TOP3_STAEQ
ID TOP3_STAEQ Reviewed; 711 AA.
AC Q5HLZ4;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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}; OrderedLocusNames=SERP1836;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00953};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00953}.
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DR EMBL; CP000029; AAW55174.1; -; Genomic_DNA.
DR RefSeq; WP_002456984.1; NC_002976.3.
DR AlphaFoldDB; Q5HLZ4; -.
DR SMR; Q5HLZ4; -.
DR STRING; 176279.SERP1836; -.
DR EnsemblBacteria; AAW55174; AAW55174; SERP1836.
DR KEGG; ser:SERP1836; -.
DR eggNOG; COG0550; Bacteria.
DR eggNOG; COG0551; Bacteria.
DR HOGENOM; CLU_002929_5_2_9; -.
DR OMA; TYPRVDT; -.
DR OrthoDB; 100725at2; -.
DR Proteomes; UP000000531; 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; 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 DNA-binding; Isomerase; Magnesium; Metal-binding; Reference proteome;
KW Topoisomerase.
FT CHAIN 1..711
FT /note="DNA topoisomerase 3"
FT /id="PRO_0000286376"
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 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; 82393 MW; 13AB643F53065FB9 CRC64;
MKSLILAEKP SVGRDIANAL NLQQKSNGYI EGKQYIVTWA LGHLVTNATP EQYNPSYKEW
NLEDLPIIPK KMKTVVISKT NRQFKIVKSL ILDKNVKEII IATDAGREGE LVARLILDKV
GNKKPIKRLW ISSVTKKAIQ EGFKQLKNGN AYQNLYEAAL ARSEADWIVG INATRALTTK
YDAQLSLGRV QTPTIQIVKS RQDEINYFKP EKYYTLSINV DGYDLNLKQQ KRYKDKKELE
LIEHKIKHQE GKILEVKGKN KKSYAQPLFN LTDLQQEAYK HYKMGPKETL NTLQHLYERH
KLVTYPRTDS NYLTDDMVDT IQERLRAILA TDYKSHVRDL ISESFSSKMH IFNNQKVSDH
HAIIPTEVRP SIEQLSQREF KIYMLIAERF LENLMNPYLY EVLTIHAQLK DYNFVLKEII
PKQLGYKALK DQTSSHTLTH SFKEGQLFKV HRIEIHEHET KAPEYFNEGS LLKAMENPQN
HIDLNDKKYA KTLKHSGGIG TVATRADIIE KLFNMNALES RDGKIKVTSK GKQILELSPS
ELTSPILTAQ WEEKLMLIEK GKYNSQKFIQ EMKNFTFKVV NKIKSSEQKY KHDNLTTTEC
PTCGKFMIKV KTKNGQMLVC QDPKCKTKKN IQRKTNARCP YCKKKMTLFG KGKEAVYRCV
CGHTETQSQM DKRMRDKTNG KVSRKEMKKY INKKEEIDNN PFKDALKNLK L
