ID   A0A2G2K7Z5_9FLAO        Unreviewed;       618 AA.
AC   A0A2G2K7Z5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=COA88_10160 {ECO:0000313|EMBL:PHS06694.1};
OS   Kordia sp.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Kordia.
OX   NCBI_TaxID=1965332 {ECO:0000313|EMBL:PHS06694.1, ECO:0000313|Proteomes:UP000221821};
RN   [1] {ECO:0000313|Proteomes:UP000221821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) 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:PHS06694.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NVVR01000024; PHS06694.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G2K7Z5; -.
DR   Proteomes; UP000221821; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; 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; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:PHS06694.1}.
FT   DOMAIN          408..514
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   COILED          345..372
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   618 AA;  70704 MW;  06572D132B57E9EF CRC64;
     MSQETKYTED NIRSLDWKEH IRMRPGMYIG KLGDGASPDD GIYILLKEVL DNSIDEFVMG
     AGKTIEITTK DGKVTVRDYG RGIPLGKVID VVSKMNTGGK YDSKAFKKSV GLNGVGTKAV
     NALSSYFRVE SNRENERKAV DFSQGNITKD YPIENVVSRK GTKVVFIPDT AIFKNYKYRS
     EYVVKMLKNY VYLNLGLTII YNGEKYFSEN GLKDLLEDNN SKEDMLYPII HLKGEDIEVA
     ITHSKTQYSE EYHSFVNGQH TTQGGTHQAA FRESIVKTIR DFYGKTYEAS DIRKSIISAV
     AIKVMEPIFE SQTKTKLGSI EMGGELSTVR TYINDFIKTQ LDNYLHKNND VSEALQRKIL
     QAERERKELS GIRKLAKDRA KKSSLHNKKL RDCRVHLGDI KKERRLESTL FITEGDSASG
     SITKSRDVNT QAVFSLRGKP LNSYGMSKKI VYENEEFNLL QAALNIEESI SDLRYNNIVI
     ATDADVDGMH IRLLLITFFL QFFPELIKEG HLYILETPLF RVRNKKETIY CYSEEERVKA
     MNKLKGKPEI TRFKGLGEIS PDEFQFFIGE DIRLDPVMLD PETSIENLLQ FYMGKNTPDR
     QKFIINNLKV ELDIIEEE
//