ID   TOP6B_METBF             Reviewed;         621 AA.
AC   Q468I5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, 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=Mbar_A2807;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ71707.1; -; Genomic_DNA.
DR   RefSeq; WP_011307748.1; NC_007355.1.
DR   AlphaFoldDB; Q468I5; -.
DR   SMR; Q468I5; -.
DR   STRING; 269797.Mbar_A2807; -.
DR   EnsemblBacteria; AAZ71707; AAZ71707; Mbar_A2807.
DR   GeneID; 3625192; -.
DR   KEGG; mba:Mbar_A2807; -.
DR   eggNOG; arCOG01165; Archaea.
DR   HOGENOM; CLU_006403_0_0_2; -.
DR   OMA; TRIELEM; -.
DR   OrthoDB; 13565at2157; -.
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; IPR040494; Top6b_C.
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; 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; 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; Topoisomerase.
FT   CHAIN           1..621
FT                   /note="Type 2 DNA topoisomerase 6 subunit B"
FT                   /id="PRO_1000005870"
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   621 AA;  68754 MW;  F63CEDF7AAE4C57F CRC64;
     MEFTIAEELA KNQKSISVAE FFEKNRQILG FDSAPRSLIT TVKEAVDNAL DACEEAGILP
     DILVQIERTG QDYVTVIIED NGPGIIKEQI PKVFAKLLYG SRFHALKQSR GQQGIGISAA
     VLYAQMTAGK QTKILSKTGS GNPAHYYELM INTSTNEPDI LKDEIRDWFR PHGTQIELEM
     KAAYVKGRRQ SISEYLKATA IVNPHARITL IEPDGNEEVF ERATDKMPKP AEEILPHPEG
     IELGTLMKML HYTERQKLAP FLRYSFCKIG LLTAEEICKA SGLDPEIDPH ALGRHEARKL
     IEAFEKVKIM SPPTDCLSPI GEELIYRGLE KETNVDFIAT STRKPAVYSG NPFVVEVGLA
     YGGKLPKEEK ISIMRFANRV PLLYQQGGCV TTHAVEDIKW KQYGLNQPGG GVPVGPAILL
     IHVASINVPF TSESKDAIAD IPVIKDEIDL AIKDVARKLK HYLSKQSNLK KRREKEIIIT
     KVLPKMAVKV ANILEKDVPD INPVVAKIMG NLLVHRKVKR NEDGTADVVI KVKNFGTSAY
     AFKVHEMLPC TILGAKPEPK VVTLGNDYDY VWDISAAAGS SKVLSYRIES TTDKELGTFP
     DLVVEGLEEE LVTGAKAFKG V