ID   GYRA_STAAM              Reviewed;         889 AA.
AC   Q932M0;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 133.
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};
GN   Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897};
GN   OrderedLocusNames=SAV0006;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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   -!- 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000017; BAB56168.1; -; Genomic_DNA.
DR   RefSeq; WP_000819068.1; NC_002758.2.
DR   AlphaFoldDB; Q932M0; -.
DR   SMR; Q932M0; -.
DR   BindingDB; Q932M0; -.
DR   KEGG; sav:SAV0006; -.
DR   HOGENOM; CLU_002977_6_1_9; -.
DR   PhylomeDB; Q932M0; -.
DR   Proteomes; UP000002481; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   CDD; cd00187; TOP4c; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR   HAMAP; MF_01897; GyrA; 1.
DR   InterPro; IPR005743; GyrA.
DR   InterPro; IPR006691; GyrA/parC_rep.
DR   InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   NCBIfam; TIGR01063; gyrA; 1.
DR   PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR   PROSITE; PS52040; TOPO_IIA; 1.
DR   World-2DPAGE; 0002:Q932M0; -.
PE   3: Inferred from homology;
KW   Antibiotic resistance; ATP-binding; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
FT   CHAIN           1..889
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145252"
FT   DOMAIN          35..501
FT                   /note="Topo IIA-type catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01384"
FT   REGION          811..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           528..534
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   COMPBIAS        825..842
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        862..879
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        123
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   889 AA;  99650 MW;  4A533AA0A1AC4943 CRC64;
     MAELPQSRIN ERNITSEMRE SFLDYAMSVI VARALPDVRD GLKPVHRRIL YGLNEQGMTP
     DKSYKKSARI VGDVMGKYHP HGDLSIYEAM VRMAQDFSYR YPLVDGQGNF GSMDGDGAAA
     MRYTEARMTK ITLELLRDIN KDTIDFIDNY DGNEREPSVL PARFPNLLAN GASGIAVGMA
     TNIPPHNLTE LINGVLSLSK NPDISIAELM EDIEGPDFPT AGLILGKSGI RRAYETGRGS
     IQMRSRAVIE ERGGGRQRIV VTEIPFQVNK ARMIEKIAEL VRDKKIDGIT DLRDETSLRT
     GVRVVIDVRK DANASVILNN LYKQTPLQTS FGVNMIALVN GRPKLINLKE ALVHYLEHQK
     TVVRRRTQYN LRKAKDRAHI LEGLRIALDH IDEIISTIRE SDTDKVAMKS LQQRFKLSEK
     QAQAILDMRL RRLTGLERDK IEAEYNELLN YISELETILA DEEVLLQLVR DELTEIRDRF
     GDDRRTEIQL GGFEDLEDED LIPEEQIVIT LSHNNYIKRL PVSTYRAQNR GGRGVQGMNT
     LEEDFVSQLV TLSTHDHVLF FTNKGRVYKL KGYEVPELSR QSKGIPVVNA IELENDEVIS
     TMIAVKDLES EDNFLVFATK RGVVKRSALS NFSRINRNGK IAISFREDDE LIAVRLTSGQ
     EDILIGTSHA SLIRFPESTL RPLGRTATGV KGITLREGDE VVGLDVAHAN SVDEVLVVTE
     NGYGKRTPVN DYRLSNRGGK GIKTATITER NGNVVCITTV TGEEDLMIVT NAGVIIRLDV
     ADISQNGRAA QGVRLIRLGD DQFVSTVAKV KEDAEDETNE DEQSTSTVSE DGTEQQREAV
     VNDETPGNAI HTEVIDSEEN DEDGRIEVRQ DFMDRVEEDI QQSSDEDEE
//