TOP3_STAAB
ID TOP3_STAAB Reviewed; 711 AA.
AC P0C2W6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Putative DNA topoisomerase 3;
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=SAB2126c;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00953};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00953}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AJ938182; Type=Frameshift; Evidence={ECO:0000305};
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; AJ938182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C2W6; -.
DR SMR; P0C2W6; -.
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; 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 5: Uncertain;
KW DNA-binding; Isomerase; Magnesium; Metal-binding; Topoisomerase.
FT CHAIN 1..711
FT /note="Putative DNA topoisomerase 3"
FT /id="PRO_0000286369"
FT DOMAIN 2..135
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953"
FT REGION 186..191
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953"
FT REGION 691..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 305
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00953"
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; 81552 MW; 7EB1133AA3D323A5 CRC64;
MKYLILAEKP SVARDIADAL QINQKRNGYF ENNQYIVTWA LGHLVTNATP EQYDKNLKEW
RLEDLPIIPK YMKTVVIGKT SKQFKTVKAL ILDNKVKDII IATDAGREGE LVARLILDKV
GNKKPLRRLW ISSVTKKAIQ QSFKNLKDGR QYNDLYYAAL ARSEADWIVG INATRALTTK
YDAQLSLGRV QTPTIQLVNT RQQEINQFKP QQYYTLSLTV KGFDFQLESN QRYTNKETLE
QIVNNLKNVD GKIKSVATKH KKSYPQSLYN LTDLQQDMYR RYKIGPKETL NTLQSLYERH
KVVTYPRTDS NYLTTDMVDT MKERIQATMA TTYKDQARPL ISKTFSSKMS IFNNQKVSDH
HAIIPTEVRP VMSDLSNREL KLYDMIVERF LEALMPPHEY DAITVTLEVA GHTFVLKENV
TTVLGFKSIR QGESITEMQQ PFSEGDEVKI SKTNIREHET TPPEYFNEGS LLKAMENPQN
FIQLKDKKYA QTLKQTGGIG TVATRADIID KLFNMNAIES RDGKIKVTSK GKQILELAPE
ELTSPLLTAQ WEEKLLLIER GKYQAKTFIN EMKGFTKDVV NGIKNSDRKY KHDNLTTTEC
PTCGKFMIKV KTKNGQMLVC QDPSCKTKKN VQRKTNARCP NCKKKLTLFG KGKEAVYRCV
CGHSETQAHM DQRMKSKSSG KVSRKEMKKY MNKNEGLDNN PFKDALKNLN L
