ID TOP1_CAMJE Reviewed; 700 AA. AC Q9PLZ2; Q0P7U5; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 136. DE RecName: Full=DNA topoisomerase 1 {ECO:0000255|HAMAP-Rule:MF_00952}; DE EC=5.6.2.1 {ECO:0000255|HAMAP-Rule:MF_00952}; DE AltName: Full=DNA topoisomerase I {ECO:0000255|HAMAP-Rule:MF_00952}; DE AltName: Full=Omega-protein; DE AltName: Full=Relaxing enzyme; DE AltName: Full=Swivelase; DE AltName: Full=Untwisting enzyme; GN Name=topA {ECO:0000255|HAMAP-Rule:MF_00952}; GN OrderedLocusNames=Cj1686c; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / OS NCTC 11168). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700819 / NCTC 11168; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., RA Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). 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:0000255|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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00952}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00952}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00952}. CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC {ECO:0000255|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; AL111168; CAL35780.1; -; Genomic_DNA. DR PIR; B81266; B81266. DR RefSeq; WP_002851268.1; NZ_SZUC01000002.1. DR RefSeq; YP_002345052.1; NC_002163.1. DR AlphaFoldDB; Q9PLZ2; -. DR SMR; Q9PLZ2; -. DR STRING; 192222.Cj1686c; -. DR PaxDb; 192222-Cj1686c; -. DR EnsemblBacteria; CAL35780; CAL35780; Cj1686c. DR GeneID; 905960; -. DR KEGG; cje:Cj1686c; -. DR PATRIC; fig|192222.6.peg.1660; -. DR eggNOG; COG0550; Bacteria. DR HOGENOM; CLU_002929_4_3_7; -. DR OrthoDB; 9804262at2; -. DR Proteomes; UP000000799; 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; IPR023406; Topo_IA_AS. 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 NCBIfam; TIGR01051; topA_bact; 1. DR PANTHER; PTHR42785:SF1; DNA TOPOISOMERASE; 1. DR PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 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; 2. DR PROSITE; PS00396; TOPO_IA_1; 1. DR PROSITE; PS52039; TOPO_IA_2; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW DNA-binding; Isomerase; Magnesium; Metal-binding; Reference proteome; KW Repeat; Topoisomerase; Zinc; Zinc-finger. FT CHAIN 1..700 FT /note="DNA topoisomerase 1" FT /id="PRO_0000145146" FT DOMAIN 3..114 FT /note="Toprim" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT DOMAIN 130..553 FT /note="Topo IA-type catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01383" FT ZN_FING 573..599 FT /note="C4-type 1" FT ZN_FING 629..656 FT /note="C4-type 2" FT ZN_FING 669..692 FT /note="C4-type 3" FT REGION 164..169 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT ACT_SITE 298 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01383" FT BINDING 9 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT BINDING 83 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 33 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 140 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 141 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 144 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 149 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 300 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" FT SITE 485 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952" SQ SEQUENCE 700 AA; 79148 MW; 86CE6DE6A8231A00 CRC64; MKKNLIIVES PAKAKTIGNF LGKDYEVIAS KGHIRDLPKS SFGIKIEDDE FIPEYRITSD HSALVKELKS KAKDAKEVYL ATDEDREGEA IAYHIAKAIG KDENTLPRIV FHEITKSAIE NALKNPRKLN MHSVNAQQTR RLLDRIVGYK LSPLLGQKIQ RGLSAGRVQS AALKIIVDRE KEIRAFVPLE YFSIDMIFQK DLDAELVEFD KAKIEKLTIT NKDRAKLILE ACKNEVYSIS DIESKERKIA PPPPFMTSTL QQSASNRLGF NPKKTMMIAQ KLYEGVNTHE GVMGVITYMR TDSLNLAKEA VENARKFIQA NFGKDYLPSK ANVYTTKTKG AQEAHEAIRP TNLSFTPEIA AKFLDKDELK LYTLIYNRFL ACQMSPAISQ TQNVFVKNDR VVFKISGRKI LFDGYYKVYG DMDKDKILPN FKIGQNLKVQ NLEMNSHFTE PPSRYSEAGL VKKLESLGIG RPSTYAPTIS ILTSRDYVTI DKKQLIPSDV AFNVTEVLEK NFSDIVDSKF TSNLENTLDE IAEDKADWQE TLKEFYYPFM RKIEEGKTKI ASQKTVTKLG ESCPDCGGEL AIRKGRFGEF VACLNFPKCK YSRNLKSESK NESENTAAKA KANGTGITCP SCQKGEIVER FSKRGKFYGC SAYPKCNFIS KYKPSEEKCE ECGETLVIKE LKKGTFLECL KCKIKKEMKD //