ID   F3YAP5_MELPT            Unreviewed;       693 AA.
AC   F3YAP5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   21-MAR-2012, entry version 7.
DE   SubName: Full=DNA topoisomerase I;
DE            EC=5.99.1.2;
GN   OrderedLocusNames=MPTP_1121;
OS   Melissococcus plutonius (strain ATCC 35311 / CIP 104052 / LMG 20360 /
OS   NCIMB 702443).
OC   Bacteria; Firmicutes; Lactobacillales; Enterococcaceae; Melissococcus.
OX   NCBI_TaxID=940190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443;
RX   PubMed=21622755; DOI=10.1128/JB.05151-11;
RA   Okumura K., Arai R., Okura M., Kirikae T., Takamatsu D., Osaki M.,
RA   Miyoshi-Akiyama T.;
RT   "Complete genome sequence of Melissococcus plutonius ATCC 35311.";
RL   J. Bacteriol. 193:4029-4030(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 35311;
RA   Okumura K., Arai R., Osaki M., Okura M., Kirikae T., Takamatsu D.,
RA   Akiyama T.;
RT   "Whole genome sequence of Melissococcus plutonius ATCC 35311.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Releases the supercoiling and torsional tension of DNA
CC       introduced during the DNA replication and transcription by
CC       transiently cleaving and rejoining one strand of the DNA duplex.
CC       Introduces a single-strand break via transesterification at a
CC       target site in duplex DNA. The scissile phosphodiester is attacked
CC       by the catalytic tyrosine of the enzyme, resulting in the
CC       formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the
CC       expulsion of a 3'-OH DNA strand. The free DNA strand than
CC       undergoes passage around the unbroken strand thus removing DNA
CC       supercoils. Finally, in the religation step, the DNA 3'-OH attacks
CC       the covalent intermediate to expel the active-site tyrosine and
CC       restore the DNA phosphodiester backbone (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded
CC       DNA, followed by passage and rejoining.
CC   -!- SIMILARITY: Belongs to the prokaryotic type I/III topoisomerase
CC       family.
CC   -!- SIMILARITY: Contains 1 Toprim domain.
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DR   EMBL; AP012200; BAK21573.1; -; Genomic_DNA.
DR   RefSeq; YP_004456382.1; NC_015516.1.
DR   GeneID; 10595947; -.
DR   PATRIC; 54621009; VBIMelPlu182073_1114.
DR   KO; K03168; -.
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:0006265; P:DNA topological change; IEA:InterPro.
DR   InterPro; IPR000380; Topo_IA.
DR   InterPro; IPR003601; Topo_IA_2.
DR   InterPro; IPR013497; Topo_IA_cen.
DR   InterPro; IPR013824; Topo_IA_cen_sub1.
DR   InterPro; IPR013825; Topo_IA_cen_sub2.
DR   InterPro; IPR023405; Topo_IA_core_domain.
DR   InterPro; IPR003602; Topo_IA_DNA-bd.
DR   InterPro; IPR013498; Topo_IA_Znf.
DR   InterPro; IPR005733; TopoI_bac-type.
DR   InterPro; IPR006171; Toprim_domain.
DR   Gene3D; G3DSA:1.10.460.10; Topo_IA_cen_sub1; 3.
DR   Gene3D; G3DSA:2.70.20.10; Topo_IA_cen_sub2; 2.
DR   PANTHER; PTHR11390; Topo_IA; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF01396; zf-C4_Topoisom; 2.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF56712; Topo_IA_core; 1.
DR   TIGRFAMs; TIGR01051; TopA_bact; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   693 AA;  79229 MW;  B7678B6B80AE047D CRC64;
     MAYKYLVIVE SPAKAKTIEK YLGRNYKVVA SVGHIRDLPK SKMGIDIEND YAPHYISIRG
     KGDVIKSLKT AAKKADKVYL AADPDREGEA IAWHLSYLLG LDPNEKNRVV FNEITKEAVK
     AAFKEPRTIN LDLVNAQQAR RILDRLVGYS ISPILWRKVK KGLSAGRVQS VALKIIIDRE
     KEIKEFIPEE YWTIDGNFQK GRKKFKASFW GIEGKKKKLP KADSVKEITD KLKDNKYQVT
     KVEKKERKRN PALPFTTSSL QQEAARKLNF RTRKIMMIAQ QLYEGISLGK KQGTVGLITY
     MRTDSTRISA SAKVEATEYI EQTYGKEFSI QEERKVKKAQ GTQDAHEAVR PSSVLRTPDS
     IKEYLNKDQL KLYTLIWSRF LASQMAPALL DTMKVTLEQN QVMFIANGSK IKFKGFMQVY
     IEGRDDGKEE KENILPELVE GDSVTSINIE PKQHFTQPPA RFSEAALIHN LEENGVGRPS
     TYAPTLETIQ KRYYVKLTNK RFEPTELGEI INTLIVDFFP QIVDVHFTAA MEEDLDKIGD
     GKEEWITVVD RFYQPFEKEL TNAEEKIEKI QIKDEPAGFS CEECDHPMVI KLGKYGKFYA
     CSNFPDCRNT KPIVKEIGVR CPICHEGQVI ERKSKKNKLF YGCSRYPDCD FTSWDKPVGR
     LCPKCGKYLV EKKVKGGKQV VCINGDYEEN VQK
//