ID   GYRA_STAEP              Reviewed;          94 AA.
AC   P0C0Q9; P54112;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897};
DE            EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01897};
DE   Flags: Fragment;
GN   Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897};
OS   Staphylococcus epidermidis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF SER-84.
RX   PubMed=1662027; DOI=10.1128/aac.35.10.2151;
RA   Sreedharan S., Peterson L.R., Fisher L.M.;
RT   "Ciprofloxacin resistance in coagulase-positive and -negative
RT   staphylococci: role of mutations at serine 84 in the DNA gyrase A protein
RT   of Staphylococcus aureus and Staphylococcus epidermidis.";
RL   Antimicrob. Agents Chemother. 35:2151-2154(1991).
CC   -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC       circular double-stranded (ds) DNA in an ATP-dependent manner to
CC       modulate DNA topology and maintain chromosomes in an underwound state.
CC       Negative supercoiling favors strand separation, and DNA replication,
CC       transcription, recombination and repair, all of which involve strand
CC       separation. Also able to catalyze the interconversion of other
CC       topological isomers of dsDNA rings, including catenanes and knotted
CC       rings. Type II topoisomerases break and join 2 DNA strands
CC       simultaneously in an ATP-dependent manner. {ECO:0000255|HAMAP-
CC       Rule:MF_01897}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01897};
CC   -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. In
CC       the heterotetramer, GyrA contains the active site tyrosine that forms a
CC       transient covalent intermediate with DNA, while GyrB binds cofactors
CC       and catalyzes ATP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_01897}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897,
CC       ECO:0000305}.
CC   -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
CC       negative supercoils. Not all organisms have 2 type II topoisomerases;
CC       in organisms with a single type II topoisomerase this enzyme also has
CC       to decatenate newly replicated chromosomes. {ECO:0000255|HAMAP-
CC       Rule:MF_01897}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_01897}.
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DR   EMBL; S72603; AAB20672.1; -; Genomic_DNA.
DR   PIR; A49832; A49832.
DR   AlphaFoldDB; P0C0Q9; -.
DR   SMR; P0C0Q9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.199.10; -; 1.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; ATP-binding; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
FT   CHAIN           1..>94
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145258"
FT   MUTAGEN         84
FT                   /note="S->F: Resistant to ciprofloxacin."
FT                   /evidence="ECO:0000269|PubMed:1662027"
FT   NON_TER         94
SQ   SEQUENCE   94 AA;  10723 MW;  72862CF17C045728 CRC64;
     MAELPQSRIN ERNITSEMRE SFLDYAMSVI VSRALPDVRD GLKPVHRRIL YGLNEQGMTP
     DKPYKKSARI VGDVMGKYHP HGDSSIYEAM VRMA