ID A0A380G4F0_STAIN Unreviewed; 711 AA. AC A0A380G4F0; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 13-FEB-2019, entry version 4. DE RecName: Full=DNA topoisomerase 3 {ECO:0000256|HAMAP-Rule:MF_00953}; DE EC=5.99.1.2 {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; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. 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, CC which is introduced during the DNA replication and transcription, CC by transiently cleaving and rejoining one strand of the DNA CC duplex. Introduces a single-strand break via transesterification CC at a target site in duplex DNA. The scissile phosphodiester is CC attacked by the catalytic tyrosine of the enzyme, resulting in the CC formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the CC expulsion of a 3'-OH DNA strand. The free DNA strand then CC undergoes passage around the unbroken strand, thus removing DNA CC supercoils. Finally, in the religation step, the DNA 3'-OH attacks CC the covalent intermediate to expel the active-site tyrosine and CC restore the DNA phosphodiester backbone. {ECO:0000256|HAMAP- CC Rule:MF_00953}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-independent breakage of single-stranded DNA, followed CC by passage and rejoining.; EC=5.99.1.2; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00953}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00953}; CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC {ECO:0000256|HAMAP-Rule:MF_00953}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of 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 Proteomes; UP000255549; Unassembled WGS sequence. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003917; F:DNA topoisomerase type I 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; 1.10.290.10; -; 1. DR Gene3D; 1.10.460.10; -; 1. DR Gene3D; 2.70.20.10; -; 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 PANTHER; PTHR11390; PTHR11390; 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; SSF56712; 1. DR TIGRFAMs; TIGR01056; topB; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000255549}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00953}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00953, KW ECO:0000313|EMBL:SUM46014.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00953}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00953}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00953}. FT DOMAIN 3 136 Toprim. {ECO:0000259|PROSITE:PS50880}. FT REGION 187 192 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00953}. FT COILED 237 257 {ECO:0000256|SAM:Coils}. FT ACT_SITE 306 306 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00953}. FT METAL 9 9 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00953}. FT METAL 105 105 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00953}. FT SITE 61 61 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00953}. FT SITE 168 168 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00953}. FT SITE 176 176 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00953}. FT SITE 308 308 Interaction with DNA. {ECO:0000256|HAMAP- FT 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 //