ID A0A0U3J234_ENTCL Unreviewed; 865 AA. AC A0A0U3J234; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 19-JAN-2022, entry version 6. 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}; OS Enterobacter cloacae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=550 {ECO:0000313|EMBL:ALV83374.1}; RN [1] {ECO:0000313|EMBL:ALV83374.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=G6809 {ECO:0000313|EMBL:ALV83374.1}; RX PubMed=26719440; RA Thomson G.K., Snyder J.W., McElheny C.L., Thomson K.S., Doi Y.; RT "Co-Production of KPC-18 and VIM-1 Carbapenemases by Enterobacter cloacae: RT Implications for Newer beta-Lactam-beta-Lactamase Inhibitor Combinations."; RL J. Clin. Microbiol. 0:0-0(2015). 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; KT884517; ALV83374.1; -; Genomic_DNA. DR RefSeq; WP_003856806.1; NZ_PEHU01000016.1. DR GeneID; 60948050; -. DR PATRIC; fig|550.257.peg.4084; -. 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; 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; 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; IPR013263; TopoI_Znr_bac. DR InterPro; IPR028612; Topoisom_1_IA. DR InterPro; IPR006171; TOPRIM_domain. DR InterPro; IPR034149; TOPRIM_TopoI. DR PANTHER; PTHR42785; PTHR42785; 1. DR Pfam; PF08272; Topo_Zn_Ribbon; 2. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR Pfam; PF01396; zf-C4_Topoisom; 2. 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; 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 REGION 192..197 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT ACT_SITE 319 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 168 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 169 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 172 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 177 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 184 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 321 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 507 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" SQ SEQUENCE 865 AA; 97333 MW; 67DB0CBCFC434058 CRC64; MGKALVIVES PAKAKTINKY LGNDYVVKSS VGHIRDLPTS GSASKKSADS TSTKGAKKPK KDERSALVNR MGVNPWHNWD AHYEVLPGKE KVVNELKQLA EKADHIYLAT DLDREGEAIA WHLREVIGGD DKRYSRVVFN EITKNAIRQA FEKPGELNID RVNAQQARRF MDRVVGYMVS PLLWKKVARG LSAGRVQSVA VRLVVERERE IKAFVPEEFW EVDANVTTPG GDALPLQVSH HNDKPFRPEN RDQTMAAVAL LEKARYQVLD REDKPTSSKP GAPFITSTLQ QAASTRLGYG VKKTMMMAQR LYEAGYITYM RTDSTNLSQD AVNMVRGYIE DNFGKKYLPD SPNQYASKEN SQEAHEAIRP SDVSVLAESL KDMEADAQKL YQLIWRQFVA CQMTPAKYDS TTLTVGAGDF RLKARGRILR FDGWTKVMPA LRKGDEDRTL PSVNKGDELS LVDLVPAQHF TKPPARFSEA SLVKELEKRG IGRPSTYASI ISTIQDRGYV RVENRRFYAE KMGEIVTDRL EANFRELMNY DFTAQMEDSL DEVASHKAEW KKVLDSFFSD FTNQLEKAEK DPEEGGMLPN QMVLTSIDCP TCGRKMGIRT ATTGVFLGCS GYALSPKERC KTTINLVPEN EVLNVLEGDD AETNALRAKR RCKKCGTAMD SYLIDPKRKL HVCGNNPTCD GYEIEEGEFR IKGYDGPIVE CEKCGSEMHL KMGRFGKYMA CTNDDCKNTR KILRNGEVAP PKEDPVPLPE LPCEKSDAYF VLRDGAAGVF LAANTFPKSR ETRAPLVEEL YRFRDRLPEK LRYLADAPQQ DPEGNKTVVR FSRKTKQQYV AAEKEGKATG WSAFFVDGKW VEGKK //