TOP6B_METTH
ID TOP6B_METTH Reviewed; 523 AA.
AC O27088;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=MTH_1007;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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; AE000666; AAB85503.1; -; Genomic_DNA.
DR PIR; C69001; C69001.
DR RefSeq; WP_010876638.1; NC_000916.1.
DR AlphaFoldDB; O27088; -.
DR SMR; O27088; -.
DR STRING; 187420.MTH_1007; -.
DR EnsemblBacteria; AAB85503; AAB85503; MTH_1007.
DR GeneID; 1471415; -.
DR KEGG; mth:MTH_1007; -.
DR PATRIC; fig|187420.15.peg.990; -.
DR HOGENOM; CLU_006403_0_0_2; -.
DR OMA; TRIELEM; -.
DR Proteomes; UP000005223; 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; IPR010979; Ribosomal_S13-like_H2TH.
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; SSF46946; SSF46946; 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..523
FT /note="Type 2 DNA topoisomerase 6 subunit B"
FT /id="PRO_0000145464"
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 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT BINDING 436
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
SQ SEQUENCE 523 AA; 58858 MW; C2E1AF324AD58296 CRC64;
MARQALDLFD EGFQELTPSE FFRKNKQMLG FTGKIRSLTI VFHELITNSF DAAEEAGILP
EIKIDLKRIG KDHYILRHQD NGPGIPEKYI PKVFCTMFAG SKFRNIQSRG QQGLGCSGCV
LLSQMTTGKP VKVISGTMEN GELKGVKMTL KMDVKKNQGL ILEKEEVEVD GTGVCIELHF
KDVSYSLSEQ GAYEYIRRTM IANPHARIVF NDPTGNRYVF NRASDVIPPM PKEVLPHPWG
VTADDLIFMA KHTDKRRFGS MLKSNLSRMS SMKIKELEEL TGIDLNKRPK DMKWEEAEQI
VEAFKKMKFM SPPTSGLIPI GEEQIDKGMK EILQPEFTAT VTRKPKTYRG GIAFIVEAGI
AYGGNSGRLV GDQRKAEIMR FANRVPLTFD AGSCAITEGV KSLDWKRYGI RDLENAPISI
FVNVVSTNVP YLSTGKQSVS PEPEILGEIR QATMIVARKL HKYLRKKKAA KEEAQRAKIF
ESYVPVIIKQ AALLAEREEP DYRELLDTVT RRAKLEILGG ITE