TOP6B_METMA
ID TOP6B_METMA Reviewed; 621 AA.
AC Q8PUB8;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=MM_2417;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) IN COMPLEX WITH TOP6A, AND SUBUNIT.
RX PubMed=17603498; DOI=10.1038/nsmb1264;
RA Corbett K.D., Benedetti P., Berger J.M.;
RT "Holoenzyme assembly and ATP-mediated conformational dynamics of
RT topoisomerase VI.";
RL Nat. Struct. Mol. Biol. 14:611-619(2007).
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, ECO:0000269|PubMed:17603498}.
CC -!- INTERACTION:
CC Q8PUB8; Q8PUB7: top6A; NbExp=2; IntAct=EBI-9026766, EBI-9026768;
CC -!- SIMILARITY: Belongs to the TOP6B family. {ECO:0000255|HAMAP-
CC Rule:MF_00322}.
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DR EMBL; AE008384; AAM32113.1; -; Genomic_DNA.
DR RefSeq; WP_011034341.1; NC_003901.1.
DR PDB; 2Q2E; X-ray; 4.00 A; B=1-621.
DR PDBsum; 2Q2E; -.
DR AlphaFoldDB; Q8PUB8; -.
DR SMR; Q8PUB8; -.
DR DIP; DIP-29415N; -.
DR IntAct; Q8PUB8; 1.
DR STRING; 192952.MM_2417; -.
DR EnsemblBacteria; AAM32113; AAM32113; MM_2417.
DR GeneID; 44087790; -.
DR GeneID; 66136078; -.
DR KEGG; mma:MM_2417; -.
DR PATRIC; fig|192952.21.peg.2765; -.
DR eggNOG; arCOG01165; Archaea.
DR HOGENOM; CLU_006403_0_0_2; -.
DR OMA; TRIELEM; -.
DR BRENDA; 5.6.2.2; 3270.
DR EvolutionaryTrace; Q8PUB8; -.
DR Proteomes; UP000000595; 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; IPR040494; Top6b_C.
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; PF18000; Top6b_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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA-binding; Isomerase; Nucleotide-binding;
KW Reference proteome; Topoisomerase.
FT CHAIN 1..621
FT /note="Type 2 DNA topoisomerase 6 subunit B"
FT /id="PRO_0000145463"
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 435
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
SQ SEQUENCE 621 AA; 68760 MW; 7D2FEC4F2FA68AD6 CRC64;
METPIAEELA KKQKSISVAE FFEKNRQILG FDSAPRSLIT TVKEAVDNAL DACEEAGILP
DILVQVERTG PDYVTVIIED NGPGIVREQI PKVFAKLLYG SRFHALKQSR GQQGIGISAA
VLYAQMTAGR HTKILSKTSP TAPAHYYELM INTSTNEPDI LVDEVRDWFR PHGTQIELEM
RAAYVKGRRQ SIYEYLKATA IVNPHARITL IDPDGNEEVF ERATDKMPEP AEEILPHPEG
IELGTLMKML HYTERQKLAP FLRYSFCKIG LLTAEEICKA AGLDPEIDPH ALGRHEARKL
IEAFEKVKIM APPTDCLSPI GEDLIYRGLE KETTVDFIAT STRKPAVYSG NPFVVEVGMA
YGGNLPKEEK ISIMRFANRV PLLYQQGGCV TTHAVEDIKW KQYGLNQPGG GIPVGPVILL
IHVASINVPF TSESKDAIAD IPVIKEEIDL AIKEVARKLK HYLSKQSNLK KRREKEIIIT
KVLPKLAAKV AHVLEKDVPD INPVVAKIMG NLLVHRVIKN NGDGTVDVAI KVKNFGTSAY
SFRVHEMLPC KVSGAKPEPK VVTMGNDYDY VWDISASAGS SKVLSYKIES ASEEELQKLP
QLIVEGIEEE LVTGAKAFKG V
