ID TOP3_SALTI Reviewed; 649 AA. AC Q8Z6F5; DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 143. 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}; Synonyms=top3; GN OrderedLocusNames=STY1816, t1177; OS Salmonella typhi. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=90370; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT18; RX PubMed=11677608; DOI=10.1038/35101607; RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T., RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., RA Barrell B.G.; RT "Complete genome sequence of a multiple drug resistant Salmonella enterica RT serovar Typhi CT18."; RL Nature 413:848-852(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700931 / Ty2; RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003; RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., RA Kodoyianni V., Schwartz D.C., Blattner F.R.; RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and RT CT18."; RL J. Bacteriol. 185:2330-2337(2003). 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 Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-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; AL513382; CAD02056.1; -; Genomic_DNA. DR EMBL; AE014613; AAO68834.1; -; Genomic_DNA. DR RefSeq; NP_456214.1; NC_003198.1. DR RefSeq; WP_001235869.1; NZ_WSUR01000034.1. DR AlphaFoldDB; Q8Z6F5; -. DR SMR; Q8Z6F5; -. DR STRING; 220341.gene:17585748; -. DR KEGG; stt:t1177; -. DR KEGG; sty:STY1816; -. DR PATRIC; fig|220341.7.peg.1829; -. DR eggNOG; COG0550; Bacteria. DR HOGENOM; CLU_002929_5_2_6; -. DR OMA; KGKTAYG; -. DR OrthoDB; 9803554at2; -. DR Proteomes; UP000000541; Chromosome. DR Proteomes; UP000002670; 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..649 FT /note="DNA topoisomerase 3" FT /id="PRO_0000145185" FT DOMAIN 1..134 FT /note="Toprim" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT DOMAIN 155..603 FT /note="Topo IA-type catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01383" FT REGION 194..199 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT REGION 614..649 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 635..649 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 328 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01383" FT BINDING 7 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT BINDING 103 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT BINDING 103 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT BINDING 105 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT SITE 61 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT SITE 170 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT SITE 178 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT SITE 185 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" FT SITE 330 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953" SQ SEQUENCE 649 AA; 73087 MW; 1620030D62ED1729 CRC64; MRLFIAEKPS LGRAIADVLP KPHRKGDGFI ECGNGQVVTW CIGHLLEQAQ PDAYDSRYAR WNLADLPIVP EKWQLQPRPS VTKQLNVIKR FLHQAGEIIH AGDPDREGQL LVDEVLDYLQ LPAEKRQQVR RCLINDLNPQ AVERAIDRLR ANSDFVPLCV SALARARADW LYGINMTRAY TILGRNAGYQ GVLSVGRVQT PVLGLVVRRD EEIENFVAKD FFEVKAHIVT PADERFTAIW QPSEACEPYQ DEEGRLLHRP LAEHVVNRIN GQPALVTSYN DKRESESAPL PFSLSTLQIE AAKRFGLSAQ NVLDICQKLY ETHKLITYPR SDCRYLPEEH FAGRQAVMNA ISVHAPDLLP QPVVNPDTRN RCWDDKKVDA HHAIIPTARS SSVHLTENEA KVYTLIARQY LMQFCPDAVF RKCVIELEIA KGKFVAKARF LAEAGWRTLL GSKERDEEND GTPLSVVAKG DELLCEKGEV VERQTQPPRH FTDATLLSAM TGIARFVQDK DLKKILRATD GLGTEATRAG IIELLFKRSF LTKKGRYIHS TDAGKALIHS LPEMAARPDM TAHWESVLTQ ISEKQCRYQD FMQPLVGTLY QLIDQAKRTP VKRFRGIVAP GGGEKKKSAP RKRAGKKSPP AEETGRQTE //