ID   F3YAP5_MELPT            Unreviewed;       693 AA.
AC   F3YAP5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   10-APR-2019, entry version 55.
DE   RecName: Full=DNA topoisomerase 1 {ECO:0000256|HAMAP-Rule:MF_00952};
DE            EC=5.99.1.2 {ECO:0000256|HAMAP-Rule:MF_00952};
DE   AltName: Full=DNA topoisomerase I {ECO:0000256|HAMAP-Rule:MF_00952};
GN   Name=topA {ECO:0000256|HAMAP-Rule:MF_00952};
GN   OrderedLocusNames=MPTP_1121 {ECO:0000313|EMBL:BAK21573.1};
OS   Melissococcus plutonius (strain ATCC 35311 / CIP 104052 / LMG 20360 /
OS   NCIMB 702443).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Melissococcus.
OX   NCBI_TaxID=940190 {ECO:0000313|EMBL:BAK21573.1, ECO:0000313|Proteomes:UP000008456};
RN   [1] {ECO:0000313|EMBL:BAK21573.1, ECO:0000313|Proteomes:UP000008456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443
RC   {ECO:0000313|Proteomes:UP000008456};
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       which is introduced during the DNA replication and transcription,
CC       by transiently cleaving and rejoining one strand of the DNA
CC       duplex. Introduces a single-strand break via transesterification
CC       at a target site in duplex DNA. The scissile phosphodiester is
CC       attacked 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 then
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. {ECO:0000256|HAMAP-
CC       Rule:MF_00952}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00721088};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00952,
CC       ECO:0000256|SAAS:SAAS00709415}.
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00952, ECO:0000256|SAAS:SAAS00721110}.
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DR   EMBL; AP012200; BAK21573.1; -; Genomic_DNA.
DR   RefSeq; WP_013774011.1; NC_015516.1.
DR   ProteinModelPortal; F3YAP5; -.
DR   EnsemblBacteria; BAK21573; BAK21573; MPTP_1121.
DR   GeneID; 34409975; -.
DR   KEGG; mps:MPTP_1121; -.
DR   eggNOG; ENOG4105C73; Bacteria.
DR   eggNOG; COG0550; LUCA.
DR   eggNOG; COG0551; LUCA.
DR   KO; K03168; -.
DR   OMA; PECKYTR; -.
DR   BioCyc; MPLU940190:G1H6C-1014-MONOMER; -.
DR   Proteomes; UP000008456; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03363; TOPRIM_TopoIA_TopoI; 1.
DR   Gene3D; 1.10.290.10; -; 1.
DR   Gene3D; 1.10.460.10; -; 1.
DR   Gene3D; 2.70.20.10; -; 1.
DR   HAMAP; MF_00952; Topoisom_1_prok; 1.
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; IPR013826; Topo_IA_cen_sub3.
DR   InterPro; IPR023405; Topo_IA_core_domain.
DR   InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR   InterPro; IPR013498; Topo_IA_Znf.
DR   InterPro; IPR005733; TopoI_bac-type.
DR   InterPro; IPR028612; Topoisom_1_IA.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034149; TOPRIM_TopoI.
DR   PANTHER; PTHR42785; PTHR42785; 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   SUPFAM; SSF56712; SSF56712; 1.
DR   TIGRFAMs; TIGR01051; topA_bact; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008456};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00952,
KW   ECO:0000256|SAAS:SAAS00721076};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00952,
KW   ECO:0000256|SAAS:SAAS00721131, ECO:0000313|EMBL:BAK21573.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00721141};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00721137};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008456};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00952,
KW   ECO:0000256|SAAS:SAAS00721067}.
FT   DOMAIN        4    114       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   REGION      164    169       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   COILED      553    573       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    300    300       O-(5'-phospho-DNA)-tyrosine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00952}.
FT   SITE         34     34       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        140    140       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        141    141       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        144    144       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        149    149       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        156    156       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        302    302       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        492    492       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
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
//