ID A0A365L6V1_9BACL Unreviewed; 702 AA.
AC A0A365L6V1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 28-JAN-2026, entry version 20.
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=DP120_01430 {ECO:0000313|EMBL:RAZ80977.1};
OS Planococcus halotolerans.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Caryophanaceae;
OC Planococcus.
OX NCBI_TaxID=2233542 {ECO:0000313|EMBL:RAZ80977.1, ECO:0000313|Proteomes:UP000251002};
RN [1] {ECO:0000313|EMBL:RAZ80977.1, ECO:0000313|Proteomes:UP000251002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCU63 {ECO:0000313|EMBL:RAZ80977.1,
RC ECO:0000313|Proteomes:UP000251002};
RA Gan L.;
RT "The draft genome sequences of strains SCU63 and S1.";
RL Submitted (JUN-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RAZ80977.1}.
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DR EMBL; QLZR01000001; RAZ80977.1; -; Genomic_DNA.
DR RefSeq; WP_112221403.1; NZ_CP047673.1.
DR AlphaFoldDB; A0A365L6V1; -.
DR Proteomes; UP000251002; Unassembled WGS sequence.
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.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:RAZ80977.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000251002};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 157..594
FT /note="Topo IA-type catalytic"
FT /evidence="ECO:0000259|PROSITE:PS52039"
SQ SEQUENCE 702 AA; 79327 MW; CEBE28DA425EFE67 CRC64;
MKPVIVAEKP SQAKAYAEAF KTAKREGFLE IMPDAIFPDG AYITWGIGHL VELKEPKAYD
PKWGKWSLAA LPILPVNYQF QIARGKYQQF NIIKKLIQQT DTVINACDVD REGSNIFYSI
YYHTGAKGKI IKRLWINSLE ADEVRKGFQE LRDNKHDLLL YQEARARQIS DWLVGMNGSR
LYSLLLQEKG IREVFAIGRV QTPTVYLIYQ REKEIEAFVP EPFYEVEGEF QAEKGKYKGK
AKIKAKVRKE AEDLLAKHAI NPKEEGTVLQ VKTAEKRQPA PQLHSLSSLQ AAANRKWKYS
PAKVLSVMQK LYEKKLVSYP RTDAQHITNA EFSYLAKQVE AYQKLIGAEF PIASRAPKKR
FVDNAKVQEH YAIIPTKSIP TARKLEGLAR DERNLYEEVM RTTLAMFHRD YRYAETKVTT
DVKGLHFFTT GKTEIDKGWK ELFPVAKESK SEPALPELQE QEAVAAKVAV KEGMTTPPKP
YTEGQLIAMM KTCGKFAEEA EDIEILKEVE GLGTEATRSG IIETIKRHEY IQISKNIVSI
TEKGRILCQA IEGNLLSSPS MTAKWESYLK KIGRGEGSPE VFLTTIGKFI EKLLADVPAQ
LQSNGLPERL EMDNSKNAIA LCPRCKKGSI VSSRGSFSCT EYANGCKQSF PGTFLKKRLT
AKTIEYLCTK GKTPVIKGFV SKNGKKFSAK LILEDGKLKM EF
//