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 04-MAR-2015, entry version 60. DE RecName: Full=Type 2 DNA topoisomerase 6 subunit B {ECO:0000255|HAMAP-Rule:MF_00322}; DE EC=5.99.1.3 {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=Mbur_1203; OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / OS ACE-M). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC 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., RA Ting L., Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., RA Ivanova N., Dalin E., Martinez M., Lapidus A., Hauser L., Land M., RA Thomas T., 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 CC exhibits a strong decatenase activity. {ECO:0000255|HAMAP- CC Rule:MF_00322}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_00322}. CC -!- SUBUNIT: Homodimer. Heterotetramer of two Top6A and two Top6B CC chains. {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 RefSeq; YP_565876.1; NC_007955.1. DR ProteinModelPortal; Q12WQ0; -. DR SMR; Q12WQ0; 11-606. DR STRING; 259564.Mbur_1203; -. DR PRIDE; Q12WQ0; -. DR EnsemblBacteria; ABE52126; ABE52126; Mbur_1203. DR GeneID; 3998359; -. DR KEGG; mbu:Mbur_1203; -. DR eggNOG; COG1389; -. DR HOGENOM; HOG000225919; -. DR KO; K03167; -. DR OMA; LLRYANK; -. DR BioCyc; MBUR259564:GHBZ-1226-MONOMER; -. DR Proteomes; UP000001979; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-HAMAP. 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; 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 Pfam; PF02518; HATPase_c; 1. DR Pfam; PF09239; Topo-VIb_trans; 1. DR PIRSF; PIRSF006553; TopoVI_B; 1. DR ProDom; PD013790; TopoVI_B_transducer; 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; Complete proteome; DNA-binding; Isomerase; KW Nucleotide-binding; Reference proteome; Topoisomerase. FT CHAIN 1 622 Type 2 DNA topoisomerase 6 subunit B. FT /FTId=PRO_1000005871. FT NP_BIND 101 102 ATP. {ECO:0000255|HAMAP-Rule:MF_00322}. FT NP_BIND 111 118 ATP. {ECO:0000255|HAMAP-Rule:MF_00322}. FT BINDING 48 48 ATP. {ECO:0000255|HAMAP-Rule:MF_00322}. FT BINDING 80 80 ATP. {ECO:0000255|HAMAP-Rule:MF_00322}. FT BINDING 435 435 ATP. {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 //