ID A0A075R966_BRELA Unreviewed; 753 AA.
AC A0A075R966;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 28-JAN-2026, entry version 45.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
DE AltName: Full=Omega-protein {ECO:0000256|ARBA:ARBA00032877};
DE AltName: Full=Relaxing enzyme {ECO:0000256|ARBA:ARBA00032235};
DE AltName: Full=Swivelase {ECO:0000256|ARBA:ARBA00030003};
DE AltName: Full=Untwisting enzyme {ECO:0000256|ARBA:ARBA00031985};
GN ORFNames=BRLA_c034560 {ECO:0000313|EMBL:AIG27768.1};
OS Brevibacillus laterosporus LMG 15441.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Brevibacillus.
OX NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG27768.1, ECO:0000313|Proteomes:UP000005850};
RN [1] {ECO:0000313|EMBL:AIG27768.1, ECO:0000313|Proteomes:UP000005850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG27768.1,
RC ECO:0000313|Proteomes:UP000005850};
RX PubMed=21914864; DOI=10.1128/JB.05696-11;
RA Djukic M., Poehlein A., Thurmer A., Daniel R.;
RT "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of
RT invertebrates.";
RL J. Bacteriol. 193:5535-5536(2011).
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};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446}.
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DR EMBL; CP007806; AIG27768.1; -; Genomic_DNA.
DR RefSeq; WP_003336735.1; NZ_CP007806.1.
DR AlphaFoldDB; A0A075R966; -.
DR STRING; 1042163.BRLA_c034560; -.
DR KEGG; blr:BRLA_c034560; -.
DR eggNOG; COG0550; Bacteria.
DR HOGENOM; CLU_002929_5_2_9; -.
DR Proteomes; UP000005850; Chromosome.
DR GO; GO:0043597; C:cytoplasmic replication fork; IEA:TreeGrafter.
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-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 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 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; IPR005738; TopoIII.
DR InterPro; IPR025589; Toprim_C_rpt.
DR InterPro; IPR006171; TOPRIM_dom.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR NCBIfam; NF005829; PRK07726.1; 1.
DR NCBIfam; TIGR01056; topB; 1.
DR PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF13342; Toprim_Crpt; 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; TOPO_IA_1; 1.
DR PROSITE; PS52039; TOPO_IA_2; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AIG27768.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005850};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 1..140
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 157..603
FT /note="Topo IA-type catalytic"
FT /evidence="ECO:0000259|PROSITE:PS52039"
FT REGION 724..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 753 AA; 85048 MW; 67F349F6016DB0E2 CRC64;
MKVIIAEKPD QASKLSSPFA HKKQQGYIEI APHRLFPQGA LVTWAVGHIC ELVPPEDYNP
TWKKWSMETL PMIPERFRYQ VMKSKAKQFT IIKQLLKRSD VTEIIHAGDA GREGELIIRT
AIELAGVKKP MKRLWISSLT DRAIVEGFEH VLDETHTRNL YYEAYSRSCA DWLIGMNASR
IYTILFKQKG VSDVFSAGRV QTPTLALVVK REKEIANFKS EPFWEVIASF TIEGKKYEGI
WQKDGESRLF DEQMATRIAQ FCEKKPASVQ EVKKERKEFL PPFLFNLSSL QATANKIFKF
SPKKTLDVAQ QLYLKGFLSY PRSDSSFVTP GEAKSFPEIL SKLAKKKEFQ SFFPTPIHSV
ANNKRYVNEK KVTDHYAIIP TEQVPHLDKL SADERHIYDL VARRLIAAHY EPAIFDYTTI
TTLVDGRATF ISKGKCQVQA GWRTVLFQGQ DEDDKDKDEE KLLPPVEKNE TGKVSRVKVK
AGKTQPPKRY TEGQLITLMK TAGKHLENSE WEKVLSKTEG LGTEATRAGI ITMLKDRKYI
EVKKNQVFAL EKGSLLIDAI GDKILASPEM TARWEQRLAE IGQGQASAQE FMEQVKKLAH
KIVQDATEQS ATWDFSGMDI EAMPKQASTF TLGKKIAVCA GCKGSIVDKG NFYGCDQYNK
TGCKITLPKK LLGKSLSATN VKKLMEQGKS GLIKGFKKGD KTFDAYLKWD IEKAQFQFEF
EAKTASSGAK EYKKPSSGAP KGKKITEALY STE
//
