ID A0AAJ0Z929_9ENTR Unreviewed; 865 AA. AC A0AAJ0Z929; DT 24-JUL-2024, integrated into UniProtKB/TrEMBL. DT 24-JUL-2024, sequence version 1. DT 02-OCT-2024, entry version 2. 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 ECO:0000313|EMBL:MBU3766780.1}; GN ORFNames=J0A64_09210 {ECO:0000313|EMBL:MBU3766780.1}; OS Enterobacter roggenkampii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=1812935 {ECO:0000313|EMBL:MBU3766780.1, ECO:0000313|Proteomes:UP000813349}; RN [1] {ECO:0000313|EMBL:MBU3766780.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BK34275 {ECO:0000313|EMBL:MBU3766780.1}; RX PubMed=34079986; DOI=10.1093/cid/ciab511; RA Klein S., Boutin S., Kocer K., Fiedler M.O., Storzinger D., Weigand M.A., RA Tan B., Richter D., Rupp C., Mieth M., Mehrabi A., Hackert T., RA Zimmermann S., Heeg K., Nurjadi D.; RT "Rapid Development of Cefiderocol Resistance in Carbapenem-resistant RT Enterobacter cloacae During Therapy Is Associated With Heterogeneous RT Mutations in the Catecholate Siderophore Receptor cirA."; RL Clin. Infect. Dis. 74:905-908(2022). 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: 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:MBU3766780.1}. 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; JAFKCP010000004; MBU3766780.1; -; Genomic_DNA. DR Proteomes; UP000813349; Unassembled WGS sequence. DR CDD; cd00186; TOP1Ac; 1. DR CDD; cd03363; TOPRIM_TopoIA_TopoI; 1. DR HAMAP; MF_00952; Topoisom_1_prok; 1. DR InterPro; IPR049330; TOP1_Znf. 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; 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_dom. 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; PF21372; TOP1_ZnF; 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 SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00952}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00952}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00952}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 3..142 FT /note="Toprim" FT /evidence="ECO:0000259|PROSITE:PS50880" FT REGION 36..65 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 192..197 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT COMPBIAS 36..50 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 51..65 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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; 97327 MW; BC23B72F208900E9 CRC64; MGKALVIVES PAKAKTINKY LGNDYVVKSS VGHIRDLPTS GSASKKSADS TSTKGAKKPK KDERSALVNR MGVNPWHNWD AQYEVLPGKE KVVNELKQLA EKADHIYLAT DLDREGEAIA WHLREVIGGD DKRYSRVVFN EITKNAIRQA FEKPGELNID RVNAQQARRF MDRVVGYMVS PLLWKKIARG LSAGRVQSVA VRLVVERERE IKAFVPEEFW EVDANVTTPG GDALPLQVSH QNDKPFRPEN RDQTMAAVAL LEKARYQVLE REDKPTSSKP GAPFITSTLQ QAASTRLGYG VKKTMMMAQR LYEAGYITYM RTDSTNLSQD AVNMVRGYIS DNFGKKYLPE SANQFASKEN SQEAHEAIRP SDVSVLAESL KDMEADAQKL YQLIWRQFVA CQMTPAQYDS TTLTVGAGDF RLKVRGRILR FDGWTKVMPA LRKGDEDRTL PAVNKGDELS LVELIPAQHF TKPPARFSEA SLVKELEKRG IGRPSTYASI ISTIQDRGYV RVENRRFYAE KMGEIVTDRL EANFRELMNY DFTAQMEDSL DQVASHQAEW KKVLDSFFSD FTDQLEKAEK DPEEGGMLPN QMVLTSIDCP TCGRKMGIRT ATTGVFLGCS GYALSPKERC KTTINLVPEN EVLNVLEGDD AETNALRAKR RCKKCGTAMD SYLIDPKRKL HVCGNNPTCD GYEIEEGEFR IKGYDGPIVE CEKCGSEMHL KMGRFGKYMA CTNDECKNTR KILRNGEVAP PKEDPVPLPE LPCEKSDAYF VLRDGAAGVF LAANTFPKSR ETRAPLVEEL YRFRDRLPEK LRYLADAPQQ DPEGNKTVVR FSRKTKQQYV AAEKEGKATG WSAFFVDGKW VEGKK //