GYRA_BACSU
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 03-AUG-2022, entry version 159.
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; Firmicutes; 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; P05653; -.
DR PRIDE; P05653; -.
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 OMA; THHWLLF; -.
DR PhylomeDB; P05653; -.
DR BioCyc; BSUB:BSU00070-MON; -.
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; 1.10.268.10; -; 1.
DR Gene3D; 2.120.10.90; -; 1.
DR Gene3D; 3.90.199.10; -; 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 Pfam; PF03989; DNA_gyraseA_C; 6.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; SSF101904; 1.
DR SUPFAM; SSF56719; SSF56719; 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 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
