ID   A0A0U3J234_ENTCL        Unreviewed;       865 AA.
AC   A0A0U3J234;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   27-NOV-2024, entry version 16.
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; Pseudomonadota; 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}.
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DR   EMBL; KT884517; ALV83374.1; -; Genomic_DNA.
DR   RefSeq; WP_003856806.1; NZ_PEHU01000016.1.
DR   AlphaFoldDB; A0A0U3J234; -.
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   FunFam; 1.10.290.10:FF:000002; DNA topoisomerase 1; 1.
DR   FunFam; 2.20.25.10:FF:000013; DNA topoisomerase 1; 1.
DR   FunFam; 3.30.65.10:FF:000001; DNA topoisomerase 1; 1.
DR   FunFam; 3.30.65.10:FF:000002; DNA topoisomerase 1; 1.
DR   FunFam; 3.30.65.10:FF:000003; DNA topoisomerase 1; 1.
DR   FunFam; 3.40.50.140:FF:000001; DNA topoisomerase 1; 1.
DR   Gene3D; 2.20.25.10; -; 1.
DR   Gene3D; 3.40.50.140; -; 1.
DR   Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 3.
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; 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; 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_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   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; 3.
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
//