TOP6A_METBF
ID TOP6A_METBF Reviewed; 369 AA.
AC Q468I6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Type 2 DNA topoisomerase 6 subunit A {ECO:0000255|HAMAP-Rule:MF_00132};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00132};
DE AltName: Full=Type II DNA topoisomerase VI subunit A {ECO:0000255|HAMAP-Rule:MF_00132};
GN Name=top6A {ECO:0000255|HAMAP-Rule:MF_00132}; OrderedLocusNames=Mbar_A2806;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
CC -!- FUNCTION: Relaxes both positive and negative superturns and exhibits a
CC strong decatenase activity. {ECO:0000255|HAMAP-Rule:MF_00132}.
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_00132};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00132};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two Top6A and two Top6B chains.
CC {ECO:0000255|HAMAP-Rule:MF_00132}.
CC -!- SIMILARITY: Belongs to the TOP6A family. {ECO:0000255|HAMAP-
CC Rule:MF_00132}.
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DR EMBL; CP000099; AAZ71706.1; -; Genomic_DNA.
DR RefSeq; WP_011307747.1; NC_007355.1.
DR AlphaFoldDB; Q468I6; -.
DR SMR; Q468I6; -.
DR STRING; 269797.Mbar_A2806; -.
DR EnsemblBacteria; AAZ71706; AAZ71706; Mbar_A2806.
DR GeneID; 3625191; -.
DR KEGG; mba:Mbar_A2806; -.
DR eggNOG; arCOG04143; Archaea.
DR HOGENOM; CLU_037229_1_0_2; -.
DR OMA; NWGEARF; -.
DR OrthoDB; 22842at2157; -.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0000287; F:magnesium ion binding; 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; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_00132; Top6A; 1.
DR InterPro; IPR002815; Spo11/TopoVI_A.
DR InterPro; IPR013049; Spo11/TopoVI_A_N.
DR InterPro; IPR036078; Spo11/TopoVI_A_sf.
DR InterPro; IPR004085; TopoVI_A.
DR InterPro; IPR034136; TOPRIM_Topo6A/Spo11.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10848; PTHR10848; 1.
DR Pfam; PF04406; TP6A_N; 1.
DR PRINTS; PR01550; TOP6AFAMILY.
DR PRINTS; PR01552; TPISMRASE6A.
DR SUPFAM; SSF56726; SSF56726; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Topoisomerase.
FT CHAIN 1..369
FT /note="Type 2 DNA topoisomerase 6 subunit A"
FT /id="PRO_1000018315"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
SQ SEQUENCE 369 AA; 42204 MW; 0E1A5ACA782F229E CRC64;
MARKISNKKT QRDLLAREKL FELAEKIYNQ FENEVVPSIS LPSRTKSNLE YSNESDVWVY
GGRESERSAK TVKGAFQLLK TTYATEFLIN EHLAQSRGST LRELYYISEG WEAAKFKEQA
ESDRLIEDLE LLTNLQREYF HMRPEEDGAT MFGPIEITEQ TNRGERNIHC QKDVGEGGYQ
IPFNVENIEF KAHDASMIIA IETGGMYARL MENGFDEAYN AILVHLKGQP ARSTRRIIKR
MNEELGIPVA VFTDGDPWSY RIYASVAYGA IKSAHLSEFM ATPAAKFLGL QPSDIVEYEL
STDKLTEQDI NALRSELSDP RFESDYWKEQ IQLQLDIGKK AEQQAFAGKG LNFVTEVYLP
NRLKEMGML