ID A0A2H9SV32_9BACT Unreviewed; 863 AA. AC A0A2H9SV32; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 18-SEP-2019, entry version 13. 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 ORFNames=CK425_02690 {ECO:0000313|EMBL:PJD97551.1}; OS Parachlamydia sp. OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae; OC Parachlamydia. OX NCBI_TaxID=2052048 {ECO:0000313|EMBL:PJD97551.1, ECO:0000313|Proteomes:UP000237012}; RN [1] {ECO:0000313|EMBL:PJD97551.1, ECO:0000313|Proteomes:UP000237012} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BC.030 {ECO:0000313|EMBL:PJD97551.1}; RX PubMed=29097994; DOI=10.3389/fmicb.2017.02036; RA Zhang Y., Kitajima M., Whittle A.J., Liu W.T.; RT "Benefits of Genomic Insights and CRISPR-Cas Signatures to Monitor RT Potential Pathogens across Drinking Water Production and Distribution RT Systems."; RL Front. Microbiol. 8:2036-2036(2017). 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: CC Reaction=ATP-independent breakage of single-stranded DNA, followed CC by passage and rejoining.; EC=5.6.2.1; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00952, CC ECO:0000256|SAAS:SAAS01216176}; 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00952}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PJD97551.1}. 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; PEQL01000003; PJD97551.1; -; Genomic_DNA. DR Proteomes; UP000237012; Unassembled WGS sequence. 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; 1.10.245.10; -; 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; IPR019835; SWIB_domain. DR InterPro; IPR036885; SWIB_MDM2_dom_sf. DR InterPro; IPR003121; SWIB_MDM2_domain. 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 PANTHER; PTHR42785; PTHR42785; 1. DR Pfam; PF02201; SWIB; 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; SM00151; SWIB; 1. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF47592; SSF47592; 1. DR SUPFAM; SSF56712; SSF56712; 1. DR TIGRFAMs; TIGR01051; topA_bact; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000237012}; 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:PJD97551.1}; KW Magnesium {ECO:0000256|SAAS:SAAS00721141}; KW Metal-binding {ECO:0000256|SAAS:SAAS00721137}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00952, KW ECO:0000256|SAAS:SAAS00721067}. FT DOMAIN 3 113 Toprim. {ECO:0000259|PROSITE:PS50880}. FT REGION 166 171 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT REGION 757 791 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT ACT_SITE 314 314 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00952}. FT SITE 33 33 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 138 138 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 139 139 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 142 142 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 147 147 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 316 316 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 508 508 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. SQ SEQUENCE 863 AA; 97380 MW; AEC5467F39A39792 CRC64; MGKALIIVES PAKIKTLRKF LGANYVFESS IGHIRDLPEK EFGIDIENDF EPKYVVMPDK EKVIANLRKA AKECDIVYLS PDPDREGEAI AWHITQILPP STKIKRVSFN SITKEAVVKA LESPRGIDIA LVNAQQARRL LDRIVGYKIS PILNRRIQRG KEGFVSAGRV QSVALKLVVD REKEIEIFKP VEYWNLGAIL KTEEDPKNFR ANLHLVGGKR IEKELIEGKE VILIDTKEKA DEILARLKGQ SFQVVKVEKK EKKRNPVPPF ITSTLQQEAS RHYGFSSAKT MNIAQTLYEG VELGNEGAEG LITYMRTDSV RIAPEALEEV RSLILKQFGK DFLPADPKNY ATSKSAQDAH EAIRPANLMH APEAIKDYLS REQFLLYQLI WKRFIASQMM PAIYDTVSAD IAAGKEFILR ATGSIMKFQG FLAIYEEKED DEDKTDEARM LPQLTEGQFL KLLELTSEQA FTRPPPRFTE ASLVKELEKC RIGRPSTYAA IMNKIQSRDY TTKENGRLKP TELGIVIAQM LESNFQEIMN IGFTASMEDG LEAIAENQQD WKGLIRDFWV KFLPTLDEAE KSAFVPKVMT DIDCPTCGSK LQKIWFKSKY FYGCSRYPDC NFTAPLEEIA FNKEDYASDF DWEQKCPECQ SDMKVRHGRF GAFLGCTRYP DCKGIINIPK KGETIIPAED MPHCVAIGCT GHMVARKSRF GKTFYSCSTF PECDVIVNDL AQLSEKYPEH PRTAYIKKAG KGKKGAVKKT VAKKSTATKA APKKAAVKKT ATPRQQPQQQ LSAELSQVVG AAEMSRGEVM KKVWEYIHAH HLQDTTNKRQ INPDVLLGKV IGSEPIDMFK MTAALGKHIH KKT //