ID   TOP1_STAA3              Reviewed;         689 AA.
AC   Q2FHI8;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=DNA topoisomerase 1;
DE            EC=5.99.1.2;
DE   AltName: Full=DNA topoisomerase I;
DE   AltName: Full=Omega-protein;
DE   AltName: Full=Relaxing enzyme;
DE   AltName: Full=Untwisting enzyme;
DE   AltName: Full=Swivelase;
GN   Name=topA; OrderedLocusNames=SAUSA300_1143;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16517273; DOI=10.1016/S0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
CC   -!- FUNCTION: The reaction catalyzed by topoisomerases leads to the
CC       conversion of one topological isomer of DNA to another (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded
CC       DNA, followed by passage and rejoining.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- MISCELLANEOUS: When a topoisomerase transiently breaks a DNA
CC       backbone bond, it simultaneously forms a protein-DNA link, in
CC       which a tyrosyl oxygen in the enzyme is joined to a DNA phosphorus
CC       at one end of the enzyme-severed DNA strand (By similarity).
CC   -!- SIMILARITY: Belongs to the prokaryotic type I/III topoisomerase
CC       family.
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DR   EMBL; CP000255; ABD21813.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_493840.1; -.
DR   GeneID; 3915296; -.
DR   GenomeReviews; CP000255_GR; SAUSA300_1143.
DR   KEGG; saa:SAUSA300_1143; -.
DR   HOGENOM; Q2FHI8; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   GO; GO:0006268; P:DNA unwinding during replication; IEA:InterPro.
DR   InterPro; IPR003601; Topo_IA_2.
DR   InterPro; IPR013497; Topo_IA_cen.
DR   InterPro; IPR013824; Topo_IA_cen_sub1.
DR   InterPro; IPR013826; Topo_IA_cen_sub3.
DR   InterPro; IPR000380; Topo_IA_core.
DR   InterPro; IPR003602; Topo_IA_DNA_bd.
DR   InterPro; IPR013498; Topo_IA_Znf.
DR   InterPro; IPR005733; TopoI_bac.
DR   InterPro; IPR006171; Toprim_domain.
DR   InterPro; IPR006154; Toprim_sub.
DR   Gene3D; G3DSA:1.10.460.10; Topo_IA_cen_sub1; 2.
DR   Gene3D; G3DSA:1.10.290.10; Topo_IA_cen_sub3; 1.
DR   PANTHER; PTHR11390; Topo_IA; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF01396; zf-C4_Topoisom; 3.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   TIGRFAMs; TIGR01051; topA_bact; 1.
DR   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; DNA-binding; Isomerase; Metal-binding;
KW   Nucleotide-binding; Repeat; Topoisomerase; Zinc; Zinc-finger.
FT   CHAIN         1    689       DNA topoisomerase 1.
FT                                /FTId=PRO_0000285943.
FT   ZN_FING     577    603       C4-type 1.
FT   ZN_FING     617    645       C4-type 2.
FT   ZN_FING     658    681       C4-type 3.
FT   ACT_SITE    298    298       For DNA cleavage activity (By
FT                                similarity).
SQ   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
//