ID   GYRA_STRP3              Reviewed;         828 AA.
AC   P0DG02; Q79X71; Q8K7H2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=SpyM3_0810;
OS   Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=198466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-595 / MGAS315;
RX   PubMed=12122206; DOI=10.1073/pnas.152298499;
RA   Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA   Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA   Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT   "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT   encoded toxins, the high-virulence phenotype, and clone emergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(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; AE014074; AAM79417.1; -; Genomic_DNA.
DR   RefSeq; WP_011054496.1; NC_004070.1.
DR   AlphaFoldDB; P0DG02; -.
DR   SMR; P0DG02; -.
DR   ChEMBL; CHEMBL3991502; -.
DR   PRIDE; P0DG02; -.
DR   EnsemblBacteria; AAM79417; AAM79417; SpyM3_0810.
DR   GeneID; 57852640; -.
DR   KEGG; spg:SpyM3_0810; -.
DR   HOGENOM; CLU_002977_6_1_9; -.
DR   OMA; THHWLLF; -.
DR   Proteomes; UP000000564; 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..828
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145265"
FT   MOTIF           524..530
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   ACT_SITE        120
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   828 AA;  92690 MW;  0CFCBD5AB0E7A523 CRC64;
     MQDRNLIDVN LTSEMKTSFI DYAMSVIVAR ALPDVRDGLK PVHRRILYGM NELGVTPDKP
     HKKSARITGD VMGKYHPHGD SSIYEAMVRM AQWWSYRHML VDGHGNFGSM DGDGAAAQRY
     TEARMSKIAL ELLRDINKNT VNFQDNYDGS EREPVVLPAR FPNLLVNGAT GIAVGMATNI
     PPHNLAESID AVKMVMEHPD CTTRELMEVI PGPDFPTGAL VMGRSGIHRA YDTGKGSIVL
     RSRTEIETTQ TGRERIVVTE FPYGVNKTKV HEHIVRLAQE KRLEGITAVR DESSREGVRF
     VIEIRREASA TVILNNLFKL TSLQTNFSFN MLAIENGVPK ILSLRQIIDN YISHQKEVII
     RRTRFDKDKA EARAHILEGL LIALDHLDEV IAIIRNSETD VIAQTELMSR FDLSERQSQA
     ILDMRLRRLT GLERDKIQSE YDDLLALIAD LSDILAKPER IITIIKEEMD EIKRKYANPR
     RTELMVGEVL SLEDEDLIEE EDVLITLSNK GYIKRLAQDE FRAQKRGGRG VQGTGVNNDD
     FVRELVSTST HDTLLFFTNF GRVYRLKAYE IPEYGRTAKG LPIVNLLKLE DGETIQTIIN
     ARKEETAGKS FFFTTKQGIV KRTEVSEFNN IRQNGLRALK LKEGDQLINV LLTSGQDDII
     IGTHSGYSVR FNEASIRNMG RSATGVRGVK LREDDRVVGA SRIQDNQEVL VITENGFGKR
     TSATDYPTKG RGGKGIKTAN ITPKNGQLAG LVTVDGTEDI MVITNKGVII RTNVANISQT
     GRATLGVKIM KLDADAKIVT FTLVQPEDSS IAEINTDREN SISKNKDN