ID   A0A0K9YND0_9BACL        Unreviewed;       845 AA.
AC   A0A0K9YND0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=ADS79_14880 {ECO:0000313|EMBL:KNB70248.1};
OS   Brevibacillus reuszeri.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=54915 {ECO:0000313|EMBL:KNB70248.1, ECO:0000313|Proteomes:UP000036834};
RN   [1] {ECO:0000313|Proteomes:UP000036834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9887 {ECO:0000313|Proteomes:UP000036834};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:KNB70248.1}.
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DR   EMBL; LGIQ01000009; KNB70248.1; -; Genomic_DNA.
DR   RefSeq; WP_049739218.1; NZ_LGIQ01000009.1.
DR   AlphaFoldDB; A0A0K9YND0; -.
DR   STRING; 54915.ADS79_14880; -.
DR   PATRIC; fig|54915.3.peg.1972; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000036834; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
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   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; IPR005741; TopoIV_A_Gpos.
DR   NCBIfam; TIGR01061; parC_Gpos; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   PANTHER; PTHR43493:SF9; DNA TOPOISOMERASE 4 SUBUNIT A; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 5.
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   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          9..468
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   REGION          811..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          440..500
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        823..845
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   845 AA;  93949 MW;  9E97F19DA7B76A39 CRC64;
     MLSNQIIKQS FAEIMGKRFG DYANLVILSR AIPDARDGLK PVQRRILYAM YQEGNTNDKP
     YRKSAKTVGY VMGTYHPHGD SAIYETMVRM AQWWKMRQVL IQGHGNFGSL DADPPAAMRY
     TESRLSALSN ELLRDIEKET VTFIPNYDNS AMQPAVLPAR FPNLLVNGAS GIAVGFATDI
     PTHNLGEVID AAIAQMKNPN ITLDELMQLV KGPDFPTGAI VQGLSGIRKA FETGRGQFII
     RAKTHVEEPK GAKVKKIVVS EIPYEVVKSK LVAQIDELVM ERKIEGAIAV RDETGRKEAE
     QKKVRIVVDI RKEADEKAIL NYLYKNTDLQ IYYNYNMNVI HEGTIRQMGL KALLAAYVDH
     QKEVVTNRSQ YDLNKKQNRE HIVQGLIRAK SILREIVDTI MDSEDRADAK RNIMEKYGFT
     DVQADAILNI QLASLTRLDI VKLEKELATL AKEIEELKAI LGSEKKLIQV ITGELNEIKK
     KYAEERLTEI QGEIEEIKID IAMQINAEDC IVTLTNEGYI KRTSPRSFKS VGGTLETCGV
     KEGDRVRYFV ETNTSHTALF FTHDGKYFAT LVNAFPDDKW KDIGSALVNV IPLEKQQRIV
     GFTIVENFKQ ELYVYHVSKS GLVKKTALSE YETNRSSALV AAKLKSDEDE FVHVFIADEA
     GGILGATKDG MGIRFMRSEV STTGRASSGV KAISLGADDE VITMLPIEEE DKRAFSLVTT
     DGVLKRTAIT DIPLQGRAGK GVTLIRKRKS NPHQLLAITI EDTMYAWIEQ NEWVLIDKEL
     VIVNEQGGIG RTVIEGGLKA IAFETILPTD EAKDDGSTKA SGEGAASGGS SQKTPNSGQS
     SLFDE
//