P21557 · GYRA_HALL2
- ProteinDNA gyrase subunit A
- GenegyrA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids858 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 133 | O-(5'-phospho-DNA)-tyrosine intermediate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | cytoplasm | |
Cellular Component | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex | |
Molecular Function | ATP binding | |
Molecular Function | DNA binding | |
Molecular Function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity | |
Biological Process | DNA topological change | |
Biological Process | DNA-templated DNA replication |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA gyrase subunit A
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Haloferax
Accessions
- Primary accessionP21557
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000145273 | 1-858 | DNA gyrase subunit A | |||
Sequence: MSSDAPDSFEPGAGIAAEVKNARIEDEMEQSYIDYAMSVIAGRALPDVRDGLKPVHRRILYAMHQAGVTSNSSHRKSSSIVGETMGDYHPHGDSAIYDTLARMAQDFSMRYPLVDGQGNFGSVDGDPPAAMRYTEARMSPIAEELLDDIDKDTVDFQSNYDDRKQEPTVLPSSFPNLLVNGSSGIAVGMSTNIPPHNLGEVVDATVELIENPDATVADLMEHIKGPDFPTGANIVGRNAVHKAYKTGRGRVRVRADYDVFEEEGRIVINELPYQENKARLIERIADDVNEGKIEGIRDIRDESDRDGIRVVIELKRGAMAEVVKNQLLDNHLESTFGVINLALVDGQPQVLTLKETLEHYLDHRRDVVRRRSEYELAEAEDRAHILDGRLKALDNIDDVVETIRNSESRDDAKAALRGEVEVEVDGEPLPTFDFSEEQANHIVSMQLGSLTSMEAAEIEAEYEDVQATIERLETILGDQSELDAVIESELLDIKDEYADDRRTSFVANTGEVTRADLIPEEDVVVVVSEDDYIKRMPVSRFRAQHRGGKGIIGTDLKEGDNVSSVFVTNTHDDLLCFTNHGQVYQLKAYQVPEMSRTARGKSAVNLLDFDDGEEITAVVNCDDLEDIEGYLTMVTRNGYIKRTGTDRFQNILSTGIIATKLDEGDELVDVEVTDGESDLVIGTERGMSIRFDEDEVRAMGRSARGVRGIKLEGDDVVAGVAAIDEAHHSWILTVTENGYGKRTDLDAYRTQSRNGKGLIDIKANERNGPVCAINTVGEGDHLVVMSDEGQILRTPVEDISTVGRNTMGVIVMDLDEGDAVASVDVIPAAMTTEAEELDDADSVEEDAETDAKADADDE |
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 45-517 | Topo IIA-type catalytic | ||||
Sequence: LPDVRDGLKPVHRRILYAMHQAGVTSNSSHRKSSSIVGETMGDYHPHGDSAIYDTLARMAQDFSMRYPLVDGQGNFGSVDGDPPAAMRYTEARMSPIAEELLDDIDKDTVDFQSNYDDRKQEPTVLPSSFPNLLVNGSSGIAVGMSTNIPPHNLGEVVDATVELIENPDATVADLMEHIKGPDFPTGANIVGRNAVHKAYKTGRGRVRVRADYDVFEEEGRIVINELPYQENKARLIERIADDVNEGKIEGIRDIRDESDRDGIRVVIELKRGAMAEVVKNQLLDNHLESTFGVINLALVDGQPQVLTLKETLEHYLDHRRDVVRRRSEYELAEAEDRAHILDGRLKALDNIDDVVETIRNSESRDDAKAALRGEVEVEVDGEPLPTFDFSEEQANHIVSMQLGSLTSMEAAEIEAEYEDVQATIERLETILGDQSELDAVIESELLDIKDEYADDRRTSFVANTGEVTRADL | ||||||
Motif | 544-550 | GyrA-box | ||||
Sequence: QHRGGKG | ||||||
Region | 833-858 | Disordered | ||||
Sequence: EAEELDDADSVEEDAETDAKADADDE | ||||||
Compositional bias | 834-858 | Acidic residues | ||||
Sequence: AEELDDADSVEEDAETDAKADADDE |
Sequence similarities
Belongs to the type II topoisomerase GyrA/ParC subunit family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length858
- Mass (Da)94,437
- Last updated2014-05-14 v2
- Checksum0D59C30C3C757155
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 105 | in Ref. 1; CAA42740 | ||||
Sequence: Q → E | ||||||
Sequence conflict | 205 | in Ref. 1; CAA42740 | ||||
Sequence: T → A | ||||||
Sequence conflict | 236 | in Ref. 1; CAA42740 | ||||
Sequence: G → A | ||||||
Sequence conflict | 304 | in Ref. 1; CAA42740 | ||||
Sequence: D → E | ||||||
Sequence conflict | 677 | in Ref. 1; CAA42740 | ||||
Sequence: S → T | ||||||
Sequence conflict | 809 | in Ref. 1; CAA42740 | ||||
Sequence: V → I | ||||||
Compositional bias | 834-858 | Acidic residues | ||||
Sequence: AEELDDADSVEEDAETDAKADADDE |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |