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Database: UniProt
Entry: A0A3E0EWJ0_9FLAO
LinkDB: A0A3E0EWJ0_9FLAO
Original site: A0A3E0EWJ0_9FLAO 
ID   A0A3E0EWJ0_9FLAO        Unreviewed;       622 AA.
AC   A0A3E0EWJ0;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=C8P67_101304 {ECO:0000313|EMBL:REH01820.1};
OS   Flavobacterium aquicola.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1682742 {ECO:0000313|EMBL:REH01820.1, ECO:0000313|Proteomes:UP000257136};
RN   [1] {ECO:0000313|EMBL:REH01820.1, ECO:0000313|Proteomes:UP000257136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100880 {ECO:0000313|EMBL:REH01820.1,
RC   ECO:0000313|Proteomes:UP000257136};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (AUG-2018) 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:REH01820.1}.
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DR   EMBL; QUNI01000001; REH01820.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E0EWJ0; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000257136; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR   CDD; cd01030; TOPRIM_TopoIIA_like; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR002288; DNA_gyrase_B_C.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR001241; Topo_IIA.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR000565; Topo_IIA_B.
DR   InterPro; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR   PANTHER; PTHR45866:SF2; DNA TOPOISOMERASE (ATP-HYDROLYZING); 1.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF00986; DNA_gyraseB_C; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR01159; DNAGYRASEB.
DR   PRINTS; PR00418; TPI2FAMILY.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:REH01820.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          412..518
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   622 AA;  70776 MW;  811C8301B134A7C0 CRC64;
     MSDQNQYNED NIRSLDWKEH IRMRPGMYIG KLGDGSSPDD GIYILLKEVL DNCIDEFVMG
     AGKTIEVTIR DKAVAVRDYG RGIPLGKVVD VVSKMNTGGK YDSKAFQKSV GLNGVGTKAV
     NALSSSFRVE SVRDEKQKAA EFSAGNLVSE EDIIETTKRK GTKVTFTPDE TIFKNYKFRL
     EYVIKMVKNY CYLNNGLTII FNGEKYYSEN GLRDLLEETI NAEDLEYPII HLKDHDIEIA
     LTHSKTQYSE EYHSFVNGQN TTQGGTHLAA YREAIVKTIR EFYNKSFEAS DVRKSIVSAI
     SIKVMEPVFE SQTKTKLGSM DMGSDDGTPP VSVRTFVNDF IKTKLDNYLH KNPPTAEALL
     RKILQAERER KELSGIRKLA TDRAKKANLH NKKLRDCRAH LPDTKNPRNL ESTLFITEGD
     SASGSITKSR DVNTQAVFSL RGKPLNSYGM SKKIVYENEE FNLLQAALDI EDGLEKLRYN
     NIVIATDADV DGMHIRLLLI TFFLQFFPEL IKEGHLYILQ TPLFRVRNKK ETIYCYSEEE
     RVDAIEKLKP KPEITRFKGL GEISPDEFKN FIGDTIRLDP VMMDKHTSIE QLLSFYMGKN
     TPDRQDFIIK NLKVELDVVE EA
//
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