLIDIKANERNGPVCAINTVGEGDHLVVMSDEGQILRTPVEDISTVGRNTMGVIVMDLDEGDAVASVDVIPAAMTTEAEELDDADSVEEDAETDAKADADDE

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict105in Ref. 1; CAA42740
Sequence conflict205in Ref. 1; CAA42740
Sequence conflict236in Ref. 1; CAA42740
Sequence conflict304in Ref. 1; CAA42740
Sequence conflict677in Ref. 1; CAA42740
Sequence conflict809in Ref. 1; CAA42740
Compositional bias834-858Acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X60178
EMBL· GenBank· DDBJ
CAA42740.1
EMBL· GenBank· DDBJ
Genomic DNA
M38373
EMBL· GenBank· DDBJ
AAB09606.1
EMBL· GenBank· DDBJ
Genomic DNA
AOLH01000015
EMBL· GenBank· DDBJ
ELZ74525.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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