ID   TOP1_PSEAE              Reviewed;         868 AA.
AC   Q9HZJ5;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 144.
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}; OrderedLocusNames=PA3011;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00952}.
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DR   EMBL; AE004091; AAG06399.1; -; Genomic_DNA.
DR   PIR; D83269; D83269.
DR   RefSeq; NP_251701.1; NC_002516.2.
DR   RefSeq; WP_003091201.1; NZ_QZGE01000009.1.
DR   AlphaFoldDB; Q9HZJ5; -.
DR   SMR; Q9HZJ5; -.
DR   STRING; 208964.PA3011; -.
DR   PaxDb; 208964-PA3011; -.
DR   GeneID; 880353; -.
DR   KEGG; pae:PA3011; -.
DR   PATRIC; fig|208964.12.peg.3159; -.
DR   PseudoCAP; PA3011; -.
DR   HOGENOM; CLU_002929_4_3_6; -.
DR   InParanoid; Q9HZJ5; -.
DR   OrthoDB; 9804262at2; -.
DR   PhylomeDB; Q9HZJ5; -.
DR   BioCyc; PAER208964:G1FZ6-3063-MONOMER; -.
DR   Proteomes; UP000002438; 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; 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_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; 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; TOPO_IA_1; 1.
DR   PROSITE; PS52039; TOPO_IA_2; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Isomerase; Magnesium; Metal-binding; Reference proteome;
KW   Repeat; Topoisomerase; Zinc; Zinc-finger.
FT   CHAIN           1..868
FT                   /note="DNA topoisomerase 1"
FT                   /id="PRO_0000145161"
FT   DOMAIN          3..147
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   DOMAIN          163..580
FT                   /note="Topo IA-type catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
FT   ZN_FING         602..633
FT                   /note="C4-type 1"
FT   ZN_FING         664..691
FT                   /note="C4-type 2"
FT   ZN_FING         713..738
FT                   /note="C4-type 3"
FT   REGION          34..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..202
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   COMPBIAS        35..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        324
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            33
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            173
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            174
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            177
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            182
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            189
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            326
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT   SITE            512
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
SQ   SEQUENCE   868 AA;  97283 MW;  5EB4B8483366C89B CRC64;
     MGKSLVIVES PAKAKTINKY LGSQYVVKSS IGHIRDLPTS GSSSSKEPAA KGRKSASEAP
     ALSPKEKARR QLVSRMGVDP EHGWKAKYEI LPGKEKVIDE LRRLAKDADT VYLATDLDRE
     GEAIAWHLRE AIGGDESRYK RVVFNEITKK AIQEAFSQPG ELDINRVNAQ QARRFLDRVV
     GYMVSPLLWQ KIARGLSAGR VQSVAVKLVV EREREIRAFV PEEYWEVHAD LGTAKGANVR
     FEVTREKGEA FKPLNEAQAM AALEKLKASA YSVAKREDRP TSSRPSAPFI TSTLQQAASN
     RLGFGVKKTM MMAQRLYEAG YITYMRTDST NLSADAIGMV RGFIEDEFGQ KYLPGKANVY
     SSKEGAQEAH EAIRPSDVNL KPTQLSGMER DAERLYDLIW RQFVACQMTP AEYLSTSVSV
     TAGDFELRAK GRILKFDGYT RVLPQQSKPG EDDVLPEMKE GENLKLIKLD PSQHFTKPPA
     RYSEASLVKE LEKRGIGRPS TYAAIISTIQ ERGYVTTHNR RFYAEKMGDI VTDRLNESFA
     NLMDYGFTAG MEEHLDDVAQ GERDWKHLLD EFYGDFKKKL EVAEVSEKGM RANQPTLTNI
     PCRECGRPMM IRTASTGVFL GCSGYSLPPK ERCKATVNLI PGDEIAADDE GESESRVLRG
     KHRCPICSTA MDAYLLDEKH KLHICGNNPD CPGYEIEEGQ YRIKGYEGPS LECDKCGSEM
     QLKTGRFGKF FGCTNPTCKN TRKLLKNGEA APPKMDAIRM PELKCEKVDD IYVLRDGASG
     MFLAASQFPK NRETRAPLVS EIIPHKAELD PKYHYLCDAP QKDPDGRPAV IRFSRKTKEQ
     YVQSEVDGKP TGWRAFYDGG KWKVEDKR
//