TOP6B_HALS3
ID TOP6B_HALS3 Reviewed; 804 AA.
AC B0R4D3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=OE_2302R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(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}.
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DR EMBL; AM774415; CAP13598.1; -; Genomic_DNA.
DR RefSeq; WP_010902623.1; NC_010364.1.
DR AlphaFoldDB; B0R4D3; -.
DR SMR; B0R4D3; -.
DR EnsemblBacteria; CAP13598; CAP13598; OE_2302R.
DR GeneID; 5954364; -.
DR KEGG; hsl:OE_2302R; -.
DR HOGENOM; CLU_006403_0_0_2; -.
DR OMA; TRIELEM; -.
DR PhylomeDB; B0R4D3; -.
DR Proteomes; UP000001321; 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; 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; Topoisomerase.
FT CHAIN 1..804
FT /note="Type 2 DNA topoisomerase 6 subunit B"
FT /id="PRO_1000116020"
FT BINDING 58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT BINDING 110..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT BINDING 120..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT BINDING 629
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
SQ SEQUENCE 804 AA; 85871 MW; 3C265ED69E764B23 CRC64;
MTSFQSTLDD DEDGIAEELA ASQREISVAE FFEKNKHMLG FDSGARGLVT AVKEAVDNAL
DATEEAGILP DIYVEISEGR DYYTLIVEDN GPGITNAQIP KIFGKLLYGS RFHAREQSRG
QQGIGISAAV LYSQLTSGKP VRIESRTQDS ETANVYELII DTDTNEPEIS AETEVSAAKS
DLRGTHGTRI EMALDANMRA RGQLHDYIKH TAVVNPHARI ELQEPGGELK SERAEEASLP
AETDEILPHP HGVELGTLIK MLAETDSHSV SGFLQSEFTR VGSKTATGII DAFRDEHFGR
EMRWRPPADA DLEATVADAV ANKDATHTAV FARTVADAVR DADSIAPAEL GALVADAAAD
AQDDTGTSFG ETVQANVVAA VRDALTSDRV ADVLGPVDEA TTVQKDDATV RGLAERIAAK
FESGGDTDRV TRDTLDEYVF RAAENTAEYA DATIGETARE NVADALWARM ATVPDDPPNT
SALADDRDAA SDLLAAMASV NVMAPPTSCL SPIEADQLEA GLRTEFDADF YAAATRDADV
HGGDPFIVEA GIAYGGDIDS EGGVQLMRFA NRVPLVYQRG ACATTDVLGD IGWRNYNLSQ
PGGSGLPQGP AVIMVHVAST NVPFTSESKD AIANVPEIEA EIELAVREAA RELKSFLQKR
QSMRKRQQKQ DVIMDILPTM AEKVGELTGR GGVDVSDSLA RIMNNVLVER ARSDDGQTVT
LRVENHGTGS VDVDVTDIVS AEPDGVGDDA SVVAMDDEYF VKWTPAVAGD DAAELTYSVD
ADADCELSVS GVADARLTVS EADT