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DNA topoisomerase 1 (EC 5.99.1.2) (DNA topoisomerase I) (Omega-protein) (Relaxing enzyme) (Swivelase) (Untwisting enzyme)

 TOP1_STAA3              Reviewed;         689 AA.
Q2FHI8;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 2.
05-DEC-2018, entry version 88.
RecName: Full=DNA topoisomerase 1 {ECO:0000255|HAMAP-Rule:MF_00952};
EC=5.99.1.2 {ECO:0000255|HAMAP-Rule:MF_00952};
AltName: Full=DNA topoisomerase I {ECO:0000255|HAMAP-Rule:MF_00952};
AltName: Full=Omega-protein;
AltName: Full=Relaxing enzyme;
AltName: Full=Swivelase;
AltName: Full=Untwisting enzyme;
Name=topA {ECO:0000255|HAMAP-Rule:MF_00952};
OrderedLocusNames=SAUSA300_1143;
Staphylococcus aureus (strain USA300).
Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
Staphylococcus.
NCBI_TaxID=367830;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USA300;
PubMed=16517273; DOI=10.1016/S0140-6736(06)68231-7;
Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
Perdreau-Remington F.;
"Complete genome sequence of USA300, an epidemic clone of community-
acquired meticillin-resistant Staphylococcus aureus.";
Lancet 367:731-739(2006).
-!- FUNCTION: Releases the supercoiling and torsional tension of DNA,
which is introduced during the DNA replication and transcription,
by transiently cleaving and rejoining one strand of the DNA
duplex. Introduces a single-strand break via transesterification
at a target site in duplex DNA. The scissile phosphodiester is
attacked by the catalytic tyrosine of the enzyme, resulting in the
formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the
expulsion of a 3'-OH DNA strand. The free DNA strand then
undergoes passage around the unbroken strand, thus removing DNA
supercoils. Finally, in the religation step, the DNA 3'-OH attacks
the covalent intermediate to expel the active-site tyrosine and
restore the DNA phosphodiester backbone. {ECO:0000255|HAMAP-
Rule:MF_00952}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP-independent breakage of single-stranded DNA, followed
by passage and rejoining.; EC=5.99.1.2;
Evidence={ECO:0000255|HAMAP-Rule:MF_00952};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_00952};
Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-
Rule:MF_00952};
-!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00952}.
-!- SIMILARITY: Belongs to the type IA topoisomerase family.
{ECO:0000255|HAMAP-Rule:MF_00952}.
-!- SEQUENCE CAUTION:
Sequence=ABD21813.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; CP000255; ABD21813.1; ALT_INIT; Genomic_DNA.
ProteinModelPortal; Q2FHI8; -.
SMR; Q2FHI8; -.
PRIDE; Q2FHI8; -.
EnsemblBacteria; ABD21813; ABD21813; SAUSA300_1143.
KEGG; saa:SAUSA300_1143; -.
HOGENOM; HOG000004018; -.
KO; K03168; -.
Proteomes; UP000001939; Chromosome.
GO; GO:0005694; C:chromosome; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
CDD; cd00186; TOP1Ac; 1.
CDD; cd03363; TOPRIM_TopoIA_TopoI; 1.
Gene3D; 1.10.290.10; -; 1.
Gene3D; 1.10.460.10; -; 1.
Gene3D; 2.70.20.10; -; 1.
HAMAP; MF_00952; Topoisom_1_prok; 1.
InterPro; IPR000380; Topo_IA.
InterPro; IPR003601; Topo_IA_2.
InterPro; IPR023406; Topo_IA_AS.
InterPro; IPR013497; Topo_IA_cen.
InterPro; IPR013824; Topo_IA_cen_sub1.
InterPro; IPR013825; Topo_IA_cen_sub2.
InterPro; IPR013826; Topo_IA_cen_sub3.
InterPro; IPR023405; Topo_IA_core_domain.
InterPro; IPR003602; Topo_IA_DNA-bd_dom.
InterPro; IPR013498; Topo_IA_Znf.
InterPro; IPR005733; TopoI_bac-type.
InterPro; IPR028612; Topoisom_1_IA.
InterPro; IPR006171; TOPRIM_domain.
InterPro; IPR034149; TOPRIM_TopoI.
PANTHER; PTHR42785; PTHR42785; 1.
Pfam; PF01131; Topoisom_bac; 1.
Pfam; PF01751; Toprim; 1.
Pfam; PF01396; zf-C4_Topoisom; 3.
PRINTS; PR00417; PRTPISMRASEI.
SMART; SM00437; TOP1Ac; 1.
SMART; SM00436; TOP1Bc; 1.
SMART; SM00493; TOPRIM; 1.
SUPFAM; SSF56712; SSF56712; 1.
TIGRFAMs; TIGR01051; topA_bact; 1.
PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
PROSITE; PS50880; TOPRIM; 1.
3: Inferred from homology;
Complete proteome; DNA-binding; Isomerase; Magnesium; Metal-binding;
Repeat; Topoisomerase; Zinc; Zinc-finger.
CHAIN 1 689 DNA topoisomerase 1.
/FTId=PRO_0000285943.
DOMAIN 3 113 Toprim. {ECO:0000255|HAMAP-
Rule:MF_00952}.
ZN_FING 577 603 C4-type 1.
ZN_FING 617 645 C4-type 2.
ZN_FING 658 681 C4-type 3.
REGION 163 168 Interaction with DNA. {ECO:0000255|HAMAP-
Rule:MF_00952}.
ACT_SITE 298 298 O-(5'-phospho-DNA)-tyrosine intermediate.
{ECO:0000255|HAMAP-Rule:MF_00952}.
METAL 9 9 Magnesium 1; catalytic.
{ECO:0000255|HAMAP-Rule:MF_00952}.
METAL 82 82 Magnesium 1; catalytic.
{ECO:0000255|HAMAP-Rule:MF_00952}.
METAL 82 82 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_00952}.
METAL 84 84 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_00952}.
SITE 33 33 Interaction with DNA. {ECO:0000255|HAMAP-
Rule:MF_00952}.
SITE 139 139 Interaction with DNA. {ECO:0000255|HAMAP-
Rule:MF_00952}.
SITE 140 140 Interaction with DNA. {ECO:0000255|HAMAP-
Rule:MF_00952}.
SITE 143 143 Interaction with DNA. {ECO:0000255|HAMAP-
Rule:MF_00952}.
SITE 148 148 Interaction with DNA. {ECO:0000255|HAMAP-
Rule:MF_00952}.
SITE 155 155 Interaction with DNA. {ECO:0000255|HAMAP-
Rule:MF_00952}.
SITE 300 300 Interaction with DNA. {ECO:0000255|HAMAP-
Rule:MF_00952}.
SITE 488 488 Interaction with DNA. {ECO:0000255|HAMAP-
Rule:MF_00952}.
SEQUENCE 689 AA; 79113 MW; 1F28D3BC10BDADE1 CRC64;
MADNLVIVES PAKAKTIEKY LGKKYKVIAS MGHVRDLPRS QMGVDTEDNY EPKYITIRGK
GPVVKELKKH AKKAKNVFLA SDPDREGEAI AWHLSKILEL EDSKENRVVF NEITKDAVKE
SFKNPREIEM NLVDAQQARR ILDRLVGYNI SPVLWKKVKK GLSAGRVQSV ALRLVIDREN
EIRNFKPEEY WTIEGEFRYK KSKFNAKFLH YKNKPFKLKT KKDVEKITAA LDGDQFEITN
VTKKEKTRNP ANPFTTSTLQ QEAARKLNFK ARKTMMVAQQ LYEGIDLKKQ GTIGLITYMR
TDSTRISDTA KVEAKQYITD KYGESYTSKR KASGKQGDQD AHEAIRPSST MRTPDDMKSF
LTKDQYRLYK LIWERFVASQ MAPAILDTVS LDITQGDIKF RANGQTIKFK GFMTLYVETK
DDSDSEKENK LPKLEQGDKV TATQIEPAQH YTQPPPRYTE ARLVKTLEEL KIGRPSTYAP
TIDTIQKRNY VKLESKRFVP TELGEIVHEQ VKEYFPEIID VEFTVNMETL LDKIAEGDIT
WRKVIDGFFS SFKQDVERAE EEMEKIEIKD EPAGEDCEIC GSPMVIKMGR YGKFMACSNF
PDCRNTKAIV KSIGVKCPKC NDGDVVERKS KKNRVFYGCS KYPECDFISW DKPIGRDCPK
CNQYLVENKK GKTTQVICSN CDYKEAAQK


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