ID   GYRA_NEIGO              Reviewed;         916 AA.
AC   P48371;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
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   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MS11;
RX   PubMed=7830580; DOI=10.1111/j.1365-2958.1994.tb01297.x;
RA   Belland R.J., Morrison S.G., Ison C., Huang W.M.;
RT   "Neisseria gonorrhoeae acquires mutations in analogous regions of gyrA and
RT   parC in fluoroquinolone-resistant isolates.";
RL   Mol. Microbiol. 14:371-380(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. {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; U08817; AAA82128.1; -; Genomic_DNA.
DR   PIR; S60779; S60779.
DR   AlphaFoldDB; P48371; -.
DR   SMR; P48371; -.
DR   ChEMBL; CHEMBL2311244; -.
DR   DrugCentral; P48371; -.
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; 7.
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..916
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145244"
FT   REGION          739..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          897..916
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           571..577
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   COMPBIAS        901..916
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        130
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   916 AA;  101530 MW;  6392550101C261CF CRC64;
     MTDATIRHDH KFALETLPVS LEDEMRKSYL DYAMSVIVGR ALPDVRDGLK PVHRRVLYAM
     HELKNNWNAA YKKSARIVGD VIGKYHPHGD SAVYDTIVRM AQNFAMRYVL IDGQGNFGSV
     DGLAAAAMRY TEIRMAKISH EMLADIEEET VNFGPNYDGS EHEPLVLPTR FPTLLVNGSS
     GIAVGMATNI PPHNLTDTIN ACLRLLDEPK TEIDELIDII QAPDFPTGAT IYGLGGVREG
     YKTGRGRVVM RGKTHIEPIG KNGERERIVI DEIPYQVNKA KLVEKIGDLV REKTLEGISE
     LRDESDKSGM RVVIELKRNE NAEVVLNQLY KLTPLQDSFG INMVVLVDGQ PRLLNLKQIL
     SEFLRHRREV VTRRTLFRLK KARHEGHIAE RKAVALSNID EIIKLIKESP NAAEAKEKLL
     ARPWASSLVE EMLTRSGLDL EMMRPEGLVA NIGLKKQGYY LSEIQADAIL RMSLRNLTGL
     DQKEIIESYK NLMGKIIDFV DILSKPERIT QIIRDELEEI KTNYGDERRS EINPFGGDIA
     DEDLIPQREM VVTLTHGGYI KTQPTTDYQA QRRGGRGKQA AATKDEDFIE TLFVANTHDY
     LMCFTNLGKC HWIKVYKLPE GGRNSRGRPI NNVIQLEEGE KVSAILAVRE FPEDQYVFFA
     TAQGMVKKVQ LSAFKNVRAQ GIKAIALKEG DYLVGAAQTG GADDIMLFSN LGKAIRFNEY
     WEKSGNDEAE DADIETEISD DLEDETADNE NTLPSGKNGV RPSGRGSGGL RGMRLPADGK
     IVSLITFAPE TEESGLQVLT ATANGYGKRT PIADYSRKNK GGQGSIAINT GERNGDLVAA
     TLVGETDDLM LITSGGVLIR TKVEQIRETG RAAAGVKLIN LDEGETLVSL ERVAEDESEL
     SGASVISNVT EPEAEN