ID   TOP1_RICFE              Reviewed;         776 AA.
AC   Q4UM42;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-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=RF_0530;
OS   Rickettsia felis (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=42862;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
CC   -!- FUNCTION: The reaction catalyzed by topoisomerases leads to the
CC       conversion of one topological isomer of DNA to another.
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.
CC   -!- SIMILARITY: Belongs to the prokaryotic type I/III topoisomerase
CC       family.
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DR   EMBL; CP000053; AAY61381.1; -; Genomic_DNA.
DR   RefSeq; YP_246546.1; -.
DR   GeneID; 3401192; -.
DR   GenomeReviews; CP000053_GR; RF_0530.
DR   KEGG; rfe:RF_0530; -.
DR   NMPDR; fig|315456.3.peg.364; -.
DR   HOGENOM; Q4UM42; -.
DR   OMA; Q4UM42; RKFYGCS.
DR   BioCyc; RFEL315456:RF_0530-MON; -.
DR   BRENDA; 5.99.1.2; 297363.
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; 1.
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; 1.
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; Topoisomerase; Zinc; Zinc-finger.
FT   CHAIN         1    776       DNA topoisomerase 1.
FT                                /FTId=PRO_0000273105.
FT   ZN_FING     600    627       C4-type.
FT   ACT_SITE    304    304       For DNA cleavage activity (By
FT                                similarity).
SQ   SEQUENCE   776 AA;  88141 MW;  7833BDDB544310E6 CRC64;
     MKLVIVESPA KAKTINKYLG DEFKVIASFG HIRDLPSKKG SVLPDENFAM KYDISDKAGK
     YVDAIVKDAK KADAVYLATD PDREGEAISW HVAEVIKEKN KVKSDDFFKR VAFNEITKKA
     IIHAVENPRK LDANLVNAQQ ARRALDYLVG FTLSPLLWRK LPGCKSAGRV QSVALRLICE
     REDEIERFKS EEYWDISLKM QNSNNELFTA KLTHVNDQKL EKFSIINEKD AKDLTEKLKS
     QNFHVDKIEK KQQKRQPQPP FITSSLQQEA ARKLGFSAKK TMQIAQKLYE GVDIGKETIG
     LITYMRTDGV TLSNDAIADI RKLIDKNYGD KYLPNSPRIY KSKVKNAQEA HEAIRPTNIT
     YTPDSLKEKL EKDYYKLYEL IWKRTIACQM ENVIMDLVVA SLASENKEYL AKANGSTIAF
     DGFYKVYRES VDDEAEEENK MLPPLKEQEP LKTKEIIPNQ HFTEPPPRYS EASLVKKLEE
     LGIGRPSTYA SILSVLQDRK YVSLEKKRFM PEELGRLVTV FLVGFFKKYV EYDFTAGLEN
     ELDEIAAGKL EWKAALNNFW SGFNHNIESV NEQKITEIIS YVQKALDYHL FSENKESKAC
     PSCKTGELSL KLGKFGAFLA CSNYPECTFR KSIVSGNDNN ENDGDLAATP NENKVLGTDK
     DGIEIYLKKG PYGPYVQLGE QEGKVKPKRS PVPASLNQND ITLEMALKLL SLPLKIGIHK
     DSGEEIMIGY GKFGPYIKYM GKFISIPKKY DFLNLSLDDA MKLIEDNKAK LEKKQA
//