ID   GYRA_KLEOX              Reviewed;         876 AA.
AC   P14829;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 113.
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};
OS   Klebsiella oxytoca.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M5a1;
RX   PubMed=2155395; DOI=10.1093/nar/18.1.151;
RA   Dimri G.P., Das H.K.;
RT   "Cloning and sequence analysis of gyrA gene of Klebsiella pneumoniae.";
RL   Nucleic Acids Res. 18:151-156(1990).
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; X16817; CAA34724.1; -; Genomic_DNA.
DR   PIR; S07722; ITKBAP.
DR   AlphaFoldDB; P14829; -.
DR   SMR; P14829; -.
DR   STRING; 571.MC52_27890; -.
DR   PRIDE; P14829; -.
DR   eggNOG; COG0188; Bacteria.
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..876
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145238"
FT   REGION          844..876
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           559..565
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   876 AA;  97155 MW;  7722CBFB07418D42 CRC64;
     MSDLAREITP VNIEEELKSS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMNVLGNDWN
     KAYKKSARVV GDVIGKYHPH GDTAVYDTIV RMAQPFSLRY MLVDGQGNFG SVDGDSAAAM
     RYTEIRMSKI AHELMADLEK ETVDFVDNYD GTEKIPDVMP TKIPNLLVNG SFGIAVGMAT
     NIPPHNLTEV INGRLAYVED EEISIEGLME HIPGPDFPTA AIINGRRGIE EAYRTGRGKV
     YICARAEVEA DAKTGRETII VHEIPYQVNK ARLIEKIAEL VKEKRVEGIS ALRDESDKDG
     MRIVIEVKRD AVGRVVLNNL YSQTQLQVSF GINMVALHHG QPKIMNLKEI IAAFVRHRRE
     VVTRRTILAL RKARDRADIL EALSIALANI DPIIELIRRA PTPAEAKAGL IARSWDLGNV
     SAMLEAGDDA ARPEWLEPEF GVRDGQYYLT EQQAQAILDL RLQKLTGLEH EKLLDEYKEL
     LEQIAELLHI LGSADRLMEV IREELELVRE QFGDARRTDI TANSVDINIE DLITQEDVVV
     TLSHEGYVKY QPVNDYEAQR RGGKGKSAPR IKEEDFIDRL LVANTHDTIL CFSSRGRLYW
     MKVYQVPEAS RGARGRPIVN LLPLEANERY TAILPVREYE EGVNVFMATA SGTVKKTPAD
     EFSRPRSAGI IAVNLNEGDE LIGVDLTSGQ DEVMLFSAAG KVVRFKEDDV RAMGRTATGV
     RGIKLAGEDK VVSLIVPRGE GRILTATENG YRKRTAVAEY PTKSRATQGV ISIKVTERNG
     SVVGAVQVDD CDQIMMITDA GTLVRIRVSE VSIVGRNTQG VILIRTAEDE NVVALQRVAE
     PVDDEELDAI DGSAAEGDED IAPEADTDDD IAEDEE