ID   GYRA_SPICI              Reviewed;         227 AA.
AC   P34030;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=DNA gyrase subunit A;
DE            EC=5.6.2.2 {ECO:0000250|UniProtKB:P0AES4};
DE   Flags: Fragment;
GN   Name=gyrA;
OS   Spiroplasma citri.
OC   Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=2133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R8A2HP;
RX   PubMed=7764984; DOI=10.1007/bf01570187;
RA   Ye F., Renaudin J., Bove J.M., Laigret F.;
RT   "Cloning and sequencing of the replication origin (oriC) of the Spiroplasma
RT   citri chromosome and construction of autonomously replicating artificial
RT   plasmids.";
RL   Curr. Microbiol. 29:23-29(1994).
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.
CC       {ECO:0000250|UniProtKB:P0AES4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000250|UniProtKB:P0AES4};
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:0000250|UniProtKB:P0AES4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AES4}.
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.
CC       {ECO:0000250|UniProtKB:P0AES4}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family.
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DR   EMBL; Z19108; CAA79524.1; -; Genomic_DNA.
DR   PIR; S35735; S35735.
DR   AlphaFoldDB; P34030; -.
DR   SMR; P34030; -.
DR   STRING; 2133.SCITRI_004; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   Gene3D; 3.90.199.10; -; 1.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 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..>227
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145250"
FT   ACT_SITE        129
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AES4"
FT   NON_TER         227
SQ   SEQUENCE   227 AA;  25356 MW;  476C66482A9010A9 CRC64;
     MMKSENDGYD YDGKIRDIDI ADEMKNGFLD YAMSVIVSRA IPDVRDGLKP VHRRIIYAMW
     DLKMTYEKQH KKSARIVGEV IGKYHPHGDT AVYEAMVRMA QDFSYRYPLI DGHGNFGSMD
     GDPPAAMRYT EAKMSKIAGE IIKDIEKETT IFIDNYDGSE EEPTFLPGYF PNLLVNGASG
     IAVGMATNIP PHNLNEVIDG VIAVTKNPEI TTVELMKIIK GPDFPTG