TOP6B_THESM
ID TOP6B_THESM Reviewed; 566 AA.
AC C6A3G4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=TSIB_1105;
OS Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=604354;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12597 / MM 739;
RX PubMed=19447963; DOI=10.1128/aem.00718-09;
RA Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT analysis.";
RL Appl. Environ. Microbiol. 75:4580-4588(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; CP001463; ACS90159.1; -; Genomic_DNA.
DR RefSeq; WP_015849378.1; NC_012883.1.
DR AlphaFoldDB; C6A3G4; -.
DR SMR; C6A3G4; -.
DR STRING; 604354.TSIB_1105; -.
DR EnsemblBacteria; ACS90159; ACS90159; TSIB_1105.
DR GeneID; 8096103; -.
DR KEGG; tsi:TSIB_1105; -.
DR eggNOG; arCOG01165; Archaea.
DR HOGENOM; CLU_006403_0_0_2; -.
DR OMA; TRIELEM; -.
DR OrthoDB; 13565at2157; -.
DR Proteomes; UP000009079; 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; IPR005734; TopoVI_B.
DR InterPro; IPR015320; TopoVI_B_transducer.
DR PANTHER; PTHR10871:SF4; PTHR10871:SF4; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF09239; Topo-VIb_trans; 1.
DR PIRSF; PIRSF006553; TopoVI_B; 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..566
FT /note="Type 2 DNA topoisomerase 6 subunit B"
FT /id="PRO_1000205149"
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 475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
SQ SEQUENCE 566 AA; 64051 MW; 50007D4B9550E357 CRC64;
MANSEADKLF KEFKIQSVSE FFRRNAAMLG YTGKLRSLTT LIHEAVTNSL DACEEAGILP
YVRVEIEELG TEHYKIIVED NGPGIPEKFI AHVFGKMLAG TKAHRNIQSR GQQGIGISGA
VMFAQITSGK ATRIITSTGE EEIIEAWVGI DVDKNEGKIF KKIKHPNPTG WRGTRIEMEV
KDVRYIRSKQ GVYWYLKLTA IANPHAHIEF IEPDGKLIVF SRSSEELPEP PEEMKPHPKG
IITDDIYRMA QRTTRTTVRT FLIGEFSRIS DKKIDELVQY ITALRLIKEE EEQNVKEQLM
KRLVDGEVDK IIASFGKRGK KVLREVRKIM EKPPKKLTWH EAEEIVEAFK YMTFLAPPTH
GLRPIGEENI EKGLTGILRP EFVTSVTRPP KVYRGGIPFQ VEVGLAFGGE LSSGFDLLRY
ANRVPLLFDA GSCVITSAAR NIDWKRYRVD DVDRAPLALL VNVVSVHVPY TSTGKQSVAN
EEEIYEEIRL AVMDVARRLA KYLGGKHRKL YQVKRRKTLE KYVPEVSRAL SILTGLPEGE
IKKMLVTIIE KKFESIDEAV EAESDA
