ID A0A1V0DBS5_9BACT Unreviewed; 860 AA.
AC A0A1V0DBS5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=DNA topoisomerase 1 {ECO:0000256|HAMAP-Rule:MF_00952};
DE EC=5.6.2.1 {ECO:0000256|HAMAP-Rule:MF_00952};
DE AltName: Full=DNA topoisomerase I {ECO:0000256|HAMAP-Rule:MF_00952};
GN Name=topA {ECO:0000256|HAMAP-Rule:MF_00952};
GN ORFNames=AWN76_004345 {ECO:0000313|EMBL:ARA92472.1};
OS Rhodothermaceae bacterium RA.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae.
OX NCBI_TaxID=1779382 {ECO:0000313|EMBL:ARA92472.1, ECO:0000313|Proteomes:UP000055617};
RN [1] {ECO:0000313|EMBL:ARA92472.1, ECO:0000313|Proteomes:UP000055617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA {ECO:0000313|EMBL:ARA92472.1,
RC ECO:0000313|Proteomes:UP000055617};
RA Liew K.J.;
RT "Complete genome of the potential lignocellulosic biomass degrader
RT Rhodothermaceae bacterium RA isolated from the saline hot spring in
RT Malaysia.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, which
CC is introduced during the DNA replication and transcription, by
CC transiently cleaving and rejoining one strand of the DNA duplex.
CC Introduces a single-strand break via transesterification at a target
CC site in duplex DNA. The scissile phosphodiester is attacked by the
CC catalytic tyrosine of the enzyme, resulting in the formation of a DNA-
CC (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH
CC DNA strand. The free DNA strand then undergoes passage around the
CC unbroken strand, thus removing DNA supercoils. Finally, in the
CC religation step, the DNA 3'-OH attacks the covalent intermediate to
CC expel the active-site tyrosine and restore the DNA phosphodiester
CC backbone. {ECO:0000256|HAMAP-Rule:MF_00952}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00952};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00952}.
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|HAMAP-Rule:MF_00952}.
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; CP020382; ARA92472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0DBS5; -.
DR STRING; 1779382.AWN76_004345; -.
DR KEGG; rbar:AWN76_004345; -.
DR OrthoDB; 9804262at2; -.
DR Proteomes; UP000055617; Chromosome.
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-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03363; TOPRIM_TopoIA_TopoI; 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 HAMAP; MF_00952; Topoisom_1_prok; 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; IPR005733; TopoI_bac-type.
DR InterPro; IPR028612; Topoisom_1_IA.
DR InterPro; IPR025589; Toprim_C_rpt.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034149; TOPRIM_TopoI.
DR NCBIfam; TIGR01051; topA_bact; 1.
DR PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR PANTHER; PTHR42785:SF1; OMEGA-PROTEIN; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF13368; Toprim_C_rpt; 4.
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, ECO:0000256|HAMAP-
KW Rule:MF_00952};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00952};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000055617};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00952}.
FT DOMAIN 3..127
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 176..181
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT REGION 467..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 325
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 33
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 152
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 153
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 156
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 161
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 168
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 327
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 524
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ SEQUENCE 860 AA; 96524 MW; 926581432B3AA78F CRC64;
MKKRLVVVES PTKARTIRNF LPPEYQVEAS MGHVRDLPSS ASEIPSRLKD EAWARLGVRV
DNGFEPLYVI PAGKRKVVNG LKAALEGAEE LYIATDEDRE GESIGWHLLE VLNPRVPVRR
MVFHEITEEA ILEALRRTRS INQHLVDAQE TRRVLDRLVG YTISPLLWKK IAPRLSAGRV
QSVAVRMLVL REKERIAFVP AQYWDLKADL VQDRQPFQAV MTHWRGIRLA TGRDFDADTG
RLKPGLEAGK DVLLLGEADA RDLAERLPEA PWRVARVEER VVTRSPAPPF ITSTLQQEAS
RKLNLSARQT MQVAQRLYEN GYITYMRTDS TVLSTEALEA ARRAVEQRYG RDYLSPSPRQ
FAGKVRNAQE AHEAIRPAGK AMRTADDLGL SGVEARLYDL IWKRTVASQM ADARLRLVTA
HIEAGEGDDV ATFRASGRSI VFPGFFRAYV EGSDDPEAAL EDREQPLPDL REGDTPACRH
VEPVGHETKP PARYTEATLV KQLEQEGIGR PSTYATIIDT IMQRGYVRKQ GNQLVPTFTA
FATNNLLEKQ FEQLVDTGFT AEMEQILDDI AEGKREATPY LRAFYKGEDG LERRVEQALD
QVDAREVSTL SFPKWGPYVV RVGKYGPYVE GELDGERVTA SLPEDLAPGD LTAEQLEELL
KAGNAEDRVL GIHPETDMPI LLRKGPYGPY VQLGDDEQEG KPKRMSLPKG VEPGEVTRQM
AIDLLSLPRT LGKHPETGQD VRVNIGRYGP YAQHGSTFAS LKKDDDIFSI DLDRALELIA
EKEAKNKPLR VLGTHPESGE VVEVWNGRYG PYVKHKRTNA TIPKDRDPEG ITMEEALELL
REREASRGKR GGRRRSKAKG
//