ID   GYRA_SYNY3              Reviewed;         860 AA.
AC   Q55738;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 138.
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=slr0417;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA10380.1; -; Genomic_DNA.
DR   PIR; S76534; S76534.
DR   AlphaFoldDB; Q55738; -.
DR   SMR; Q55738; -.
DR   IntAct; Q55738; 1.
DR   STRING; 1148.1001649; -.
DR   PaxDb; Q55738; -.
DR   PRIDE; Q55738; -.
DR   EnsemblBacteria; BAA10380; BAA10380; BAA10380.
DR   KEGG; syn:slr0417; -.
DR   eggNOG; COG0188; Bacteria.
DR   InParanoid; Q55738; -.
DR   OMA; THHWLLF; -.
DR   PhylomeDB; Q55738; -.
DR   Proteomes; UP000001425; 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..860
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145269"
FT   MOTIF           530..536
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   ACT_SITE        122
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   860 AA;  95073 MW;  8CE4E91C4CE874C5 CRC64;
     MTDSPDRLIA TDLRNEMSQS YLEYAMSVIV GRALPDARDG LKPVHRRILY AMYELGLTPD
     RPFRKCARVV GEVLGKYHPH GDTAVYDALV RMAQDFSMRE PLIDGHGNFG SVDNDPPAAM
     RYTESRLRPL STNSLLRDIE AETVDFIDNF DGSQQEPTVL PARIPQLLIN GSSGIAVGMA
     TNIPPHNLGE VIDGAIALIR NPEITEQELM QIIPGPDFPT GAQILGRSGI REAYLTGRGS
     ITMRGVASIE TMEHPGRPDR DAIIVTELPY QTNKAALIER IADLVNDKKI DGIADIRDES
     DRDGMRIVIE LKRDAYARVV LNNLYKQTPI QSNFGANLLA LVNGTPEVLT IKKFLTVFWE
     FRIETITRRT RYELRKAEER DHLLQGLLIA LDNLDAVIRL IRGAADTASA KTELVEGFSL
     SEVQADAILQ MQLRRLTALE ADKITAEHDE LQTKIADFQD ILARRERVNA IIEEELEQIK
     AIHATPRRTV IVQEDGELID TDLIANDQAL ILLTEQGYIK RMPASTFGTQ NRATRGKAAA
     KIKDDDGVEH FLSCCDHDKV LFFSDRGVVY SLNAYQIPIA SRTARGVPIV QMLPIPKDEK
     ITSLVSVSEF DDDTYFIMLT KQGYIKKTAL SAFSNIRANG LIAISLVEGD QLRWVRLAKA
     EDSVIIGSQK GMAIHFKADQ DELRALGRAT RGVKSMRLRS GDALISMDIL PSQVVANIAV
     GSEDEPDEDL GGDTDAILEE SDNPGPWLLG VTMKGFGKRV PIGQFRLQHR AGLGVKAIRF
     KSKDDQLVAL HVVNADDELM IVTNRGIIIR QSVNDISPQS RSATGVRVQR LDADDAIAAV
     ALVPPSGEEE LAEMSESEES