ID   A8AXK8_STRGC            Unreviewed;       817 AA.
AC   A8AXK8;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   18-JUN-2025, entry version 118.
DE   RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897};
DE            EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_01897};
GN   Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897,
GN   ECO:0000313|EMBL:ABV10548.1};
GN   OrderedLocusNames=SGO_1231 {ECO:0000313|EMBL:ABV10548.1};
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705 {ECO:0000313|EMBL:ABV10548.1, ECO:0000313|Proteomes:UP000001131};
RN   [1] {ECO:0000313|EMBL:ABV10548.1, ECO:0000313|Proteomes:UP000001131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288
RC   {ECO:0000313|Proteomes:UP000001131};
RX   PubMed=17720781; DOI=10.1128/JB.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
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:0000256|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:0000256|ARBA:ARBA00000185,
CC         ECO:0000256|HAMAP-Rule:MF_01897, ECO:0000256|PROSITE-
CC         ProRule:PRU01384};
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:0000256|HAMAP-Rule:MF_01897}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_01897}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000256|ARBA:ARBA00008263, ECO:0000256|HAMAP-
CC       Rule:MF_01897}.
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DR   EMBL; CP000725; ABV10548.1; -; Genomic_DNA.
DR   RefSeq; WP_012000631.1; NC_009785.1.
DR   AlphaFoldDB; A8AXK8; -.
DR   STRING; 467705.SGO_1231; -.
DR   KEGG; sgo:SGO_1231; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_6_1_9; -.
DR   Proteomes; UP000001131; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IEA:TreeGrafter.
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:UniProtKB-ARBA.
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   FunFam; 1.10.268.10:FF:000001; DNA gyrase subunit A; 1.
DR   FunFam; 2.120.10.90:FF:000004; DNA gyrase subunit A; 1.
DR   FunFam; 3.30.1360.40:FF:000002; DNA gyrase subunit A; 1.
DR   FunFam; 3.90.199.10:FF:000001; DNA gyrase subunit A; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 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   InterPro; IPR050220; Type_II_DNA_Topoisomerases.
DR   NCBIfam; TIGR01063; gyrA; 1.
DR   NCBIfam; NF004043; PRK05560.1; 1.
DR   NCBIfam; NF004044; PRK05561.1; 1.
DR   PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR   PROSITE; PS52040; TOPO_IIA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01897};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01897};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01897};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01897};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01897}; Reference proteome {ECO:0000313|Proteomes:UP000001131};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_01897}.
FT   DOMAIN          32..497
FT                   /note="Topo IIA-type catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS52040"
FT   MOTIF           524..530
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT   ACT_SITE        120
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897,
FT                   ECO:0000256|PROSITE-ProRule:PRU01384"
SQ   SEQUENCE   817 AA;  91499 MW;  5CD5449F8C79653F CRC64;
     MQDKNLVNVN LTSEMKTSFI DYAMSVIVSR ALPDVRDGLK PVHRRILYGM NELGVTPDKP
     HKKSARITGD VMGKYHPHGD SSIYEAMVRM AQWWSYRYML VDGHGNFGSM DGDGAAAQRY
     TEARMSKIAL EMLRDINKNT VDFIDNYDAN EREPIVLPAR FPNLLVNGAT GIAVGMATNI
     PPHNLAESID AVKLVMDNPE ATTRDIMEVL PGPDFPTGAL VMGKSGIHRA YETGKGSIVL
     RSRTEIEEMK NGRERIVVTE FPYMVNKTKV HEHIVRLVQE KRIDGITAVR DESNREGVRF
     VIEVRRDASA HVILNNLFKL TQMQTNFSFN MLAIQNGVPK ILSLREILLA YIEHQKEVVT
     RRTAFDKDKA EARAHILAGL LIALDHIDEV IRIIRNSETD AEAQAELMAK FELSERQSQA
     ILDMRLRRLT GLERDKIQSE YDELIALIAD LADILAKPER VLTIIREELD EVKRKFADER
     RTELMVGEVL SLEDEDLIEE ADVLITLSNK GYIKRLNQDE FTAQKRGGRG VQGTGVKDDD
     FVKELVSTST HDRLLFFTNK GRVYRLKGYE IPEYGRTAKG LPIVNLLKLD EGETIQTIIN
     VEQDHSQDSY LFFTTRLGVV KRTSVADFAN IRQNGLKALN LKDEDELINV FLTDGAADVI
     IGTKFGYSVR FNETAVRNMS RIATGVRGVN LRDGDQVVGA GVVSDNDEVL VITEKGYGKR
     TLASEYPTKG RGGKGIKTAN ITEKNGPLAG LMTVNGQEDL MIITNTGVII RTSVANISQT
     GRSTMGVKVM RLDQNAQIVT FTTVEADDKE ELQDEKE
//