ID TOP3_STAHJ Reviewed; 711 AA. AC Q4L8B8; DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 129. DE RecName: Full=DNA topoisomerase 3 {ECO:0000255|HAMAP-Rule:MF_00953}; DE EC=5.6.2.1 {ECO:0000255|HAMAP-Rule:MF_00953}; DE AltName: Full=DNA topoisomerase III {ECO:0000255|HAMAP-Rule:MF_00953}; GN Name=topB {ECO:0000255|HAMAP-Rule:MF_00953}; OrderedLocusNames=SH0798; OS Staphylococcus haemolyticus (strain JCSC1435). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=279808; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCSC1435; RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005; RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., RA Hiramatsu K.; RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the RT extreme plasticity of its genome and the evolution of human-colonizing RT staphylococcal species."; RL J. Bacteriol. 187:7292-7308(2005). CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, which CC is introduced during the DNA replication and transcription, by CC transiently cleaving and rejoining one strand of the DNA duplex. CC Introduces a single-strand break via transesterification at a target CC site in duplex DNA. The scissile phosphodiester is attacked by the CC catalytic tyrosine of the enzyme, resulting in the formation of a DNA- CC (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH CC DNA strand. The free DNA strand then undergoes passage around the CC unbroken strand, thus removing DNA supercoils. Finally, in the CC religation step, the DNA 3'-OH attacks the covalent intermediate to CC expel the active-site tyrosine and restore the DNA phosphodiester CC backbone. {ECO:0000255|HAMAP-Rule:MF_00953}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-independent breakage of single-stranded DNA, followed by CC passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00953}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00953}; CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00953, ECO:0000255|PROSITE- CC ProRule:PRU01383}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP006716; BAE04107.1; -; Genomic_DNA. DR RefSeq; WP_011275121.1; NC_007168.1. DR AlphaFoldDB; Q4L8B8; -. DR SMR; Q4L8B8; -. DR KEGG; sha:SH0798; -. DR eggNOG; COG0550; Bacteria. DR eggNOG; COG0551; Bacteria. DR HOGENOM; CLU_002929_5_2_9; -. DR OrthoDB; 9803554at2; -. DR Proteomes; UP000000543; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) 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 CDD; cd00186; TOP1Ac; 1. DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1. DR Gene3D; 3.40.50.140; -; 1. DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1. DR Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1. DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1. DR HAMAP; MF_00953; Topoisom_3_prok; 1. DR InterPro; IPR000380; Topo_IA. DR InterPro; IPR003601; Topo_IA_2. DR InterPro; IPR023406; Topo_IA_AS. DR InterPro; IPR013497; Topo_IA_cen. DR InterPro; IPR013824; Topo_IA_cen_sub1. DR InterPro; IPR013825; Topo_IA_cen_sub2. DR InterPro; IPR013826; Topo_IA_cen_sub3. DR InterPro; IPR023405; Topo_IA_core_domain. DR InterPro; IPR003602; Topo_IA_DNA-bd_dom. DR InterPro; IPR005738; TopoIII. DR InterPro; IPR006171; TOPRIM_domain. DR InterPro; IPR034144; TOPRIM_TopoIII. DR NCBIfam; TIGR01056; topB; 1. DR PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1. DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1. DR PROSITE; PS00396; TOPO_IA_1; 1. DR PROSITE; PS52039; TOPO_IA_2; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW DNA-binding; Isomerase; Magnesium; Metal-binding; Topoisomerase. FT CHAIN 1..711 FT /note="DNA topoisomerase 3" FT /id="PRO_0000286378" FT DOMAIN 2..135 FT /note="Toprim" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT DOMAIN 152..580 FT /note="Topo IA-type catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01383" FT REGION 186..191 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT REGION 672..699 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 672..693 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 305 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01383" FT BINDING 8 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT BINDING 104 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT SITE 60 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT SITE 167 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT SITE 175 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT SITE 307 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" SQ SEQUENCE 711 AA; 81732 MW; 20D6F54E0A534035 CRC64; MKSLILAEKP SVARDIAEAM NIKGKRNGYI ENEKYVVTWA LGHLVTNAQP EHYDKAYKEW KLEDLPIIPK RMQTVVIGKT SKQFKTVKSL ILDKKVKEVI IATDAGREGE LVARLILDKV HNKKPIKRLW ISSVTKKAIQ EGFKKLKDGR EFQHLYEAAL ARSEADWIVG INATRALTTK YDAQLSLGRV QTPTIQLVNA RQQEINHFKA KKYYTLSTEI GGLTFQLSTN KQHMTMEDAT QIANEIKHVE GNVDSVEKKV KKSHPKPLYN LTDLQQEAYQ RYKMGPKETL NTIQNLYERH KVLTYPRTDS NYLTDDMVDT IKERLYALLA TDYKSQVKSL LGQSYSSKMR IFKNHKVSDH HAIIPTEVRP DMQSLSNRES KIYMMVAERF LESLMAPHEY EAVRVNVTVG QHIFAFNEKV TRQLGYKALK MNNDNVVKKV AFQKGEKYHL QSLKVNEHET TPPDYFNEGS LLKAMENPQN YIQLKEKKHA NTLRQTGGIG TVATRADIIE KLFNLNAIES RDGKIKVTSK GKQILDLAPQ ELTSPLLTAE WEEKLLLIEK GRYNSRHFID EMKAFTQSIV NTIKNSEQKY KHDNLTTTEC PTCGKFMIKV KTKNGQMLVC QDPTCKTKKN VQRKTNARCP NCKKKMTLFG RGKDAVYRCV CGHTETQEQM DKRFKNKSSG KVSKKEMKKY MNNEDSLENN PFKDALKNLK L //