ID A0A0A8EM99_9ACTN Unreviewed; 947 AA.
AC A0A0A8EM99;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
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 ORFNames=GZL_04341 {ECO:0000313|EMBL:AJC56919.1};
OS Streptomyces sp. 769.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1262452 {ECO:0000313|EMBL:AJC56919.1, ECO:0000313|Proteomes:UP000031113};
RN [1] {ECO:0000313|EMBL:AJC56919.1, ECO:0000313|Proteomes:UP000031113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=769 {ECO:0000313|EMBL:AJC56919.1,
RC ECO:0000313|Proteomes:UP000031113};
RA Du Q., Wang Q., Li Q., Wang L., Zhang Z., Ren J., Wang J., Wang M.;
RT "Complete Genome Sequence of Streptomyces gongzhulingensis.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003987; AJC56919.1; -; Genomic_DNA.
DR RefSeq; WP_039634246.1; NZ_CP003987.1.
DR AlphaFoldDB; A0A0A8EM99; -.
DR KEGG; stre:GZL_04341; -.
DR HOGENOM; CLU_002929_2_0_11; -.
DR Proteomes; UP000031113; Chromosome.
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; 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; IPR005733; TopoI_bac-type.
DR InterPro; IPR028612; Topoisom_1_IA.
DR InterPro; IPR025589; Toprim_C_rpt.
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; PF13368; Toprim_C_rpt; 4.
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 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}.
FT DOMAIN 13..137
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 186..191
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT REGION 874..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..924
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 336
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 43
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 162
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 163
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 166
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 171
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 178
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 338
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 536
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ SEQUENCE 947 AA; 103021 MW; BC6757D71DEDF8F0 CRC64;
MSPTSETAEG GGRRLVIVES PAKAKTIKGY LGPGYVVEAS VGHIRDLPNG AAEVPAKYKG
ESWARLGVNV DADFQPIYVV NTDKKDQVKK LKALLAESDE LFLATDEDRE GEAIAWHLQE
ILKPKVPVHR MVFHEITKDA IREAVANPRD LNQKLVDAQE TRRILDRLYG YEVSPVLWKK
VMPRLSAGRV QSVATRLVVE RERERIAFRS AEYWDLTGTF STGRAGDTSD PSTLTARLNS
VDGRRVAQGR DFGPNGQLKN ADVLHLDEAN ARALAAALAD TQFSVRSVES KPYRRSPYAP
FRTTTLQQEA SRKLGFGAKA TMQVAQKLYE NGFITYMRTD STTLSDTAVA AARAQVTQLY
GAGYLPDKPR TYAGKVKNAQ EAHEAIRPSG DRFRTPAETG LTGDQFRLYE LIWKRTVASQ
MKDATGNSVT VKIGGRAADG RDTEFSASGK TITFHGFLKA YVEGADDPNA ELDDRERRLP
QVAEGDALTA QEITADGHAT KPPARYTEAT LVKELEEREI GRPSTYASII GTILDRGYVF
KKGTALVPSF LSFAVVNLLE KHFGRLVDYD FTAKMEDDLD RIARGEAQAV PWLRRFYFGE
GAGAGESGAA DAGNGDGDHL GGLKELVTDL GAIDAREISS FPVGNGVTLR VGRYGPYVER
GEKDEEGHQR ADVPDDLAPD ELTVEYAEEL LAKPSGDYEL GMDPESGHQI VAKDGRYGPY
VTEVLPEGTP KTGKNAVKPR TASLFKSMSL DTVTLADALK LMSLPRVVGT DAEGVEITAQ
NGRYGPYLKK GTDSRSLERE EQLFTITLDE ALAIYAQPKQ RGRAAAKPPL KELGTDPVSG
KPVVVKDGRF GAYVTDGETN ATLRRDDDVE TITPERGYEL LAEKRAKGPA KKTAAKKTAA
KKTTAKKTTA KKTAAKKTAA KKTTAKKAAT KTAAKTAAKK TAAPAED
//
