TOP6A_METJA
ID TOP6A_METJA Reviewed; 369 AA.
AC Q57815;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
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, ECO:0000269|PubMed:10545127};
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=MJ0369;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP PROTEIN SEQUENCE OF 1-69, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 69-369
RP IN COMPLEX WITH MAGNESIUM IONS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBUNIT, AND MUTAGENESIS OF GLU-197.
RX PubMed=10545127; DOI=10.1093/emboj/18.21.6177;
RA Nichols M.D., DeAngelis K., Keck J.L., Berger J.M.;
RT "Structure and function of an archaeal topoisomerase VI subunit with
RT homology to the meiotic recombination factor Spo11.";
RL EMBO J. 18:6177-6188(1999).
CC -!- FUNCTION: Relaxes both positive and negative superturns and exhibits a
CC strong decatenase activity. {ECO:0000255|HAMAP-Rule:MF_00132,
CC ECO:0000269|PubMed:10545127}.
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-Rule:MF_00132,
CC ECO:0000269|PubMed:10545127};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00132,
CC ECO:0000269|PubMed:10545127};
CC Note=Mg(2+) is directly coordinated by Glu-197 and Asp-249 as well as
CC indirectly coordinated through 2 water molecules by Asp-251
CC (PubMed:10545127). {ECO:0000269|PubMed:10545127};
CC -!- SUBUNIT: Homodimer (PubMed:10545127). Heterotetramer of two Top6A and
CC two Top6B chains. {ECO:0000255|HAMAP-Rule:MF_00132,
CC ECO:0000269|PubMed:10545127}.
CC -!- SIMILARITY: Belongs to the TOP6A family. {ECO:0000255|HAMAP-
CC Rule:MF_00132}.
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DR EMBL; L77117; AAB98358.1; -; Genomic_DNA.
DR PIR; A64346; A64346.
DR RefSeq; WP_010869868.1; NC_000909.1.
DR PDB; 1D3Y; X-ray; 2.00 A; A/B=69-369.
DR PDBsum; 1D3Y; -.
DR AlphaFoldDB; Q57815; -.
DR SMR; Q57815; -.
DR STRING; 243232.MJ_0369; -.
DR EnsemblBacteria; AAB98358; AAB98358; MJ_0369.
DR GeneID; 1451226; -.
DR KEGG; mja:MJ_0369; -.
DR eggNOG; arCOG04143; Archaea.
DR HOGENOM; CLU_037229_1_0_2; -.
DR InParanoid; Q57815; -.
DR OMA; NWGEARF; -.
DR OrthoDB; 22842at2157; -.
DR PhylomeDB; Q57815; -.
DR EvolutionaryTrace; Q57815; -.
DR Proteomes; UP000000805; Chromosome.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; DNA-binding;
KW Isomerase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Topoisomerase.
FT CHAIN 1..369
FT /note="Type 2 DNA topoisomerase 6 subunit A"
FT /id="PRO_0000145449"
FT ACT_SITE 103
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9M4A2"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:10545127"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:10545127"
FT MUTAGEN 197
FT /note="E->A: Reduces affinity for DNA."
FT /evidence="ECO:0000269|PubMed:10545127"
FT HELIX 73..91
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1D3Y"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1D3Y"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:1D3Y"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:1D3Y"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:1D3Y"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1D3Y"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:1D3Y"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:1D3Y"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:1D3Y"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 303..315
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 323..335
FT /evidence="ECO:0007829|PDB:1D3Y"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 341..347
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 356..362
FT /evidence="ECO:0007829|PDB:1D3Y"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:1D3Y"
SQ SEQUENCE 369 AA; 41829 MW; 7F75282B3E547834 CRC64;
MVKLPAISKK PREIAKQKII ELAKKMYEDL MKGKRPKITM PIRSLSNAMF DKEKGSFTLV
GKEKARTLTV NQAKIFAQTT KMLEFAKQLL ETDDFSTLRE AYYVSKNWGE ARFDDQQASN
NVIEDLEAAL GVLREHLGFI PEEDGSSVVG PLKIIEETPE GELVVDCTKL GTGAYNIPND
VTKLNLETDA DFILAIETSG MFARLNAERF WDKHNCILVS LKGVPARATR RFIKRLHEEH
DLPVLVFTDG DPYGYLNIYR TLKVGSGKAI HLADKLSIPA ARLIGVTPQD IIDYDLPTHP
LKEQDIKRIK DGLKNDDFVR SFPEWQKALK QMLDMGVRAE QQSLAKYGLK YVVNTYLPEK
IKDESTWLP
