ID F4G4U0_ALIDK Unreviewed; 671 AA.
AC F4G4U0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 67.
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 OrderedLocusNames=Alide2_1747 {ECO:0000313|EMBL:AEB84135.1};
OS Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Alicycliphilus.
OX NCBI_TaxID=596154 {ECO:0000313|EMBL:AEB84135.1, ECO:0000313|Proteomes:UP000007938};
RN [1] {ECO:0000313|EMBL:AEB84135.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RX PubMed=21742888; DOI=10.1128/JB.00365-11;
RA Oosterkamp M.J., Veuskens T., Plugge C.M., Langenhoff A.A., Gerritse J.,
RA van Berkel W.J., Pieper D.H., Junca H., Goodwin L.A., Daligault H.E.,
RA Bruce D.C., Detter J.C., Tapia R., Han C.S., Land M.L., Hauser L.J.,
RA Smidt H., Stams A.J.;
RT "Genome Sequences of Alicycliphilus denitrificans Strains BC and K601T.";
RL J. Bacteriol. 193:5028-5029(2011).
RN [2] {ECO:0000313|EMBL:AEB84135.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Oosterkamp M.,
RA Pieper D., van Berkel W., Langenhoff A., Smidt H., Stams A., Woyke T.;
RT "Complete sequence of chromosome of Alicycliphilus denitrificans K601.";
RL Submitted (APR-2011) 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; CP002657; AEB84135.1; -; Genomic_DNA.
DR RefSeq; WP_013721848.1; NC_015422.1.
DR AlphaFoldDB; F4G4U0; -.
DR STRING; 596154.Alide2_1747; -.
DR KEGG; adk:Alide2_1747; -.
DR eggNOG; COG0550; Bacteria.
DR HOGENOM; CLU_002929_5_2_4; -.
DR OMA; VEHCRYR; -.
DR OrthoDB; 9803554at2; -.
DR Proteomes; UP000007938; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
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: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; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 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; IPR013498; Topo_IA_Znf.
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 Pfam; PF01396; zf-C4_Topoisom; 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 SUPFAM; SSF57783; Zinc beta-ribbon; 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:AEB84135.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007938};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..132
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 648..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 73098 MW; CB262E66F025A8E8 CRC64;
MRVFLCEKPS QGKDIARVLG AGQRGNGCYS GAGVVVTWCI GHLVEAVPPE GYGEQYKRWA
IEQLPILPER WRVEPKSATA AQFKVVQQLV AKAGELVIAT DADREGEMIA REIIDLCSYR
GPIQRLWLSA LNDVSIRKAL GALKPSAETL PLYFSALARS RADWLIGMNL SRLFTLLGRQ
AGYTGVLSVG RVQTPTLKLV VDRDREIARF VCVPFWAIEV ALSHAGQSFV ASWTPPQGST
DDAGRCLQQP VAQQAVERLR TAGAAQVRSV ETERVREGPP LPFDLGTLQE VCSKQLGLDV
QETLDIAQAL YETHKATTYP RSDSGYLPES MLAEVPTVLD SMVKTDPSLR PLIERLDRQQ
RSRAWNDGKV SAHHGIIPTL EPANLSAMNE KELAVYRLIR AHYLAQFLPH HEFDRTVAQF
SCGSQSLAAV GKQIAVIGWR EVLATPGPDD ADGEDAQRSQ VLPALHAGLS CPVGKVDLKA
LKTLPPKPYT QGELIKAMKT VAKFVTDPRL KQKLRDTTGI GTEATRANII NGLIGRGYLV
KKGRAVRASD AAFTLIDAVP SAIADPGTTA VWEHALDMIE AGQMALDTFI EKQAAWVGQL
VQQYRGATLS LKLPPAPACP QCGAPMQQRT GKSGAFWSCS RYPDCKGTLP IESPTGRRSA
PRKRRAASKA S
//