ID TOP6B_SULIM Reviewed; 530 AA.
AC C3MYN1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
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=M1425_1255;
OS Sulfolobus islandicus (strain M.14.25 / Kamchatka #1).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=427317;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.14.25 / Kamchatka #1;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(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}.
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DR EMBL; CP001400; ACP38010.1; -; Genomic_DNA.
DR RefSeq; WP_012711263.1; NC_012588.1.
DR AlphaFoldDB; C3MYN1; -.
DR SMR; C3MYN1; -.
DR GeneID; 8761184; -.
DR KEGG; sia:M1425_1255; -.
DR HOGENOM; CLU_006403_0_0_2; -.
DR Proteomes; UP000001350; 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; 3.30.230.10; -; 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; 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; PF05833; NFACT_N; 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..530
FT /note="Type 2 DNA topoisomerase 6 subunit B"
FT /id="PRO_1000205145"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT BINDING 97..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT BINDING 106..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT BINDING 427
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
SQ SEQUENCE 530 AA; 60563 MW; A89C3767142BF421 CRC64;
MSAKEKFTSL SPAEFFKRNP ELAGFPNPAR ALYQTVRELI ENSLDATDVH GILPNIKITI
DLIDEARQIY KVNVVDNGIG IPPQEVPNAF GRVLYSSKYV NRQTRGMYGL GVKAAVLYSQ
MHQDKPIEIE TSPANSKRIY TFKLKIDINK NEPIIVERGS VENTRGFHGT SVAISIPGDW
PKAKSRIYEY IKRTYIITPY AEFIFKDPEG NVTYYPRLTN KIPKPPQEVK PHPYGVDREE
IKILINNLKR DYTIKEFLVN EFQSIGDTTA DKILELAGLK PNKKVKNLTE EEITRLVETF
KKYEDFRSPS ADSLSVIGED LIELGLKKIF NPDFAASITR KPKAYQGHPF IVEAGVAFGG
SIPVGEEPIV LRYANKIPLI YDEKSDVIWK VVEELDWKRY GIESDQYQMV VMVHLCSTKI
PYKSAGKESI AEVEDIEKEI KNALMEVARK LKQYLSEKRK EQEAKKKLLA YLKYIPEVSR
SLATFLASGN KELVSKYQNE ISEGLFKLIS KKLDLINIEE YRKVYRVDSE
//
