ID   TOP6B_METS5             Reviewed;         531 AA.
AC   A4YHK7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=Msed_1754;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
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}.
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; CP000682; ABP95909.1; -; Genomic_DNA.
DR   RefSeq; WP_012021696.1; NC_009440.1.
DR   AlphaFoldDB; A4YHK7; -.
DR   SMR; A4YHK7; -.
DR   STRING; 399549.Msed_1754; -.
DR   EnsemblBacteria; ABP95909; ABP95909; Msed_1754.
DR   GeneID; 5104754; -.
DR   GeneID; 59457128; -.
DR   KEGG; mse:Msed_1754; -.
DR   eggNOG; arCOG01165; Archaea.
DR   HOGENOM; CLU_006403_0_0_2; -.
DR   OMA; TRIELEM; -.
DR   Proteomes; UP000000242; 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..531
FT                   /note="Type 2 DNA topoisomerase 6 subunit B"
FT                   /id="PRO_1000205141"
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   531 AA;  60766 MW;  63FEC08E4664356C CRC64;
     MSAKEKFTSI SPAEFFKRNP ELAGFSNPAR AMYQALRELV ENALDATDVH EILPSIKVII
     ERTSQEKEIY RLTVEDNGIG IPPHVVPDAF GRVLYSSKYV LRQTRGMYGL GVKAAVLYSQ
     MYQDKPIEIT TAPLNSKRIY SFKLKIDVTK NEPIIYERGS VNNDTGYHGT SVSMYILGDW
     MRAKSRVYEY IKRTYIITPY AEFYFKDPEG NVVLYPRLTN KMPVPPKEVK PHPYGVDIEL
     LKNMISRQKE DTTVKEFLVK EFQSVGEKTA LSVIEMAGLD PDKRVQKLTD DQLSKLVDAM
     KNFPDFRPPS PEALSTIGAD LIELGLKQTF NPEYVGAVTR RPKAYQGHPF IVEVGLAYGG
     DIQPSEEPTV LRYANKIPLI YDEKSDVVWK VVEEIDWKRY GIEDEQLPLV VMVHLCSTKV
     PYKSAGKESI ADVEEIEKEI RNGIMEASRS LKTFMTEKRK EEEARKRLLT YLKYIPELAR
     SLSIFVTDGK KELAPKVQEE IQNKMIDLVV TKLNIKDKDL ELFKSYRVET L