ID A0A0B7IVX6_9PROT Unreviewed; 864 AA.
AC A0A0B7IVX6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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:CEN55232.1};
GN ORFNames=BN1209_0178 {ECO:0000313|EMBL:CEN55232.1};
OS Candidatus Methylopumilus turicensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylopumilus.
OX NCBI_TaxID=1581680 {ECO:0000313|EMBL:CEN55232.1, ECO:0000313|Proteomes:UP000056322};
RN [1] {ECO:0000313|Proteomes:UP000056322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-10A-171 {ECO:0000313|Proteomes:UP000056322};
RA Salcher M.M.;
RL Submitted (DEC-2014) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00952}.
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DR EMBL; LN794158; CEN55232.1; -; Genomic_DNA.
DR RefSeq; WP_045750540.1; NZ_LN794158.1.
DR AlphaFoldDB; A0A0B7IVX6; -.
DR STRING; 1581680.BN1209_0178; -.
DR KEGG; mbac:BN1209_0178; -.
DR HOGENOM; CLU_002929_3_2_4; -.
DR OrthoDB; 9803554at2; -.
DR Proteomes; UP000056322; Chromosome 1.
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; 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; IPR013498; Topo_IA_Znf.
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; 3.
DR Pfam; PF01396; zf-C4_Topoisom; 1.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000056322};
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 2..112
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 166..171
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT ACT_SITE 306
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 32
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 143
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 146
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 158
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 308
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 501
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ SEQUENCE 864 AA; 96113 MW; 4BF39DAB3D83EA4E CRC64;
MSKLLIVESP SKAKTLEKYL GKEFKVLASY GHVRDLIPKS GAVDTDNDFA MKYEIIDRNS
KHVDAITRAV KDADAIYLAT DPDREGEAIS WHIAEILKSK NLVKNKLMKR VVFHEITKTA
VQHAIDEPRD ILMPLVNAQQ ARRALDYLVG FNLSPLLWKK IRRGLSAGRV QSPALRLIVE
RELEIEAFKS QEYWSIHLES RKHQHAFDAK LIQLDGKKVE QFTVINQDQQ ADIVGELLLK
SAGKTTVSRV EKKQRSRSPA APFTTSTLQQ EAVRKLGFTT SRAMRIAQQL YEGIDTGGGA
VGLITYMRTD SFSLAAEAIA QIRGYIKDNY SAEYLPKLPI AYKTKSKNAQ EAHEAIRPTD
ISRTPTSVEQ FLTPEQFKLY EMIWKRSVAC QMAPAKFDAV SVDLSVGSDA NLFRATGQTL
VFPGFMGVYM EGVDDAEEEN ETKLPVLETG EILDVQKIFG DQHFTEPPPR YGEASLVKVL
EEYGIGRPST YASIISTLQD REYVLLDKKR FTPTDVGRVV NKFLTDHFTR YVDYDFTANL
ENKLDSVADG EHEWIPLLKE FWDGLHKQID DKKDVERPGT ELIDEACPKC GKQLSKQLSR
YGSFIGCTGY NDTPKCDYKR NVDGAAAISS EPIVMGLDAA SGKDILLLNG PYGPYLQLGL
PEADAKKKPK RVSIPKDIPF ANVNLDIALQ LIALPRDLGL HPETNKKVIA NIGRFGPYVN
HDAKFKSIPK TDSVFDIDLP RAVELLAQAN TGPAPIRELG NHPTEDGQIA IYAGRYGPYV
QHGKVRATIA KSEDPESLTL EEALELLAAK VLKDAPAKKK PTAKKVAAKK TVVKKAVVKK
TAVKKVTPKK TVAKKAAVKK TATE
//
