ID   TOP3_STAS1              Reviewed;         712 AA.
AC   Q49ZH2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 114.
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};
GN   OrderedLocusNames=SSP0659;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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}.
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DR   EMBL; AP008934; BAE17804.1; -; Genomic_DNA.
DR   RefSeq; WP_011302595.1; NZ_MTGA01000036.1.
DR   AlphaFoldDB; Q49ZH2; -.
DR   SMR; Q49ZH2; -.
DR   KEGG; ssp:SSP0659; -.
DR   PATRIC; fig|342451.11.peg.661; -.
DR   eggNOG; COG0550; Bacteria.
DR   eggNOG; COG0551; Bacteria.
DR   HOGENOM; CLU_002929_5_2_9; -.
DR   OrthoDB; 9803554at2; -.
DR   Proteomes; UP000006371; 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; Reference proteome;
KW   Topoisomerase.
FT   CHAIN           1..712
FT                   /note="DNA topoisomerase 3"
FT                   /id="PRO_0000286379"
FT   DOMAIN          2..135
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00953"
FT   DOMAIN          152..581
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   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   712 AA;  81398 MW;  ECC25B17796FAF11 CRC64;
     MKSLIIAEKP SVGRDIANTL NINEKRNGYF ENNKYIVTWA LGHLVTNATP EQYDASYKEW
     KLNDLPIIPN KMKTIVISKT RKQFSTVQSL INNNKVKDII IATDAGREGE LVARLILDKA
     HNKKPTKRLW ISSVTNKAIK EGFNKLQDGR KFNNLYHAAL ARSEADWIVG INATRALTTK
     YDAQLSLGRV QTPTIQLVQM RQNEINHFKP QTYYTMKLNA AGLTFHCTKP QSHPDKTVLE
     SIKKAIDGQS GHIASISKTH KKAYPQQLYN LTDLQQDAYK RFHLGPKETL NTLQTLYERH
     KLVTYPRTDS NYLTDDMVDT LKDRLKAIMA TSLKDMAKAQ MSQTFSSKQR FVNNNKVSDH
     HAIIPTEVRP DINQLSQRES KIYMMIAQRY LENLMPPHEY EAIAIELKVG QHTFTFKDKV
     TTKLGFKAIY ENKESINTQI DQLQKGTKLN VTKILIEEHE TTAPPYFNEG SLLKAMESPQ
     KFFDLSDKKH DKTLKDTGGI GTVATRADII EKLFNMNAIE ARDGKIKVTS KGKQILELAP
     QKLTSPLLTA EWEEKLLLIE QGKYNASQFI SEMKAFTNQV VNEIKESEQN YKHDNLTTTE
     CPTCGKFMIK VKTKNGQMLV CQDPQCKTKK NVQRKTNARC PNCHKKMTLF GRGKDAVYRC
     VCGHTETQAQ MDKRHKNKKS DKVNKKDLKK YMNNDEGIEN NPFQDALKGL KF
//