ID A0A1F8B823_9BACT Unreviewed; 877 AA.
AC A0A1F8B823;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=A3A75_05670 {ECO:0000313|EMBL:OGM60161.1};
OS Candidatus Woesebacteria bacterium RIFCSPLOWO2_01_FULL_39_10.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1802516 {ECO:0000313|EMBL:OGM60161.1, ECO:0000313|Proteomes:UP000179018};
RN [1] {ECO:0000313|EMBL:OGM60161.1, ECO:0000313|Proteomes:UP000179018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGM60161.1}.
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DR EMBL; MGHC01000010; OGM60161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8B823; -.
DR STRING; 1802516.A3A75_05670; -.
DR Proteomes; UP000179018; 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; 2.
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 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; 2.
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}; 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};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 9..507
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 858..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 472..527
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 569..575
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 862..877
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 877 AA; 97786 MW; EBCC94D96F1DDD8C CRC64;
MEIGKVQPAN IVEEMQKSYL DYAMSVIVAR ALPDVRDGLK PVHRRILYAM HQMGLTHTSS
FTKSAKVVGE VLGKYHPHGD MAVYDSLVRM AQEFSLRYPL IKGQGNFGSV DGDPAAAMRY
TEVKLSSISQ FMLQDIEKET VSFLDNFDAT LKEPVYLPAL LPNLLLMGSE GIAVGMATKI
PPHNLSEVVE AVIATISKGT VTFEKKVQEE ETEFVIKKIN LVAAGHEETP KDGEIAASEV
GFESDITTEE LVEIVPGPDF PTGGAIYDAV SLRDVYATGR GRILVRGIAE IKDGTKGRQN
IIISEIPYQV NKAMLVKKVA DLVKEKKIVG IADLRDESDK DGMRVVIELK RDSRPKSVLN
NLFKHTQLQS SFPANFVTLV DGTPYTLNLK QIIVEYIKHR QKVITKRTIF ELTAAKRRAH
ILEGLKIALD NLDEVIATIR KSQTQEDAKN NLIKKFGLTD IQATAILDMQ LRRLAALERD
KIEKEYEELK KIIDRLTAIL KDPKKVLEII VKELTELKEK YKDARRTKIY KQRLGEFSEE
DLIPKEETLI TLTRTGYVKR VPRTIYRAQR RGGKGVTGMT TKEEDEIEQI ISATTHDMLL
FFTNTGRVFG TKVWEIPESS RQSKGQAVVN LIDLGQDEKI MSILPMNSKG AHLLMTTRQG
VVKKTKTSEF ENLRASGLIA IRLDPKDSLV GVHETTGNDH VLLVTKNGKG IRFPEANTRS
MGRATSGMRG IRLDSDDEVI GMEVFPGKED KPSDKRKKFF RDILTISEKG LGKRTPVHLF
PIQRRAGKGV KAAVVNVKTG KLAAASMVTQ ETEQIVITSR SGQVIKLPNK NIPQLGRSTQ
GVILMRFARK SDSVAAVAPL NRNGEDEEEE LGEKKVN
//
