ID   TOP6B_SULTO             Reviewed;         532 AA.
AC   Q971T2;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=STK_12940;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
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; BA000023; BAB66338.1; -; Genomic_DNA.
DR   RefSeq; WP_010979316.1; NC_003106.2.
DR   AlphaFoldDB; Q971T2; -.
DR   SMR; Q971T2; -.
DR   STRING; 273063.STK_12940; -.
DR   EnsemblBacteria; BAB66338; BAB66338; STK_12940.
DR   GeneID; 1459296; -.
DR   KEGG; sto:STK_12940; -.
DR   PATRIC; fig|273063.9.peg.1455; -.
DR   eggNOG; arCOG01165; Archaea.
DR   OMA; TRIELEM; -.
DR   OrthoDB; 13565at2157; -.
DR   Proteomes; UP000001015; Chromosome.
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; IPR010979; Ribosomal_S13-like_H2TH.
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; SSF46946; SSF46946; 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..532
FT                   /note="Type 2 DNA topoisomerase 6 subunit B"
FT                   /id="PRO_0000145472"
FT   BINDING         41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         96..97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         105..112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         427
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
SQ   SEQUENCE   532 AA;  61204 MW;  17965DCF1CAC27AF CRC64;
     MSSEKFTSIS PAEFFKRNPE LAGFSNPARA LYQTVRELVE NALDATDVHN ILPSIKIIIE
     LVDPQKQIYK VNVEDNGIGI PPHIVPNAFG KVLYSSKYVL RQTRGMYGLG VKAAVLYSQM
     YQERPVEVVT SPINSKRIYF FKLKIDVVKN EPIILQKTSV VNEKNWHGTS VTLYLYADWQ
     RAKQKIYEYV KKTYIISPYA EFFFKDPDNN VIYYKRLTDK IPEPPKEVKP HPYGVDIELI
     KFMIVKKDKP VPVRDFLINE FQSIGDVTAD KILEMAKLPK DKKTTELTDE EISRLVEVMK
     KFDDFRPPSA EALSVIGEDL IKLGLKSIFN PEFAEAITRK PKAYQGHPFI VEAGIAYGGA
     IQPSPEPIVL RYANKIPLIY DEKSDVIWKV VTEEMDWKRY GIEEEQPPLV VMVHLCSTKV
     PYRSAGKESI ADVEEIEKEI KLALMDVARK LKKYITEKRK EEEAKKRLIT YLKYIPEVSR
     GLALFLVGGD KQKIGDAYSD LREKLLKIAL NKLEVNDKKL EEEIRNYKVE EL