ID A0A1M6HZR8_9CLOT Unreviewed; 809 AA.
AC A0A1M6HZR8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=SAMN02745176_03022 {ECO:0000313|EMBL:SHJ27759.1};
OS Lutispora thermophila DSM 19022.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Lutispora.
OX NCBI_TaxID=1122184 {ECO:0000313|EMBL:SHJ27759.1, ECO:0000313|Proteomes:UP000184442};
RN [1] {ECO:0000313|EMBL:SHJ27759.1, ECO:0000313|Proteomes:UP000184442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19022 {ECO:0000313|EMBL:SHJ27759.1,
RC ECO:0000313|Proteomes:UP000184442};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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 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; FQZS01000025; SHJ27759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6HZR8; -.
DR STRING; 1122184.SAMN02745176_03022; -.
DR Proteomes; UP000184442; Unassembled WGS sequence.
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; 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 NCBIfam; TIGR01063; gyrA; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01897}; 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:UP000184442};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..464
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 525..531
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 809 AA; 90903 MW; 3B2348235108A8A1 CRC64;
MENKEGNLLY VNIEDEMKNS FIDYAMSVIV QRALPDVRDG LKPVHRRILY AMHSLGFTPD
KPHRKSATTV GEVLGKYHPH GDAAVYDTMV RMAQDFNYRY TLIDGHGNFG SIDGDSAAAM
RYTEARMSKI AMEMLKDINK ETVDFVPNYD ESLKEPSVLP SKFPNLLVNG SNGIAVGMAT
SIPPHNLGEV IDGIIATIDN PDIELEELMK HIKGPDFPTG ALIMGKDGIR KAYATGRGKV
VVRAKAEIES MFGNRQRIVV TEIPYQVNKA NLIEKIADLV KEKKIEGISD LRDESDREGM
RIVIELKRDA NANIVLNLLY KHTQMQSAFS IIMLALDNGQ PKVMNLKEMI QKYIDHQRQI
IIRRTQYDLR KAEERAHILE GLKIALDHID EIINIIRSSK TVNEARERMM ARFGLSEEQA
TAIAEMRLKS LTGLEREKIE EEYLGLIKDI EYYKSILASE LMVSNIIKEE LLEIKKTYAD
KRRSKITHSV EEVNEEDLIE EEEVAVTLTH FGYIKRLPAD TYKSQRRGGK GITALQTRED
DFVEHLFITS THNQLLFFTN KGRMFRLKAY EIPEAGRQAK GTALVNLLQL DKNEAVNAVI
PIKEFEDEGY LIFMTKNGII KKTELKQYSS HRATGLNAIT LKDEDELISV KLTRGTSELI
AITRQGLAIR FPEKDVRDMG RTAMGVKGVT LNPGDSVIAL DIVEEGADLL VISERGFGKR
TPLSEYRVQS RGGKGIKTSN ITAKTGYLVG AKVVKDDCEV MLISAEGVII RLHINDISVM
GRSTQGVTLM KLAEHDSVVA LAKIVPDEE
//
