ID A0A1K1SQP9_9BACT Unreviewed; 712 AA.
AC A0A1K1SQP9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05661012_05931 {ECO:0000313|EMBL:SFW86618.1};
OS Chitinophaga sancti.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1004 {ECO:0000313|EMBL:SFW86618.1, ECO:0000313|Proteomes:UP000183788};
RN [1] {ECO:0000313|EMBL:SFW86618.1, ECO:0000313|Proteomes:UP000183788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 784 {ECO:0000313|EMBL:SFW86618.1,
RC ECO:0000313|Proteomes:UP000183788};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FPIZ01000029; SFW86618.1; -; Genomic_DNA.
DR RefSeq; WP_072365392.1; NZ_FPIZ01000029.1.
DR AlphaFoldDB; A0A1K1SQP9; -.
DR STRING; 1004.SAMN05661012_05931; -.
DR OrthoDB; 9803554at2; -.
DR Proteomes; UP000183788; 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; 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_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 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; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:SFW86618.1};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 1..134
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 601..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 712 AA; 80523 MW; AEEF84862F80103C CRC64;
MKVCIAEKPS VARDIAEVIG AKTRKDGYYE GNGYQVTWTF GHFCTLKEPH DYTEQWKFWR
LEDLPMIPSH FGIKLIENGG VEKQFKVIES LVQACDEVIN CGDAGQEGEL IQRWVLLKAQ
CTVPVKRLWI SSLTVQAIQD GFQKLKDASQ YDNLYAAGSA RAIGDWLLGM NATRLFTKKF
AIGKTVLSIG RVQTPTLAMI VQRQKEINAF VSEEYWELKT IYRETEFTAT IDRIKNLDRA
NKGLEYLKQH PFEITSFEKK EGKEGNPRLF DLTGLQVEAN KKFGFTADDT LKYIQNLYEK
KLTTYPRVDT TYLSEDLHPK VAGILQDLKP YANLTAPILA NPIPKLKSVF DDKKVTDHHA
IIPTGEYPSN LPLEEKRIYD LVARRFIAAF YPECKISNTT VLGVVGQVEF KVTGKQILEP
GWKEVYANDA PAPKESKDGK EEVEEKVLPV FVVGETGPHT PRVHQGKTTP PKAFTEATLL
RAMETAGKQV DDEEMRELMK DNGIGRPSTR ANIIETLFRR KYIEKRKKNL FATQTGMDLI
DTITSDLLKS AELTGQWERK LRQIEKGEYQ LDTFKQELIQ MVVDLTREVK NASYKTIVAV
QTPPPAPEKE KAKEEKPKKA PKPKQEIASL QCPKCKEHPL IKGNAAYGCA NFKVCGFKVP
FESYGKKLSD KQLADLLTKG KTTKLKGLKL PDGTEVEGKL VLNTEFNISV EK
//
