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Database: UniProt
Entry: A0A370EWJ2_9FLAO
LinkDB: A0A370EWJ2_9FLAO
Original site: A0A370EWJ2_9FLAO 
ID   A0A370EWJ2_9FLAO        Unreviewed;       617 AA.
AC   A0A370EWJ2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=DEU42_102216 {ECO:0000313|EMBL:RDI14519.1};
OS   Flavobacterium sp. AG291.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2184000 {ECO:0000313|EMBL:RDI14519.1, ECO:0000313|Proteomes:UP000254305};
RN   [1] {ECO:0000313|EMBL:RDI14519.1, ECO:0000313|Proteomes:UP000254305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG291 {ECO:0000313|EMBL:RDI14519.1,
RC   ECO:0000313|Proteomes:UP000254305};
RA   Venturi V.;
RT   "Genome sequencing of rice bacterial endophytes.";
RL   Submitted (JUL-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:RDI14519.1}.
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DR   EMBL; QQAR01000002; RDI14519.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A370EWJ2; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000254305; 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; 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; 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:RDI14519.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000254305}.
FT   DOMAIN          408..514
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   617 AA;  70364 MW;  49333B2AD2E30B11 CRC64;
     MLEQNQYTED NIRSLDWKEH IRMRPGMYIG KLGDGSSPDD GIYILIKEVI DNSIDEFVMG
     TGKTIEVTLK DKTVSVRDFG RGIPLGKVVD VVSKMNTGGK YDSKAFKKSV GLNGVGTKAV
     NALSNYFRVE SVRDGIIKAA EFSAGELTNE EAETETSKRK GTKVTFIADD TIFKNYKYRN
     EYIIKMLKNY CYLNTGLTII YNGEKYFSED GLKDLLAETI SEEDRIYDII HLKDDDIEIA
     MTHSKTQYSE EYYSFVNGQN TTQGGTHLGA FREAIVRTIK EFYNKPFEAS DIRKSIVSAI
     SVKVEEPVFE SQTKTKLGST DMGPDAPSVR TFVNDFIKNK LDNFLHRNPE TADALLKKIL
     QAERERKELS GIRKLARDRA KKASLHNKKL RDCRVHLTDA KNPRSLESTL FITEGDSASG
     SITKSRDVNT QAVFSLRGKP LNSYGMTKKI VYENEEFNLL QAALDIEEEM ENLRYNNIVI
     ATDADVDGMH IRLLLITFFL QFFPELIKEN HLYILQTPLF RVRNKKETIY CYSEDERKAA
     IEKLKGKPEI TRFKGLGEIS PDEFKHFIGQ DIRLDPVLMD KATSIETLLE FYMGKNTPDR
     QEFIINNLKV ELDAVDE
//
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