ID   TOP6B_HALMA             Reviewed;         796 AA.
AC   Q5V4R5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=rrnAC0457;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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; AY596297; AAV45487.1; -; Genomic_DNA.
DR   RefSeq; WP_011223034.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V4R5; -.
DR   SMR; Q5V4R5; -.
DR   STRING; 272569.rrnAC0457; -.
DR   PRIDE; Q5V4R5; -.
DR   EnsemblBacteria; AAV45487; AAV45487; rrnAC0457.
DR   GeneID; 40154725; -.
DR   KEGG; hma:rrnAC0457; -.
DR   PATRIC; fig|272569.17.peg.1230; -.
DR   eggNOG; arCOG01165; Archaea.
DR   HOGENOM; CLU_006403_0_0_2; -.
DR   OMA; TRIELEM; -.
DR   Proteomes; UP000001169; Chromosome I.
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; 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   SMART; SM00387; HATPase_c; 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..796
FT                   /note="Type 2 DNA topoisomerase 6 subunit B"
FT                   /id="PRO_1000005869"
FT   BINDING         57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         109..110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         119..126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
SQ   SEQUENCE   796 AA;  87759 MW;  DC4FC12432E15C99 CRC64;
     MTSYQSQLGE GEGIAEELAE SQRAISIAEF FEKNKHMLGF DSEARALVTA VKEAVDNALD
     ACEEAGILPD IYVEIQESGD YYKLVVEDNG PGITKEQAPK IFGKLLYGSR FHAREQNRGQ
     QGIGISAAVL YSQLTSGKPA KITSRPKGQD EAQYFELIVD TDTNEPEISV DETTTWERPH
     GTRIELEMEA NMRARSTLRD YIQDTAVVNP HARVEFDEPG LDESLKFERA ERAELPDETE
     EIRPHPHGVE LGTLLKMLEA TDSYSVSGFM QEEFTRVGGK TADSVIANFN DRHYGRGMAW
     QPPKVNEDAD IERAVEDAVA NKGAETTATF AAAVSDAIHD RDRVAYHEVE SIVDSAAEDA
     EADGDTTFGA TVRENAVDAA WNAVSDNLSS DLYALVDDVT TKRKDDAAVE GLASRLADKF
     DDDGRHRLTR DELRGYIDRA ADMTEEQDDA TFGETARENV LEALWTAAEG VREEPPKVSD
     IADDRDTASQ LLSAMRETDI IAPPTDCLSP ISAELVEEGL RKEFDADFYA ASTRDASVHG
     GDPFIVEAGI AYGGELESEG TVDVMRFANR VPLVYQRGAC ATTDVVKSIR WRNYNLDQPG
     GSGIPKGPAV IMVHVASTNV PFTSESKDAI ANVPEMEDEI ELAIREAARE LKSYLNKRRS
     MQQRREKQDK LATILPEMAE KLTEVTDNDE LHIDDSLARI MNNVLVEREV EDDTVRVRIE
     NNDDTNADVE LTDIVTAEPQ VTNGATVVEM DGEWFVKWSP TVGAGETAVL EYSVTDEAEF
     TVSVDGIEEE KLTVNA