ID   TOP6B_THEKO             Reviewed;         567 AA.
AC   Q5JH81;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Type 2 DNA topoisomerase 6 subunit B {ECO:0000255|HAMAP-Rule:MF_00322};
DE            EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00322};
DE   AltName: Full=Type II DNA topoisomerase VI subunit B {ECO:0000255|HAMAP-Rule:MF_00322};
DE            Short=TopoVI-B {ECO:0000255|HAMAP-Rule:MF_00322};
GN   Name=top6B {ECO:0000255|HAMAP-Rule:MF_00322}; OrderedLocusNames=TK0799;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- FUNCTION: Relaxes both positive and negative superturns and exhibits a
CC       strong decatenase activity. {ECO:0000255|HAMAP-Rule:MF_00322}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00322};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two Top6A and two Top6B chains.
CC       {ECO:0000255|HAMAP-Rule:MF_00322}.
CC   -!- SIMILARITY: Belongs to the TOP6B family. {ECO:0000255|HAMAP-
CC       Rule:MF_00322}.
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DR   EMBL; AP006878; BAD84988.1; -; Genomic_DNA.
DR   RefSeq; WP_011249750.1; NC_006624.1.
DR   AlphaFoldDB; Q5JH81; -.
DR   SMR; Q5JH81; -.
DR   IntAct; Q5JH81; 1.
DR   MINT; Q5JH81; -.
DR   STRING; 69014.TK0799; -.
DR   PRIDE; Q5JH81; -.
DR   EnsemblBacteria; BAD84988; BAD84988; TK0799.
DR   GeneID; 3235675; -.
DR   KEGG; tko:TK0799; -.
DR   PATRIC; fig|69014.16.peg.779; -.
DR   eggNOG; arCOG01165; Archaea.
DR   HOGENOM; CLU_006403_0_0_2; -.
DR   InParanoid; Q5JH81; -.
DR   OMA; TRIELEM; -.
DR   OrthoDB; 13565at2157; -.
DR   PhylomeDB; Q5JH81; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd00823; TopoIIB_Trans; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00322; Top6B; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005734; TopoVI_B.
DR   InterPro; IPR015320; TopoVI_B_transducer.
DR   PANTHER; PTHR10871:SF4; PTHR10871:SF4; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF09239; Topo-VIb_trans; 1.
DR   PIRSF; PIRSF006553; TopoVI_B; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR01052; top6b; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Isomerase; Nucleotide-binding;
KW   Reference proteome; Topoisomerase.
FT   CHAIN           1..567
FT                   /note="Type 2 DNA topoisomerase 6 subunit B"
FT                   /id="PRO_0000145469"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         99..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         109..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         472
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
SQ   SEQUENCE   567 AA;  64233 MW;  BFA35FF582EC40FA CRC64;
     MAEANQLFKE FKIQSVSEFF RRNAAMLGYT GKVRSLTTLV HEAVTNSLDA CEEAGIPPYV
     RVEIEELGNE HYKVVVEDNG PGIPEKYITH VFGKMLAGTK AHRNIQSRGQ QGIGISGAVM
     FAQITSGKAT RVITSTGNDE IIEAWVKIDV DKNEGKIVKK EKHPNPKGWR GTRIELEVKN
     VKYMRSKQGV FWYLKLTAIA NPHAHIELIE PDGKLIVFPR SSDYIPEPPV EMKPHPKGVL
     TDDVYRLAKK TRRNTVRRFL IGEFSRISDK KVDELIEYIA ALRLIKTVED KKLQEQYYQK
     LMEGHVKAVL RAFKGYTKVV KQVAKMMEKP PEKLTWHEAE EIVEAFKYMK FLAPPTHGLR
     PIGEENIEKG LKGILKPEFV TAVTRPPKVY SGGIPFQVEV GIAYGGEIPA GFDLYRYANR
     VPLLFDAGSC VTTQAARSID WKRYKIDDLD RAPLVLMINV VSVHVPYTGT GKQSIASVDE
     IYNEIRLAIM DAARRLQTYL SGKHRKLAQV KRRKTFEKYV PEIARALSIL TGEPEEKIRE
     YFIRFIESKF ASAEVEEVAA EEVAENA