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Entry: A0A2S0U912_9BACL
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ID   A0A2S0U912_9BACL        Unreviewed;       701 AA.
AC   A0A2S0U912;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=DCC85_08680 {ECO:0000313|EMBL:AWB44285.1};
OS   Paenibacillus sp. CAA11.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1532905 {ECO:0000313|EMBL:AWB44285.1, ECO:0000313|Proteomes:UP000244407};
RN   [1] {ECO:0000313|EMBL:AWB44285.1, ECO:0000313|Proteomes:UP000244407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAA11 {ECO:0000313|EMBL:AWB44285.1,
RC   ECO:0000313|Proteomes:UP000244407};
RA   Um Y., Kim S., Gong G.;
RT   "Complete genome of CAA11.";
RL   Submitted (APR-2018) 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; CP028922; AWB44285.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S0U912; -.
DR   OrthoDB; 9804262at2; -.
DR   Proteomes; UP000244407; 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; 2.
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; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR   PANTHER; PTHR42785:SF1; OMEGA-PROTEIN; 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; 1.
DR   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000244407};
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..114
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          163..168
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   COILED          546..573
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        298
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            33
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            140
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            148
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            155
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            300
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            492
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ   SEQUENCE   701 AA;  79287 MW;  3B269B9CF11AD5C4 CRC64;
     MADSLVIVES PAKAKTIGKY LGSKYIVKAS MGHVRDLPKS QIGVEVENDF NPKYITIRGK
     GSVLKELKDA RKKVKKVYLA ADPDREGEAI AWHLAHVLDL DQTEDCRVVF NEITKQAVKD
     AFKTPRKINM DLVNAQQARR ILDRLVGYKI SPLLWKKVKK GLSAGRVQSV AVKIILDREN
     EIAAFEPEEY WSITAGLKIA ESTFEAKFHQ YQGEKKELSS EADVKQILQA IEGASFVVQN
     VKEKERLRHP SPPFTTSSLQ QEAARKLNFR AAKTMSVAQQ LYEGVDLGKE GTVGLITYMR
     TDSTRIAASA QEEAREYITG KYGADYTPET PRQYSKKAAN AQDAHEAIRP TAALRDPESI
     KPILSRDQFR LYKLIWERFM ASQMASAILD TLSVDIRANE VTFRAVGSKV RFPGFMKVYV
     EGNDDGNAVE DDKFLPPLKS GDELVTESIE PKQHFTQPPP RYTEARLVKT LEELGIGRPS
     TYAPTLETIQ KRGYVAVEEK KFMPTELGEL VIEQMEQFFP EILNVEFTAN MEGDLDHVEE
     GSEDWVRVLN EFYESFEKRL EVAEEEMKEI EIEDEVSDEI CEKCGNPMVY KLGRFGKFLA
     CSGFPDCRNT KPIIKDIGVT CPKCKEGHVV ERRSKKGRVF YGCNRYPECD FVSWDKPSTK
     PCPSCGSLMV EKRSKQGIKL QCTSCDHSEM VEEDQEETAE L
//
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