ID   GYRA_STRCO              Reviewed;         857 AA.
AC   P35885; Q9KXX5;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   03-AUG-2022, entry version 141.
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}; OrderedLocusNames=SCO3873;
GN   ORFNames=SCH18.10c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=7828880; DOI=10.1016/0378-1119(94)90628-9;
RA   Calcutt M.J.;
RT   "Gene organization in the dnaA-gyrA region of the Streptomyces coelicolor
RT   chromosome.";
RL   Gene 151:23-28(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAA65216.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L27063; AAA65216.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL939118; CAB92993.1; -; Genomic_DNA.
DR   RefSeq; NP_628060.1; NC_003888.3.
DR   RefSeq; WP_011029284.1; NC_003888.3.
DR   AlphaFoldDB; P35885; -.
DR   SMR; P35885; -.
DR   STRING; 100226.SCO3873; -.
DR   GeneID; 1099309; -.
DR   KEGG; sco:SCO3873; -.
DR   PATRIC; fig|100226.15.peg.3946; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_6_1_11; -.
DR   InParanoid; P35885; -.
DR   OMA; THHWLLF; -.
DR   PhylomeDB; P35885; -.
DR   Proteomes; UP000001973; 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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW   Reference proteome; Topoisomerase.
FT   CHAIN           1..857
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145261"
FT   REGION          825..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           534..540
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   ACT_SITE        127
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   CONFLICT        41
FT                   /note="D -> V (in Ref. 1; AAA65216)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   857 AA;  94583 MW;  4306FD52CE64C547 CRC64;
     MTTPEGDALA MRVEPVGLET EMQRSYLDYA MSVIVSRALP DVRDGLKPVH RRVLYAMYDG
     GYRPERGFYK CARVVGDVMG NYHPHGDSSI YDALVRLAQP WSMRMPLVDS NGNFGSPGND
     PAAAMRYTEC KMAPLSMEMV RDIDEETVDF TDNYDGRSQE PTVLPARFPN LLINGSAGIA
     VGMATNIPPH NLREVAAGAQ WYLENYEASH EELLDALIER IKGPDFPTGA LVVGRKGIEE
     AYRTGRGSIT MRAVVEVEEI QNRQCLVVTE LPYQTNPDNL AQKIADLVKD GKVGGIADVR
     DETSSRTGQR LVIVLKRDAV AKVVLNNLYK HTDLQSNFGA NMLALVDGVP RTLSLDAFIR
     HWVNHQIEVI VRRTRFRLRK AEERAHILRG LLKALDAIDE VIALIRRSDT VEIARGGLMD
     LLEIDEIQAN AILEMQLRRL AALERQKIVR EHDELQAKIT EYNEILASPV RQRGIVSEEL
     TALVEKYGDD RKTKLIPYEG DMSIEDLIAE EDIVVTVTRG GYIKRTKTDD YRAQKRGGKG
     VRGTKLKEDD IVNHFFVSTT HHWLLFFTNK GRVYRAKAYE LPDAGRDARG QHVANLLAFQ
     PDETIAQIRA IRDYEAVPYL VLATKAGLVK KTPLKDYDSP RSGGVIAINL REQADGSDDE
     LIGAELVSAE DDLLLISKKA QSIRFTASDD TLRPMGRATS GVKGMSFREG DELLSMNVVR
     AGTFVFTATD GGYAKRTSVD EYRVQGRGGL GIKAAKIVED RGSLVGALVV EEHDEILAIT
     LSGGVIRTRV NGVRETGRDT MGVQLINLGK RDAVVGIARN AEAGREAEEV DGDVAVDETA
     EGAATTGTDE GEAPSAE