ID   Q9PLT3_CHLMU            Unreviewed;       865 AA.
AC   Q9PLT3;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   02-SEP-2026, entry version 161.
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:AAF38905.1};
GN   OrderedLocusNames=TC_0012 {ECO:0000313|EMBL:AAF38905.1};
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
OC   Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161 {ECO:0000313|EMBL:AAF38905.1, ECO:0000313|Proteomes:UP000000800};
RN   [1] {ECO:0000313|EMBL:AAF38905.1, ECO:0000313|Proteomes:UP000000800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg {ECO:0000313|Proteomes:UP000000800};
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(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: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, ECO:0000256|PROSITE-ProRule:PRU10131};
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       ECO:0000256|PROSITE-ProRule:PRU01383}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00952,
CC       ECO:0000256|PROSITE-ProRule:PRU00995}.
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DR   EMBL; AE002160; AAF38905.1; -; Genomic_DNA.
DR   PIR; H81749; H81749.
DR   RefSeq; WP_010229101.1; NC_002620.2.
DR   AlphaFoldDB; Q9PLT3; -.
DR   GeneID; 1245536; -.
DR   KEGG; cmu:TC_0012; -.
DR   PATRIC; fig|243161.6.peg.22; -.
DR   eggNOG; COG0550; Bacteria.
DR   HOGENOM; CLU_002929_4_3_0; -.
DR   OrthoDB; 9804262at2; -.
DR   Proteomes; UP000000800; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   CDD; cd10567; SWIB-MDM2_like; 1.
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; 1.10.245.10; SWIB/MDM2 domain; 1.
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; IPR019835; SWIB_domain.
DR   InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR   InterPro; IPR003121; SWIB_MDM2_domain.
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_dom.
DR   InterPro; IPR034149; TOPRIM_TopoI.
DR   NCBIfam; NF004966; PRK06319.1; 1.
DR   NCBIfam; TIGR01051; topA_bact; 1.
DR   PANTHER; PTHR42785:SF1; DNA TOPOISOMERASE; 1.
DR   PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR   Pfam; PF02201; SWIB; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF01396; Zn_ribbon_Top1; 3.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00151; SWIB; 1.
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; SSF47592; SWIB/MDM2 domain; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS51925; SWIB_MDM2; 1.
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 {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   Reference proteome {ECO:0000313|Proteomes:UP000000800};
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   DOMAIN          3..112
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   DOMAIN          128..577
FT                   /note="Topo IA-type catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS52039"
FT   DOMAIN          785..863
FT                   /note="DM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51925"
FT   REGION          164..169
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   REGION          752..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..766
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        773..786
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        315
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952,
FT                   ECO:0000256|PROSITE-ProRule:PRU10131"
FT   SITE            33
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            138
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            139
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            142
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            147
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            317
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            509
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ   SEQUENCE   865 AA;  97933 MW;  4A3588647BC39755 CRC64;
     MKKSLIIVES PAKIKTLRKL LGEGFIFDSS LGHIVDLPAK GFGIDIEKGF IPDYQILEGK
     EEVIRKICAE AKKCDVVYLA PDPDREGEAI AWHIANQLPK NTKIQRISFN AITKGAVTEA
     LKHPREIDMA LVNAQQARRF LDRIVGYKIS PILGRKLQRW SGVSAGRVQS VALKLVVDRE
     YAIEQFVPVE FWNIRVNLQD PKSQKTFWAH LHSVNGKKWE KEIPEGKSSE DVVLIDSKEK
     ADDLVSLLES ATYCVDRVES KEKKRNAYPP FITSTLQQEA SRHYRFSSSR TMNIAQTLYE
     GVDLDSQGAV GLITYMRTDS VRTDPEAIKQ VRKYIENHFG KEYVPSSPNM YATKKMAQDA
     HEAIRPTDVS LSPESIRTKL TEDQYKLYSL IWKRFVASQM IAAIYDTLAI QIATNKGIDL
     RATGSCLKFK GFLAVYEEKR DEEGDEDENI QLPKLHERDE LKKEEIEAEQ SHTKPLPRFT
     EASLVKELEK SGIGRPSTYA TIMNKIQSRE YTLKEGQRLR PTELGKVVCQ FLETNFPRIM
     DIGFTAKMED ELELIADNKK PWKQLLQEFC ELFLPFVVTA EKEAFIPRIV TEMDCPRCHK
     GKLVKIWSKN RYFFGCSEYP TCDYKTSEEE LTFDKSEYAD DTPWDAPCAL CGGQMKVRHG
     KFGSFLGCEN YPQCHYIVNL FKKGEAGSEP EEIVSCPAEG CTGHLVKRRS RFNKMFYSCS
     EYPACSVIGN SVDAVIEKYT GTPKTPYEKK IKAKKATASK KGKATKGKAS TTKTKKKSTV
     TTKNRKTATY TPSSALAAVI GPDPIDGFPE ATKKIWAYIK EQGLQSPNNK RVIVPDSKMK
     HVIGDDPIDM FALSKKIQAH LTKQE
//