ID   D5DPQ9_PRIM1            Unreviewed;       294 AA.
AC   D5DPQ9;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   02-SEP-2026, entry version 68.
DE   SubName: Full=DNA topoisomerase {ECO:0000313|EMBL:ADE68980.1};
GN   OrderedLocusNames=BMQ_1951 {ECO:0000313|EMBL:ADE68980.1};
OS   Priestia megaterium (strain ATCC 12872 / QMB1551) (Bacillus megaterium).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Priestia.
OX   NCBI_TaxID=545693 {ECO:0000313|EMBL:ADE68980.1, ECO:0000313|Proteomes:UP000000935};
RN   [1] {ECO:0000313|EMBL:ADE68980.1, ECO:0000313|Proteomes:UP000000935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12872 / QMB1551 {ECO:0000313|Proteomes:UP000000935};
RX   PubMed=21705586; DOI=10.1128/JB.00449-11;
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Koenig S.S., Huot Creasy H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA   Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA   Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA   Bremer E., Jahn D., Ravel J., Vary P.S.;
RT   "Genome sequences of the biotechnologically important Bacillus megaterium
RT   strains QM B1551 and DSM319.";
RL   J. Bacteriol. 193:4199-4213(2011).
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01383}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01383}.
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DR   EMBL; CP001983; ADE68980.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5DPQ9; -.
DR   STRING; 545693.BMQ_1951; -.
DR   KEGG; bmq:BMQ_1951; -.
DR   eggNOG; COG0550; Bacteria.
DR   HOGENOM; CLU_002929_5_1_9; -.
DR   Proteomes; UP000000935; Chromosome.
DR   GO; GO:0043597; C:cytoplasmic replication fork; IEA:TreeGrafter.
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:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:TreeGrafter.
DR   GO; GO:0006281; P:DNA repair; IEA:TreeGrafter.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR   Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR   InterPro; IPR000380; Topo_IA.
DR   InterPro; IPR013497; Topo_IA_cen.
DR   InterPro; IPR013824; Topo_IA_cen_sub1.
DR   InterPro; IPR013825; Topo_IA_cen_sub2.
DR   InterPro; IPR023405; Topo_IA_core_domain.
DR   InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR   InterPro; IPR025589; Toprim_C_rpt.
DR   PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR   PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF13342; Toprim_Crpt; 1.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR   PROSITE; PS52039; TOPO_IA_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU01383};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ADE68980.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000935};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          1..174
FT                   /note="Topo IA-type catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS52039"
SQ   SEQUENCE   294 AA;  32758 MW;  AAEEE9056DC15426 CRC64;
     MEKRAAFISK GKQQIQEGWR KVIFQNEKDD DVILPNVQEG EEGKVVKVDV KEGKTQPPKR
     YTEGQLITLM KTAGKHLDND ELEKILAKSE GLGTEATRAG IITMLKDRKY IDVKKNQVFA
     TDKGKVLIDA IGDKILASPE MTAKWEQRLA EIGEGAASAA AFMEQTKKLS AKIIEDAVEA
     ESKWNFSGYD TESIQRKGKG KGKSFSSKSF GSCKLCDGKV VDKGSFYGCS NYAKTKCTFT
     VSKKILDKTV TQANLKKLLS EGQTDLIEGF KKGDKTFNAK LEWKENKVQF LFEK
//