ID   TOP1_HELPY              Reviewed;         736 AA.
AC   P55991;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=DNA topoisomerase 1 {ECO:0000255|HAMAP-Rule:MF_00952};
DE            EC=5.6.2.1 {ECO:0000255|HAMAP-Rule:MF_00952};
DE   AltName: Full=DNA topoisomerase I {ECO:0000255|HAMAP-Rule:MF_00952};
DE   AltName: Full=Omega-protein;
DE   AltName: Full=Relaxing enzyme;
DE   AltName: Full=Swivelase;
DE   AltName: Full=Untwisting enzyme;
GN   Name=topA {ECO:0000255|HAMAP-Rule:MF_00952};
GN   OrderedLocusNames=HP_0116;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00952};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00952};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00952}.
CC   -!- INTERACTION:
CC       P55991; O26081: HP_1559; NbExp=3; IntAct=EBI-7493738, EBI-7500288;
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00952}.
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DR   EMBL; AE000511; AAD07184.1; -; Genomic_DNA.
DR   PIR; D64534; D64534.
DR   RefSeq; NP_206916.1; NC_000915.1.
DR   RefSeq; WP_000681408.1; NC_018939.1.
DR   AlphaFoldDB; P55991; -.
DR   SMR; P55991; -.
DR   DIP; DIP-3057N; -.
DR   IntAct; P55991; 16.
DR   MINT; P55991; -.
DR   STRING; 85962.HP_0116; -.
DR   PaxDb; 85962-C694_00575; -.
DR   EnsemblBacteria; AAD07184; AAD07184; HP_0116.
DR   KEGG; hpy:HP_0116; -.
DR   PATRIC; fig|85962.47.peg.125; -.
DR   eggNOG; COG0550; Bacteria.
DR   eggNOG; COG0551; Bacteria.
DR   InParanoid; P55991; -.
DR   OrthoDB; 9804262at2; -.
DR   PhylomeDB; P55991; -.
DR   Proteomes; UP000000429; Chromosome.
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; 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; 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:SF1; DNA TOPOISOMERASE; 1.
DR   PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 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; 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; TOPO_IA_1; 1.
DR   PROSITE; PS52039; TOPO_IA_2; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Isomerase; Magnesium; Metal-binding; Reference proteome;
KW   Repeat; Topoisomerase; Zinc; Zinc-finger.
FT   CHAIN           1..736
FT                   /note="DNA topoisomerase 1"
FT                   /id="PRO_0000145150"
FT   DOMAIN          2..113
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   DOMAIN          129..552
FT                   /note="Topo IA-type catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
FT   ZN_FING         572..598
FT                   /note="C4-type 1"
FT   ZN_FING         616..642
FT                   /note="C4-type 2"
FT   ZN_FING         663..689
FT                   /note="C4-type 3"
FT   ZN_FING         702..725
FT                   /note="C4-type 4"
FT   REGION          163..168
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   ACT_SITE        297
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   BINDING         82
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            32
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            139
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            140
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            143
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            299
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            484
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
SQ   SEQUENCE   736 AA;  83196 MW;  357CE39735F48475 CRC64;
     MKHLIIVESP AKAKTIKNFL DKNYEVIASK GHVRDLSKFA LGIKIDETGF TPNYVVDKDH
     KELVKQIIEL SKKASITYIA TDEDREGEAI GYHVACLIGG KLESYPRIVF HEITQNAILN
     ALKTPRKIDM SKVNAQQARR FLDRIVGFKL SSLIASKITK GLSAGRVQSA ALKLVIDKER
     EIKAFKPLTY FTLDAYFESH LEAQLISYKG NKLKAQELID EKKAQEIKNE LEKESYAISS
     IVKKSKKSPT PPPFMTSTLQ QSASSLLGFS PTKTMSIAQK LYEGVATPQG VMGVITYMRT
     DSLNIAKEAL EEARNKILKD YGKDYLPPKA KVYSSKNKNA QEAHEAIRPT SIILEPNALK
     DYLKPEELRL YTLIYKRFLA SQMQDALFES QSVVVACEKG EFKASGRKLL FDGYYKILGN
     DDKDKLLPNL KENDPIKLEK LESNAHVTEP PARYSEASLI KVLESLGIGR PSTYAPTISL
     LQNRDYIKVE KKQISALESA FKVIEILEKH FEEIVDSKFS ASLEEELDNI AQNKADYQQV
     LKDFYYPFMD KIEAGKKNII SQKVHEKTGQ SCPKCGGELV KKNSRYGEFI ACNNYPKCKY
     VKQTESANDE ADQELCEKCG GEMVQKFSRN GAFLACNNYP ECKNTKSLKN TPNAKETIEG
     VKCPECGGDI ALKRSKKGSF YGCNNYPKCN FLSNHKPINK RCEKCHYLMS ERIYRKKKAH
     ECIKCKERVF LEEDNG
//