ID   TOP1_RICBR              Reviewed;         800 AA.
AC   Q1RIM1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=RBE_0712;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae
RT   in gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04793.1; -; Genomic_DNA.
DR   RefSeq; YP_537882.1; -.
DR   GeneID; 3995312; -.
DR   GenomeReviews; CP000087_GR; RBE_0712.
DR   KEGG; rbe:RBE_0712; -.
DR   HOGENOM; Q1RIM1; -.
DR   OMA; Q1RIM1; TGQVVKF.
DR   BioCyc; RBEL336407:RBE_0712-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; 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    800       DNA topoisomerase 1.
FT                                /FTId=PRO_0000273104.
FT   ZN_FING     600    627       C4-type.
FT   ACT_SITE    304    304       For DNA cleavage activity (By
FT                                similarity).
SQ   SEQUENCE   800 AA;  91229 MW;  686E7F5561AF337D CRC64;
     MKLVIVESPA KAKTINKYLG DEFKVIASFG HIRDLPSKKG SVIPDENFSM KYDISEKAGK
     YVDAIIKDAK KAESVYLATD PDREGESISW HIAEVIKEKN KVKSDDFFKR VAFNEITKKA
     ITHAIENPRK LDNNLVNAQQ ARRALDYLVG FTLSPLLWRK LPGCKSAGRV QSVALRLICE
     REDEIERFKS EEYWDISLKM LNSNNELFTA KLTHINDQKL EKFSITNDKE AKDLTEKLKS
     QNFHVDKIEK KQQKRQPQPP FITSSLQQEA ARKLGFSAKK TMQIAQKLYE GVDIGKETIG
     LITYMRTDGV TLSNDAVDEI RKLINKDYGD KYLPSSPRIY KSKVKNAQEA HEAIRPTNIN
     YIPNDLKEKL EKDYYKLYEL IWKRTIACQM ENVIMDLVNA TLASENKEYL ARANGSTIAF
     DGFYKVYRES IDDEAEEENK MLPPLKEQEH LKTKEIIPNQ HFTEPPPRYS EASLVKKLEE
     LGIGRPSTYA TILSVLQDRK YVTLEKKRFI PEELGRLVTV FLVGFFKKYV EYDFTAGLEN
     ELDEIAAGKL EWKSALGNFW NGFNHNIESV NKQNITEIIS YVQQALDYHI FGENKDSKVC
     PSCKTGELSL KLGKFGAFLA CSNYPECNFR KSIVSGNDNN EADGEAKDIV NENKVLGKDK
     EGIEIYLKKG PYGPYIQYGE QVDSKIKPKR SPLPAGLNQN DITLDMALKL LSLPLKIGNH
     KESGEEVLVG YGKFGPYIKY MGKFISIPKK YDFLNLSLDD AMKLIEEKLN AIAAKQPNPL
     NMDEVTNLVD KKIKVKKTKK
//