ID   GYRA_LAWIP              Reviewed;         820 AA.
AC   Q1MQ89;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=LI0784;
OS   Lawsonia intracellularis (strain PHE/MN1-00).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Lawsonia.
OX   NCBI_TaxID=363253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHE/MN1-00;
RA   Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA   Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT   "The complete genome sequence of Lawsonia intracellularis: the causative
RT   agent of proliferative enteropathy.";
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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; AM180252; CAJ54838.1; -; Genomic_DNA.
DR   RefSeq; WP_011526867.1; NC_008011.1.
DR   AlphaFoldDB; Q1MQ89; -.
DR   SMR; Q1MQ89; -.
DR   STRING; 363253.LI0784; -.
DR   KEGG; lip:LI0784; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_6_1_7; -.
DR   OMA; THHWLLF; -.
DR   OrthoDB; 217468at2; -.
DR   Proteomes; UP000002430; 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   Reference proteome; Topoisomerase.
FT   CHAIN           1..820
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000409827"
FT   MOTIF           523..529
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   ACT_SITE        119
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   820 AA;  91735 MW;  065A898744EAADA8 CRC64;
     MSQTEHHISI EQEMRKSYLE YSLSVIIGRA IPDVRDGLKP VHRRILFAQQ ELGNSYTRPP
     KKCARIVGDV IGKYHPHGDS AVYDALVRMA QDFSMRDPLE EGQGNFGSID GDAPAAMRYT
     EVRMSRLASE FLSDIDKETV DFRPNYDNSL EEPIVLPTKV PNLLLNGSSG IAVGMATNIP
     PHNLGELCNA LLKIIDDPDV PIDNLLNIIH GPDFPTGGFI YVGQGLYDAY TKGRGTVKVR
     GKVEIEERKK GAQSIVIREI PFGLNKSSLV EKIAILVNER KIDGIADLRD ESDRKGIRVV
     IELKKGVIPE IIINALYKFT PLETSFGINM LAVVDNRPQL LTIKSALTYF LDHRREVIVR
     RTRFELNKAE ARLHILIGLI HALDHIDEVV NLIRSSSTPA EAKIRLIERF SLSEIQAQSI
     LDMRLQRLTG LEREKLEEEM HELQTKIAWY ESILGDTKIL WGVIRDEVTG IKEMYTTPRR
     TEVIRETLTN IEIEDLIPDD DVVITLSRRG YIKRTNLAIY QQQRRGGKGV AGLHTSEDDF
     VQEFITTTNH QFLLLFTNKG RMHQLKVHQV PEGSRTAKGT HIANIVPLEK EEWVTTILTV
     REFSDNKFFL FATRKGMVKR SSASYYARSR RTGLLAVGLR EDDELIMVKE VTNNDFIVLA
     TAEGFAIRFS CEDVRNMGRG AAGVKGIALR PGDSVVACLI LQEKQDTPAI MTVSNLGYGK
     RTSIDLYRVQ TRGGKGIINF KVTQKTGLVI GAKPVSDDNA LVLLTSTNKI IRMSVDEVRS
     AGRATMGVRL VKLDDGAYVV GFDTVDGTVD DSCDDATINT