ID D0J9D6_BLASP Unreviewed; 698 AA.
AC D0J9D6;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
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:ACX83957.1};
GN OrderedLocusNames=BPLAN_339 {ECO:0000313|EMBL:ACX83957.1};
OS Blattabacterium sp. subsp. Periplaneta americana (strain BPLAN)
OS (Periplaneta americana symbiotic bacterium).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Blattabacteriaceae; Blattabacterium.
OX NCBI_TaxID=600809 {ECO:0000313|EMBL:ACX83957.1, ECO:0000313|Proteomes:UP000002225};
RN [1] {ECO:0000313|EMBL:ACX83957.1, ECO:0000313|Proteomes:UP000002225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPLAN {ECO:0000313|EMBL:ACX83957.1,
RC ECO:0000313|Proteomes:UP000002225};
RX PubMed=19880743; DOI=10.1073/pnas.0907504106;
RA Sabree Z.L., Kambhampati S., Moran N.A.;
RT "Nitrogen recycling and nutritional provisioning by Blattabacterium, the
RT cockroach endosymbiont.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19521-19526(2009).
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; CP001429; ACX83957.1; -; Genomic_DNA.
DR RefSeq; WP_012821484.1; NC_013418.2.
DR AlphaFoldDB; D0J9D6; -.
DR STRING; 600809.BPLAN_339; -.
DR KEGG; bpi:BPLAN_339; -.
DR eggNOG; COG0550; Bacteria.
DR HOGENOM; CLU_002929_3_2_10; -.
DR OrthoDB; 9804262at2; -.
DR Proteomes; UP000002225; 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; 2.
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; 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; 2.
DR Pfam; PF01751; Toprim; 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 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:UP000002225};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00952}.
FT DOMAIN 3..113
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 ACT_SITE 284
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 155
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 286
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 471
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ SEQUENCE 698 AA; 81433 MW; A36E01711F150023 CRC64;
MKKNLVIVES PTKANTIQLF LGKEFYVVPS YGHIIDLPEK KIGIDINKDF QPNYAILPKK
RKIVQNLKTL IKDFNLIWLA SDEDREGEAI AYQIYRILNI PSEKFRRIVF HEITKKAILH
AIKNPRLINH NLVYAQQARR ILDRLVGFQL SPILWKKINA GLSAGRVQSA ALRLIVEREQ
NIQNFIPISG YQIFGIFTNK NKITLNAKLE KKIEGEKKMK NILQACVDSS FFIKKIVTKQ
EKKTPPPPFT TSSLQQEACK KLNFSISKTM FLAQKLYEKG YITYMRTDST NLSKDVLSEI
KNYILSSYGK SYLSPKEFSS KKKFSQEAHE AIHPTNIEKN SLEDLDTSQK ILYKLIWERT
LIGQMTDANI EKKIFYIQSS NFEIPFVFTE KTIIFDGFMK IHGKEDFKKK ETNLSEIKKG
TLLQKKVITA KQVFTKHLPR YNEASLVKNL EKLGIGRPST YVPIISTIQK RNYVNLQKSI
NKKEYRESFI LKKNIIIEKK DEITEIEKNK FIPTEIGVLT TNFLKKNFHE IVDYDFTANL
EKEFDNIAKG EVSWKRIIKN FYDRFHEKIE HVEKNVKKFI KNVFLGIDPI SKKKIFSQVA
RFGPIVQMGE FKDKEKPKFS PLLINQKIDT ISLETALKLL ELPKILGIFE EEEVLLKVNK
YNVYIRHKNK SIPIEEKIFF NSFHLKDAID VIKKNRKK
//
