ID   GYRA_BUCAP              Reviewed;         825 AA.
AC   Q8K9W2;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=BUsg_174;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(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}.
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DR   EMBL; AE013218; AAM67740.1; -; Genomic_DNA.
DR   RefSeq; WP_011053707.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9W2; -.
DR   SMR; Q8K9W2; -.
DR   STRING; 198804.BUsg_174; -.
DR   PRIDE; Q8K9W2; -.
DR   EnsemblBacteria; AAM67740; AAM67740; BUsg_174.
DR   KEGG; bas:BUsg_174; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_6_1_6; -.
DR   OMA; THHWLLF; -.
DR   OrthoDB; 217468at2; -.
DR   Proteomes; UP000000416; 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   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   Topoisomerase.
FT   CHAIN           1..825
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145224"
FT   MOTIF           542..548
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   825 AA;  93365 MW;  46130AAE8311219E CRC64;
     MKHLAREIVQ VDIEKELKSS YLDYAMSVIV GRALPDVRDG LKPVHRRILF AMHVLSNYWN
     KAYKKSARVV GDVIGKYHPH GDSAVYDSIV RMAQNFSLRY MLIDGQGNFG SIDGDAAAAM
     RYTEVRMSKI SQELLADLEK NTVEFIPNYD GTEHIPEILP SKIPNLLING SSGIAVGMAT
     NIPPHNLNEV IDGCLAYIKD DNITLRELIQ HIPGPDFPTA GIINGKKGIE EAYRTGKGKI
     YIRARNKIEK NKKNKKESII FYEIPYQVNK SRLIEKIAEL VKEKRIDGIT ALRDESDKDG
     MRIVVEIKKE AMSEIILNQL YSLTQLQISF GINMVALCQG QPKTLSLKEI LKHFLSHREE
     IVTRRSIFEL DKTCKRSHIL EGLSIALINI NCIIDLIKKA KSSLEAKELI IKKTWIYKNS
     EKINQKDHDY HFTEEQVQAI LDLRLHKLTS LEKNKLVLEY DCLTKKIKEL KKILKSRDRM
     REVIRDELVS IKNNFGDQRR TEITENNPDI SIEDLINQED VVVTLSHSGY VKYQPLSDYN
     AQKRGGKGKS AAKIKEEDFI ESLVVTNTHD TILCFSSRGI LYWMKVYQLP ESSRHAKGRP
     IVNLLPLSNK ERITAILPIH EFKDNLNIFM ATAQGIVKKS SLKEFKKPRI AGIIAINLRA
     NDELIGVSLT NGKNNIMLFT QNGKVVQFLE NSVRTMGRTA SGVRGIKISK NDKVVSLIVP
     YKKESILIAT NNGYGKRTKI TDFPIKSRAT QGVISIKITK KNGKIIGAIQ VVEKDQIMMI
     TNAGTLVRIR ASEIGVLKRN TQGVILIRTS KNEKVVALQR IVEPI