ID   TOP6B_SACI2             Reviewed;         530 AA.
AC   C3MPN7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   10-JUN-2026, entry version 88.
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};
GN   OrderedLocusNames=LS215_1342;
OS   Saccharolobus islandicus (strain L.S.2.15 / Lassen #1) (Sulfolobus
OS   islandicus).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=429572;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L.S.2.15 / Lassen #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001399; ACP35350.1; -; Genomic_DNA.
DR   RefSeq; WP_012711263.1; NC_012589.1.
DR   AlphaFoldDB; C3MPN7; -.
DR   SMR; C3MPN7; -.
DR   GeneID; 15297612; -.
DR   KEGG; sis:LS215_1342; -.
DR   HOGENOM; CLU_006403_0_0_2; -.
DR   OrthoDB; 65493at2157; -.
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:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   CDD; cd16933; HATPase_TopVIB-like; 1.
DR   CDD; cd00823; TopoIIB_Trans; 1.
DR   FunFam; 1.10.8.50:FF:000014; Type 2 DNA topoisomerase 6 subunit B; 1.
DR   FunFam; 3.30.230.10:FF:000091; Type 2 DNA topoisomerase 6 subunit B; 1.
DR   FunFam; 3.30.565.10:FF:000062; Type 2 DNA topoisomerase 6 subunit B; 1.
DR   Gene3D; 1.10.8.50; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   HAMAP; MF_00322; Top6B; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR003594; HATPase_dom.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR005734; TopoVI_B.
DR   InterPro; IPR015320; TopoVI_B_transducer.
DR   NCBIfam; NF003218; PRK04184.1; 1.
DR   NCBIfam; TIGR01052; top6b; 1.
DR   PANTHER; PTHR48444; DNA TOPOISOMERASE 6 SUBUNIT B; 1.
DR   PANTHER; PTHR48444:SF1; DNA TOPOISOMERASE 6 SUBUNIT B; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF05833; NFACT_N; 1.
DR   Pfam; PF09239; Topo-VIb_trans; 1.
DR   PIRSF; PIRSF006553; TopoVI_B; 1.
DR   SMART; SM00387; HATPase_c; 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; SSF46946; S13-like H2TH domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Isomerase; Nucleotide-binding; Topoisomerase.
FT   CHAIN           1..530
FT                   /note="Type 2 DNA topoisomerase 6 subunit B"
FT                   /id="PRO_1000205144"
FT   BINDING         42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         76
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         97..98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         106..113
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   530 AA;  60563 MW;  A89C3767142BF421 CRC64;
     MSAKEKFTSL SPAEFFKRNP ELAGFPNPAR ALYQTVRELI ENSLDATDVH GILPNIKITI
     DLIDEARQIY KVNVVDNGIG IPPQEVPNAF GRVLYSSKYV NRQTRGMYGL GVKAAVLYSQ
     MHQDKPIEIE TSPANSKRIY TFKLKIDINK NEPIIVERGS VENTRGFHGT SVAISIPGDW
     PKAKSRIYEY IKRTYIITPY AEFIFKDPEG NVTYYPRLTN KIPKPPQEVK PHPYGVDREE
     IKILINNLKR DYTIKEFLVN EFQSIGDTTA DKILELAGLK PNKKVKNLTE EEITRLVETF
     KKYEDFRSPS ADSLSVIGED LIELGLKKIF NPDFAASITR KPKAYQGHPF IVEAGVAFGG
     SIPVGEEPIV LRYANKIPLI YDEKSDVIWK VVEELDWKRY GIESDQYQMV VMVHLCSTKI
     PYKSAGKESI AEVEDIEKEI KNALMEVARK LKQYLSEKRK EQEAKKKLLA YLKYIPEVSR
     SLATFLASGN KELVSKYQNE ISEGLFKLIS KKLDLINIEE YRKVYRVDSE
//