ID   GYRA_BACSU              Reviewed;         821 AA.
AC   P05653;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   27-MAR-2024, entry version 167.
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}; Synonyms=cafB, nalA;
GN   OrderedLocusNames=BSU00070;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2987847; DOI=10.1093/nar/13.7.2251;
RA   Moriya S., Ogasawara N., Yoshikawa H.;
RT   "Structure and function of the region of the replication origin of the
RT   Bacillus subtilis chromosome. III. Nucleotide sequence of some 10,000 base
RT   pairs in the origin region.";
RL   Nucleic Acids Res. 13:2251-2265(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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}.
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DR   EMBL; X02369; CAA26222.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05243.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11783.1; -; Genomic_DNA.
DR   PIR; F22930; F22930.
DR   RefSeq; NP_387888.1; NC_000964.3.
DR   RefSeq; WP_003244540.1; NZ_JNCM01000034.1.
DR   PDB; 4DDQ; X-ray; 3.30 A; A/B/C/D/E/F=1-502.
DR   PDBsum; 4DDQ; -.
DR   AlphaFoldDB; P05653; -.
DR   SMR; P05653; -.
DR   IntAct; P05653; 5.
DR   MINT; P05653; -.
DR   STRING; 224308.BSU00070; -.
DR   BindingDB; P05653; -.
DR   DrugBank; DB00537; Ciprofloxacin.
DR   jPOST; P05653; -.
DR   PaxDb; 224308-BSU00070; -.
DR   EnsemblBacteria; CAB11783; CAB11783; BSU_00070.
DR   GeneID; 940002; -.
DR   KEGG; bsu:BSU00070; -.
DR   PATRIC; fig|224308.179.peg.7; -.
DR   eggNOG; COG0188; Bacteria.
DR   InParanoid; P05653; -.
DR   OrthoDB; 9806486at2; -.
DR   PhylomeDB; P05653; -.
DR   BioCyc; BSUB:BSU00070-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR   GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
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.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Reference proteome; Topoisomerase.
FT   CHAIN           1..821
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145221"
FT   DOMAIN          35..500
FT                   /note="Topo IIA-type catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01384"
FT   MOTIF           527..533
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   ACT_SITE        123
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   TURN            38..40
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           44..55
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          60..62
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          64..66
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           67..77
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           82..92
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   TURN            96..98
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          103..108
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          125..128
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           132..136
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          146..148
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          152..159
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           166..170
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          172..176
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          179..183
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           188..200
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           206..210
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          222..224
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           227..236
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          237..244
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          246..251
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          257..263
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           270..282
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          289..294
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          303..307
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           313..323
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          324..333
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          335..344
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           347..388
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           390..398
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           403..414
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           418..425
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           429..432
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           434..459
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   HELIX           461..479
FT                   /evidence="ECO:0007829|PDB:4DDQ"
FT   STRAND          485..487
FT                   /evidence="ECO:0007829|PDB:4DDQ"
SQ   SEQUENCE   821 AA;  92099 MW;  717847A5F35FB857 CRC64;
     MSEQNTPQVR EINISQEMRT SFLDYAMSVI VSRALPDVRD GLKPVHRRIL YAMNDLGMTS
     DKPYKKSARI VGEVIGKYHP HGDSAVYESM VRMAQDFNYR YMLVDGHGNF GSVDGDSAAA
     MRYTEARMSK ISMEILRDIT KDTIDYQDNY DGSEREPVVM PSRFPNLLVN GAAGIAVGMA
     TNIPPHQLGE IIDGVLAVSE NPDITIPELM EVIPGPDFPT AGQILGRSGI RKAYESGRGS
     ITIRAKAEIE QTSSGKERII VTELPYQVNK AKLIEKIADL VRDKKIEGIT DLRDESDRTG
     MRIVIEIRRD ANANVILNNL YKQTALQTSF GINLLALVDG QPKVLTLKQC LEHYLDHQKV
     VIRRRTAYEL RKAEARAHIL EGLRVALDHL DAVISLIRNS QTAEIARTGL IEQFSLTEKQ
     AQAILDMRLQ RLTGLEREKI EEEYQSLVKL IAELKDILAN EYKVLEIIRE ELTEIKERFN
     DERRTEIVTS GLETIEDEDL IERENIVVTL THNGYVKRLP ASTYRSQKRG GKGVQGMGTN
     EDDFVEHLIS TSTHDTILFF SNKGKVYRAK GYEIPEYGRT AKGIPIINLL EVEKGEWINA
     IIPVTEFNAE LYLFFTTKHG VSKRTSLSQF ANIRNNGLIA LSLREDDELM GVRLTDGTKQ
     IIIGTKNGLL IRFPETDVRE MGRTAAGVKG ITLTDDDVVV GMEILEEESH VLIVTEKGYG
     KRTPAEEYRT QSRGGKGLKT AKITENNGQL VAVKATKGEE DLMIITASGV LIRMDINDIS
     ITGRVTQGVR LIRMAEEEHV ATVALVEKNE EDENEEEQEE V
//