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Database: UniProt
Entry: A0A1G7GJD4_9BACL
LinkDB: A0A1G7GJD4_9BACL
Original site: A0A1G7GJD4_9BACL 
ID   A0A1G7GJD4_9BACL        Unreviewed;       746 AA.
AC   A0A1G7GJD4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=SAMN04488542_10379 {ECO:0000313|EMBL:SDE88173.1};
OS   Fontibacillus panacisegetis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Fontibacillus.
OX   NCBI_TaxID=670482 {ECO:0000313|EMBL:SDE88173.1, ECO:0000313|Proteomes:UP000198972};
RN   [1] {ECO:0000313|EMBL:SDE88173.1, ECO:0000313|Proteomes:UP000198972}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28129 {ECO:0000313|EMBL:SDE88173.1,
RC   ECO:0000313|Proteomes:UP000198972};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNBG01000003; SDE88173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7GJD4; -.
DR   STRING; 670482.SAMN04488542_10379; -.
DR   OrthoDB; 9803554at2; -.
DR   Proteomes; UP000198972; Unassembled WGS sequence.
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: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; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034144; TOPRIM_TopoIII.
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   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};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:SDE88173.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198972};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          2..134
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          434..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..455
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..628
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   746 AA;  83977 MW;  A396EBF813148993 CRC64;
     MKTLVIAEKP DMGRTIAAVI EPRAKNNRSY LEGEHYIITW AIGHLLGLAE PDAYDDKYKR
     WNFGDLPILP QQFKIVPNPK TKDQLKTIGE LSKRCNAVVN ACDAGREGQY IFDLIQQHIK
     LDQPVKRLWI SDLTAESIAK GFEGLHEGRE FHNLTLAARA RSEADWLVGM NASRAFTTKH
     NTLLSVGRVQ TPVLALIYDR QKEIESFDSL TYYDIKAVFQ QLERSYTGTW QGDRLTDGEK
     AASIAEKVRG KAGAITSYEV KETKEYPYKL YDLTLLQREA NAKYGYSAKK TLDLAQALYE
     RHKVISYPRT SSNYVNEQNI DGMHKALHML KSTSYRDLAE GANQSIVNVN NKSVCNPSRV
     EDHHAILPTL RRAGNLSKEE QDIYDLVIRR FLSHFYPPAE YKQHTVLTEV ESETFKTNVK
     ELLFLGWKVC QPNEDNSKSS GKGRKKEEED EAEELVSEPF HINPEEKVHC SEVEVKEKAT
     QPPKSYTEGT LLKAMESAGK QLENEELRDA MKEGGLGTPA TRAATIERLK KVGYITMQGK
     RITVTQKGRT AIELIRLAGV ELLTSPEMTG HWERRLHQIS KGEAAGEKFM ESVKKFTISI
     IEKVRTQRKA DASRFESPEE DKTKGKSKRS SGSSPRSTTD SSRSRPSSGS TPPSGGLQPL
     APCPRDGCGG QIIEGRKGYG CSHFKQGCGF VIWKEFSGKK ISHAMLNTLL EKGHTQLLTF
     KDPEGEYKAR ISLVDRISGK LEIDRE
//
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