ID A0A380G4F0_STAIN Unreviewed; 711 AA. AC A0A380G4F0; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 27-NOV-2024, entry version 24. DE RecName: Full=DNA topoisomerase 3 {ECO:0000256|HAMAP-Rule:MF_00953}; DE EC=5.6.2.1 {ECO:0000256|HAMAP-Rule:MF_00953}; DE AltName: Full=DNA topoisomerase III {ECO:0000256|HAMAP-Rule:MF_00953}; GN Name=topB {ECO:0000256|HAMAP-Rule:MF_00953, GN ECO:0000313|EMBL:SUM46014.1}; GN ORFNames=NCTC11048_01006 {ECO:0000313|EMBL:SUM46014.1}; OS Staphylococcus intermedius NCTC 11048. OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus; Staphylococcus intermedius group. OX NCBI_TaxID=1141106 {ECO:0000313|EMBL:SUM46014.1, ECO:0000313|Proteomes:UP000255549}; RN [1] {ECO:0000313|EMBL:SUM46014.1, ECO:0000313|Proteomes:UP000255549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 11048 {ECO:0000313|Proteomes:UP000255549}; RG Pathogen Informatics; RA Doyle S.; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. 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:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00000213, ECO:0000256|HAMAP- CC Rule:MF_00953}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00953}; CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|HAMAP-Rule:MF_00953}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00953}. 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; UHDP01000003; SUM46014.1; -; Genomic_DNA. DR RefSeq; WP_019167893.1; NZ_UHDP01000003.1. DR AlphaFoldDB; A0A380G4F0; -. DR STRING; 1141106.GCA_000308095_01884; -. DR OrthoDB; 9803554at2; -. DR Proteomes; UP000255549; Unassembled WGS sequence. 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_dom. 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; TOPOISOMERASE_I_PROK; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_00953}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00953}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00953}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00953}; KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP- KW Rule:MF_00953}. FT DOMAIN 3..136 FT /note="Toprim" FT /evidence="ECO:0000259|PROSITE:PS50880" FT REGION 187..192 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953" FT ACT_SITE 306 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953" FT BINDING 9 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953" FT BINDING 105 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953" FT SITE 61 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953" FT SITE 168 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953" FT SITE 176 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953" FT SITE 308 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953" SQ SEQUENCE 711 AA; 81786 MW; AC033F31CB41CD91 CRC64; MSKALILAEK PSVGRDIANA LNIGSRKEGY FENQQYIVTW ALGHLVTNAT PEQYDKKYQQ WVLEDLPIIP KQMKSVVIGK TRKQFNTVQH LMKRSDVNEL IIATDAGREG ELVARLIIEK AHVKKPIKRL WISSVTPKAI KEGFKKLKDG RAYDHLYQAA LARSEADWIV GINATRALTT KYDAQLSLGR VQTPTIQLVA MRQEQIKNFK PQQYYTLEAE VNGVTMTYQH EGRIYHKEKL EAIVQELQHQ HAQVNNVHEK EKKVYPQPLF NLTDLQQAAY QKYHLGAKQT LNTLQQLYER HKLVTYPRTD SNYLTTDMVD TLKERVQATM GTDLMPYARE ILQQPFAKKL SFVNNQKVSD HHAIIPTEVR ANIETLSPNE RKIYTMIAQR YLEVLMPPYR YRAQHVEVRI GKHTFTYQSQ VPVELGFKKL QQDRAQTERA VSFNQGETFE IGRLQIVAHE TTPPAYFNEG TLLKAMERPD KFFDLKDKKS AQTLKTIGGI GTVATRADII DKLFNMNAIE SQDGKIKVTS KGKQILDLAP PALTSPRLTA EWEDKLMQIE KGQFKAQQFM QEMKKFTHEI INTIKSSEQK YKHDNLTSAQ CPTCGKFMLK VNTKNGSMLV CQDPSCKTKK DVKTKTNARC PQCKKRLTKF GTGKKATYRC VCGYTETQEH MDQRFKNKGK DKVSKREMKK YMKEDELENN PFKDALKGLN L //