TOP6B_PYRAB
ID TOP6B_PYRAB Reviewed; 564 AA.
AC Q9V135; G8ZJ59;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=PYRAB05940;
GN ORFNames=PAB0407;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248284; CAB49516.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69986.1; -; Genomic_DNA.
DR PIR; E75179; E75179.
DR RefSeq; WP_010867718.1; NC_000868.1.
DR AlphaFoldDB; Q9V135; -.
DR SMR; Q9V135; -.
DR IntAct; Q9V135; 1.
DR MINT; Q9V135; -.
DR STRING; 272844.PAB0407; -.
DR EnsemblBacteria; CAB49516; CAB49516; PAB0407.
DR GeneID; 1495499; -.
DR KEGG; pab:PAB0407; -.
DR PATRIC; fig|272844.11.peg.632; -.
DR eggNOG; arCOG01165; Archaea.
DR HOGENOM; CLU_006403_0_0_2; -.
DR OMA; TRIELEM; -.
DR OrthoDB; 13565at2157; -.
DR PhylomeDB; Q9V135; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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; Topoisomerase.
FT CHAIN 1..564
FT /note="Type 2 DNA topoisomerase 6 subunit B"
FT /id="PRO_0000145465"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT BINDING 78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT BINDING 99..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT BINDING 471
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
SQ SEQUENCE 564 AA; 63797 MW; 267C0D89DD4C1F22 CRC64;
MAEARDLFKE FKVQSVSEFF RRNAAMLGYT GKIRSLTTII HEAVTNSLDA CEEAGILPYI
RVEIEELGKE HYKVIVEDNG PGIPEEYIPH VFGKMLAGTK AHRNIQSRGQ QGIGISGAVM
FAQITSGKAT RVITSTGGEI VEAWVKIDVQ KNEGKIVKKL KHPNPKGWRG TRIELEVKDV
KYVRSKQGVY WYLKLTAIAN PHAHIELVEP DGKLVVFPRS SEDIPEPPVE MKPHPKGVMV
DDVYTMAHRS KRSSVRRFLV SEFSRISDKK VDELIKYITA LRLIKSETNK EVKEKLYEKL
VSGDVDSVLR AFGRKWKKEL EKVAKIMDKS PEKLTWHEAE EIVEAFKLMK FLAPPTHGLR
PIGEENIKKG LTSILKPEFV TAVTRAPRVY AGGIPFQVEV GLAYGGQIQG SEILRYANRV
PLLFDAGSCV ITSAVRSIDW KRYKIDSFDS APLVVLVNVV SVHVPYTSTG KQSIADIDEI
HNEIRLALMD AARRLSFYLG GKFRRMYQVK RRKTLEKYLP EIARSLHILT GEPEEKIKEY
FLKLIESKIE VEEVSEVEAE EAEA
