ID A0A2H9SV32_9BACT Unreviewed; 863 AA. AC A0A2H9SV32; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 13-SEP-2023, entry version 23. 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; Chlamydiota; Chlamydiia; 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, 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00952}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; A0A2H9SV32; -. DR EnsemblBacteria; PJD97551; PJD97551; CK425_02690. 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 (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; cd10567; SWIB-MDM2_like; 1. 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; 3. DR Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1. 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; 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 NCBIfam; TIGR01051; topA_bact; 1. DR PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1. DR PANTHER; PTHR42785:SF1; OMEGA-PROTEIN; 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; SSF56712; Prokaryotic type I DNA topoisomerase; 1. DR SUPFAM; SSF47592; SWIB/MDM2 domain; 1. DR SUPFAM; SSF57783; Zinc beta-ribbon; 2. DR PROSITE; PS51925; SWIB_MDM2; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 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 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 3..113 FT /note="Toprim" FT /evidence="ECO:0000259|PROSITE:PS50880" FT DOMAIN 784..861 FT /note="DM2" FT /evidence="ECO:0000259|PROSITE:PS51925" FT REGION 166..171 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT REGION 757..791 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 314 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 33 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 138 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 139 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 142 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 147 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 316 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 508 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-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 //