ID   TOP1_STAS1              Reviewed;         688 AA.
AC   Q49X35;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=SSP1518;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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.
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DR   EMBL; AP008934; BAE18663.1; -; Genomic_DNA.
DR   RefSeq; YP_301608.1; -.
DR   GeneID; 3615164; -.
DR   GenomeReviews; AP008934_GR; SSP1518.
DR   KEGG; ssp:SSP1518; -.
DR   NMPDR; fig|342451.4.peg.1534; -.
DR   HOGENOM; Q49X35; -.
DR   OMA; Q49X35; RKFYGCS.
DR   BioCyc; SSAP342451:SSP1518-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    688       DNA topoisomerase 1.
FT                                /FTId=PRO_0000285947.
FT   ZN_FING     576    602       C4-type 1.
FT   ZN_FING     616    644       C4-type 2.
FT   ZN_FING     657    680       C4-type 3.
FT   ACT_SITE    298    298       For DNA cleavage activity (By
FT                                similarity).
SQ   SEQUENCE   688 AA;  79130 MW;  24BC79B6DD63D72B CRC64;
     MAENLVIVES PAKAKTIEKY LGKKYKVIAS MGHVRDLPRS QMGVDAENDY EPKYITIRGK
     GPVVKELKKH AKKAKKVFLA SDPDREGEAI AWHLANILNL EDSTENRVVF NEITKDAVKD
     SFKHPRGIEM ELVDAQQARR ILDRLVGYNI SPVLWKKVKK GLSAGRVQSV ALRLVIDREN
     EIRNFKPEEY WKIEGEFRYK KTKFTAKFLH FKNKPFKLTE KADVEKITTQ LDGDQFEVTK
     VTKKEKTRYP ANPFTTSTLQ QEAARKLNFK ARKTMMLAQQ LYEGIDLKKQ GTVGLITYMR
     TDSTRISDQA QSEAKNYIQE TYGNDYTSNR KSKGQGDQDA HEAIRPSSTL RTPNEMKNFL
     TRDQHRLYKL IWERFVASQM APAILDTVAM DLTQNDIKFR ANGQTIKFKG FMTLYVETKD
     DSEDGKDNKL PNIGEGEMVT ATNIEPSQHF TQPPPRYTEA RLVKTMEELK IGRPSTYAPT
     IDTIQKRNYV KNESKRFVPT ELGEIVHEQV KDYFPEIIDV DFTVNMETLL DKVADGEIGW
     KKVISDFYSS FKQDVERAEE EMEKIEIKDE PAGEDCEVCG SPMVIKMGRY GKFMACSNFP
     DCRNTKAIVK TIGVTCPKCK EGDVVERKSK KNRIFYGCSK YPECDFVTWD KPIGRDCPKC
     EHYLVEKKQG RKSQVVCSNC DYKEEEQK
//