ID F3YAP5_MELPT Unreviewed; 693 AA. AC F3YAP5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-NOV-2018, entry version 52. 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 -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded CC DNA, followed by passage and rejoining. {ECO:0000256|HAMAP- CC Rule:MF_00952, ECO:0000256|SAAS:SAAS00721095}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP012200; BAK21573.1; -; Genomic_DNA. DR RefSeq; WP_013774011.1; NC_015516.1. DR ProteinModelPortal; F3YAP5; -. DR STRING; 940190.MPTP_1121; -. 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 OrthoDB; POG091H02BN; -. 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 //