ID F3YAP5_MELPT Unreviewed; 693 AA. AC F3YAP5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 22-FEB-2023, entry version 69. DE RecName: Full=DNA topoisomerase 1 {ECO:0000256|HAMAP-Rule:MF_00952}; DE EC=5.6.2.1 {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 / NCIMB OS 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, which CC is 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 target CC site in duplex DNA. The scissile phosphodiester is attacked by the CC catalytic tyrosine of the enzyme, resulting in the formation of a DNA- CC (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH CC DNA strand. The free DNA strand then undergoes passage around the CC unbroken strand, thus removing DNA supercoils. Finally, in the CC religation step, the DNA 3'-OH attacks the covalent intermediate to CC expel the active-site tyrosine and restore the DNA phosphodiester CC backbone. {ECO:0000256|HAMAP-Rule:MF_00952}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-independent breakage of single-stranded DNA, followed by CC passage and rejoining.; EC=5.6.2.1; CC Evidence={ECO:0000256|ARBA:ARBA00000213, ECO:0000256|HAMAP- CC Rule:MF_00952}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00952}. CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|HAMAP-Rule:MF_00952}. 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 AlphaFoldDB; F3YAP5; -. DR STRING; 940190.MPTP_1121; -. DR EnsemblBacteria; BAK21573; BAK21573; MPTP_1121. DR KEGG; mps:MPTP_1121; -. DR HOGENOM; CLU_002929_4_3_9; -. DR OMA; PECKYTR; -. DR OrthoDB; 9804262at2; -. 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 (single strand cut, ATP-independent) 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; 3.40.50.140; -; 1. DR Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 2. DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1. DR Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1. DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 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; DNA TOPOISOMERASE, TYPE IA, CORE; 1. DR PANTHER; PTHR42785:SF1; OMEGA-PROTEIN; 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; Prokaryotic type I DNA topoisomerase; 1. DR SUPFAM; SSF57783; Zinc beta-ribbon; 1. DR TIGRFAMs; TIGR01051; topA_bact; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_00952}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00952}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Reference proteome {ECO:0000313|Proteomes:UP000008456}; KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP- KW Rule:MF_00952}; Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 4..114 FT /note="Toprim" FT /evidence="ECO:0000259|PROSITE:PS50880" FT REGION 164..169 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT ACT_SITE 300 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 34 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 140 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 141 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 144 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 149 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 156 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 302 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 492 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-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 //