ID R4W6I0_9EURY Unreviewed; 821 AA.
AC R4W6I0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Type 2 DNA topoisomerase 6 subunit B {ECO:0000256|HAMAP-Rule:MF_00322};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00322};
DE AltName: Full=Type II DNA topoisomerase VI subunit B {ECO:0000256|HAMAP-Rule:MF_00322};
DE Short=TopoVI-B {ECO:0000256|HAMAP-Rule:MF_00322};
GN Name=top6B {ECO:0000256|HAMAP-Rule:MF_00322};
GN ORFNames=L593_02260 {ECO:0000313|EMBL:AGN00403.1};
OS Salinarchaeum sp. Harcht-Bsk1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Natronoarchaeaceae; Salinarchaeum.
OX NCBI_TaxID=1333523 {ECO:0000313|EMBL:AGN00403.1, ECO:0000313|Proteomes:UP000014072};
RN [1] {ECO:0000313|EMBL:AGN00403.1, ECO:0000313|Proteomes:UP000014072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Harcht-Bsk1 {ECO:0000313|EMBL:AGN00403.1};
RX PubMed=23868130;
RA Dominova I.N., Sorokin D.Y., Kublanov I.V., Patrushev M.V.,
RA Toshchakov S.V.;
RT "Complete Genome Sequence of Salinarchaeum sp. Strain HArcht-Bsk1T,
RT Isolated from Hypersaline Lake Baskunchak, Russia.";
RL Genome Announc. 1:E00505-13(2013).
CC -!- FUNCTION: Relaxes both positive and negative superturns and exhibits a
CC strong decatenase activity. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_00322};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two Top6A and two Top6B chains.
CC {ECO:0000256|HAMAP-Rule:MF_00322}.
CC -!- SIMILARITY: Belongs to the TOP6B family. {ECO:0000256|HAMAP-
CC Rule:MF_00322}.
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DR EMBL; CP005962; AGN00403.1; -; Genomic_DNA.
DR RefSeq; WP_020445297.1; NC_021313.1.
DR AlphaFoldDB; R4W6I0; -.
DR STRING; 1333523.L593_02260; -.
DR GeneID; 16180144; -.
DR KEGG; sali:L593_02260; -.
DR PATRIC; fig|1333523.5.peg.458; -.
DR eggNOG; arCOG01165; Archaea.
DR HOGENOM; CLU_006403_0_0_2; -.
DR OrthoDB; 65493at2157; -.
DR Proteomes; UP000014072; 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; 1.10.8.50; -; 1.
DR Gene3D; 2.60.40.2960; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 6.10.20.80; -; 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; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR040494; Top6b_C.
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; PF18000; Top6b_C; 1.
DR Pfam; PF09239; Topo-VIb_trans; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00322}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00322};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00322};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00322}; Reference proteome {ECO:0000313|Proteomes:UP000014072};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00322}.
FT DOMAIN 42..163
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT COILED 657..684
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00322"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00322"
FT BINDING 109..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00322"
FT BINDING 119..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00322"
FT BINDING 647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00322"
SQ SEQUENCE 821 AA; 90251 MW; 3F7EA674FB7602E2 CRC64;
MTSFQQTLGA EEGVAEELAE TQRAISIAEF FEKNKHMLGF DSGARGLVTA VKEAVDNALD
ATEEAGILPD IYVEIEEVGD YYRLTVEDNG PGITKEQLPK IFGKLLYGSR FHVREQNRGQ
QGIGISAAVL YSQLTSGKPA KITSRPKGAE RAQYFELIID TDENEPEIRA EEETTWDRPH
GTRIELEMEA NMRARQQLRN YIRATAVVNP HARLELREPG LDEPLKFERA TDELPAETDE
IRPHPHGVEL GTLLKMLQST DSHSVSGFLQ GEFTRVGKKT ADGIIDSFRD EHYGRELSWS
TPGAHEDADV RRAVQQAVSN KGKEATADFA DRIANVLEER ERVSYHALET IVDNAGDAVE
EEYPKAFGST VRQNAVEAVW GQVTGDAAAA DAEAADVDPD AETRRRADVY ALVNDATSDR
KDDATVEGLA RRIAEKLTNE TGERDRLTRD DLEDYVARSA DMTEKQDDDA SIGDTARENI
VEAIWEITRT VPDDPPKVRS LSDDRDAASA LLEGMRAVDV MAPPTSCLAP ITDELIEAGL
KKEYDADFYA ASTRDADVHG GDPFIVEAGI AYGGEIDEEG SVDVMRFANR VPLVYQRGAC
ATTDVVKSIG WRNYNLEQPG GSGIPNGPAV VMIHVASTNV PFTSESKDAV ANVPAIEDEI
ELAIREAARE LKSFLNKRQS MQQRKRKQNK LAEILPQMAT KVAEVTEQDE PMFDDALARI
MNNVLIEREV EENGDGTAVS VTVENNSDRS ESPKLTEIVT AEPRDVSGDA SVTEMDGEYF
LTWEPSVGGG ESATLAYETD ADAEYDLQVD GVEDAKLTVS E
//
