ID   TOP1_STAHJ              Reviewed;         689 AA.
AC   Q4L5V2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
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=SH1664;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP006716; BAE04973.1; -; Genomic_DNA.
DR   RefSeq; YP_253579.1; -.
DR   GeneID; 3481647; -.
DR   GenomeReviews; AP006716_GR; SH1664.
DR   KEGG; sha:SH1664; -.
DR   NMPDR; fig|279808.3.peg.1036; -.
DR   HOGENOM; Q4L5V2; -.
DR   OMA; Q4L5V2; RKFYGCS.
DR   BioCyc; SHAE279808:SH1664-MON; -.
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_0000285946.
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;  79373 MW;  C41C302CDCE30145 CRC64;
     MADNLVIVES PAKAKTIEKY LGKKYKVIAS MGHVRDLPRS QMGVDVEDNY EPKYITIRGK
     GPVVKDLKKY AKKAKNVFLA SDPDREGEAI AWHLSKILEL DDSKENRVVF NEITKDAVKE
     SFKHPRGIEM DLVDAQQARR ILDRLVGYNI SPVLWKKVKK GLSAGRVQSV ALRLVIDREN
     EIRNFKPEEY WSIEGEFRYK KSKFTAKFLH YKNKPFKLKT KKDVEKVTAE LDGDKFEITN
     VNKKEKTRNP ANPFTTSTLQ QEAARKLNFK ARKTMMLAQQ LYEGIDLKRQ GTVGLITYMR
     TDSTRISQTA KDEAKQYIED KYGKDYLSNR TAKGKQGDQD AHEAIRPTST LRTPYEMKAY
     LTRDQHRLYK LIWERFVASQ MAPAILDTVA LDVTQNNIKF RANGQTIKFK GFMTLYVEAK
     DDKDNEKENK LPNLSKGDEV TATQIEPAQH FTQPPPRYTE ARLVKTLEEL KIGRPSTYAP
     TIDTIQKRNY VKLESKRFVP TELGEIVYEQ VKDYFPEIID VEFTVNMETL LDKIAEGDIG
     WRKVIDNFYG SFKLDVERAE EEMEKVEIKD EPAGEDCEVC GSPMVIKMGR YGKFMACSNF
     PDCRNTKAIV KTIGVTCPKC KDGDVVERKS KKNRLFYGCS NYPECDFISW DKPVGRDCPK
     CNHYLMEHKK GRSSQVICSN CDYKEEVQK
//