ID TOP6B_METBU Reviewed; 622 AA. AC Q12WQ0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 24-JUL-2024, entry version 100. 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=Mbur_1203; OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / OS ACE-M). OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanosarcinales; Methanosarcinaceae; Methanococcoides. OX NCBI_TaxID=259564; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M; RX PubMed=19404327; DOI=10.1038/ismej.2009.45; RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S., RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L., RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N., RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T., RA Cavicchioli R.; RT "The genome sequence of the psychrophilic archaeon, Methanococcoides RT burtonii: the role of genome evolution in cold adaptation."; RL ISME J. 3:1012-1035(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}. 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; CP000300; ABE52126.1; -; Genomic_DNA. DR RefSeq; WP_011499272.1; NC_007955.1. DR AlphaFoldDB; Q12WQ0; -. DR SMR; Q12WQ0; -. DR STRING; 259564.Mbur_1203; -. DR GeneID; 3998359; -. DR KEGG; mbu:Mbur_1203; -. DR HOGENOM; CLU_006403_0_0_2; -. DR OrthoDB; 65493at2157; -. DR Proteomes; UP000001979; 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; cd16933; HATPase_TopVIB-like; 1. DR CDD; cd00823; TopoIIB_Trans; 1. DR Gene3D; 1.10.8.50; -; 1. DR Gene3D; 2.60.40.2960; -; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 6.10.20.80; -; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR HAMAP; MF_00322; Top6B; 1. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR036890; HATPase_C_sf. 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; IPR050761; TOP6B. DR InterPro; IPR040494; Top6b_C. DR InterPro; IPR005734; TopoVI_B. DR InterPro; IPR015320; TopoVI_B_transducer. DR NCBIfam; TIGR01052; top6b; 1. DR PANTHER; PTHR48356; DNA TOPOISOMERASE 6 SUBUNIT B; 1. DR PANTHER; PTHR48356:SF1; DNA TOPOISOMERASE 6 SUBUNIT B; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF18000; Top6b_C; 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..622 FT /note="Type 2 DNA topoisomerase 6 subunit B" FT /id="PRO_1000005871" FT BINDING 48 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322" FT BINDING 80 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322" FT BINDING 101..102 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322" FT BINDING 111..118 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322" FT BINDING 435 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322" SQ SEQUENCE 622 AA; 68876 MW; 701F62BAE803127A CRC64; MAAPIAEELA KKQQAISVAE FFEKNRQILG FDSAPRSLIT TVKEAVDNSL DACEEAEILP DILLHIERVG KDNVSVIVED NGPGIVKEQI PKVFAKLLYG SRFHALKQSR GQQGIGISAS VLYAQLTAGH PTSVISKIGP DSPAHHYEVM INTSTNDPEI LLDEVIDWDR PHGTRVELEM EASYVKGRRQ SIYEYLKATA IVNPHARLTL IEPDGNEVIF DRATDKLPIP AKEILPHPHG IELGTLMKML RYTDRQKLAP FLRYSFSKIG LLTAEEICKA AGLDTEMLPS KLTRDQTKKL LDAFKKVKIM APPTDCLSPI GEELIYKGLE KEFNVDFIAT TTRSPSVFSG NPFVVEVGIA YGGVLQKDDR IDIMRFANRV PLLYQQGGCA TTHAVEGIKW KQYGLNQPGG GMPTGPVVLL VHVASTNVPF TSESKDAIAD IPEIRDEVEL AIKEVSRKLN RYLNRQVSLK KRREKEIIIT KVLPKMAQKL ADTLERDLPD INPVVAKVMG NLLVMRHVEH GANGDAAVTI KVKNFGSKLT EFKLHDMLPY EISDVSPEPK VISMGSDFDY VWTMKVSPEG SKAVTYSLSS MSEDEIKRLP QLIVEGLDEE LVTGAKAIKG LI //