ID   Q2FUD5_METHJ            Unreviewed;       839 AA.
AC   Q2FUD5;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   18-JUN-2025, entry version 117.
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   OrderedLocusNames=Mhun_1045 {ECO:0000313|EMBL:ABD40795.1};
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Methanomicrobia; Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259 {ECO:0000313|EMBL:ABD40795.1, ECO:0000313|Proteomes:UP000001941};
RN   [1] {ECO:0000313|Proteomes:UP000001941}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1
RC   {ECO:0000313|Proteomes:UP000001941};
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
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};
CC   -!- SUBUNIT: Heterotetramer composed of ParC and ParE.
CC       {ECO:0000256|ARBA:ARBA00063644}.
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; CP000254; ABD40795.1; -; Genomic_DNA.
DR   RefSeq; WP_011448074.1; NC_007796.1.
DR   AlphaFoldDB; Q2FUD5; -.
DR   STRING; 323259.Mhun_1045; -.
DR   EnsemblBacteria; ABD40795; ABD40795; Mhun_1045.
DR   GeneID; 3924758; -.
DR   KEGG; mhu:Mhun_1045; -.
DR   eggNOG; arCOG04367; Archaea.
DR   HOGENOM; CLU_002977_6_1_2; -.
DR   InParanoid; Q2FUD5; -.
DR   Proteomes; UP000001941; 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:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
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; 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   FunFam; 2.120.10.90:FF:000005; DNA topoisomerase 4 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {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:UP000001941};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_01897}.
FT   DOMAIN          41..504
FT                   /note="Topo IIA-type catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS52040"
FT   REGION          808..839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          435..490
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           531..537
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT   COMPBIAS        826..839
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        129
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   839 AA;  94274 MW;  79040DCC250B53AA CRC64;
     MTSEESQQPL FVPKVNPVNI EEEMKSSYID YAMSVIIGRA IPDVRDGLKP VHRRSLFAMW
     EMGNTHDKPY KKSARVVGDV MGKYHPHGDA SIYDTIVKMA QPFSYRMMLV DGQGNFGSVD
     GDAPAAMRYT EVRLKREAEE LLTDLEKETV EFVPNFDESL QEPSVLPAKL PNLLINGSDG
     IAVGIATKMP PHNLGEVCDA VCHYLEHPDT TVYELMQIMP GPDFPTGGII MGTDGIQNAY
     LSGQGKLTVR GVAEIDESGK RNQIIITEIP YQVNKAKLIE HIAELVKEKR IEGISDLRDE
     SDKDGMRIVI DLRKDARPQL ILNHLYKHTA LESTFGIINY AIVDRQPKIL GLIPLIEQFV
     RHRITVITRR SEFDKRKAEE RVHILRGLLH AIDNIDAVIT TIRAAQTADE AKEALIAKFS
     LDEAQAGAIL QMQLRRLAAL EKQKLIDERE QLEAEIRKLI ELLSSEDNIR AEISRELQEL
     REKYADKRRT QITGDLQEIV REDLIPNKQV LVCLTHQNYV KHMDVDAYRV QGRGGRGVMG
     ISIKDGDYVE QVFVANTHDH LLCFTSTGRA YWLRVFDIPE GSRQSKGKAI VNLLDLRSEE
     RVTAVIPVQE FSSDRFFLFL TERGMIIKIP QDEFSRPRST GVNAISLREG DNLVHVMVSD
     GSQEIIITTK YGQSLRFHEE QIPLRHRNAL GVIGMRMKDD DIVTSMTVIE EGKHLLTITS
     SGYGKRTNFD EYRGHGRGTM GVRNIKLKRN DGIVTAFSAG PEEEIILMSA EGIVIRTSVE
     KITIQGRSTQ GVRIMRLAAG DRVVGVTSLS PEEQKDISDD IPQAEIIDEG PDENGSSDE
//