ID A0A0P1G168_9RHOB Unreviewed; 888 AA.
AC A0A0P1G168;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 ECO:0000313|EMBL:CUH75517.1};
GN ORFNames=TRM7557_00426 {ECO:0000313|EMBL:CUH75517.1};
OS Tritonibacter multivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=928856 {ECO:0000313|EMBL:CUH75517.1, ECO:0000313|Proteomes:UP000052022};
RN [1] {ECO:0000313|EMBL:CUH75517.1, ECO:0000313|Proteomes:UP000052022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7557 {ECO:0000313|EMBL:CUH75517.1,
RC ECO:0000313|Proteomes:UP000052022};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00952}.
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DR EMBL; CYSD01000012; CUH75517.1; -; Genomic_DNA.
DR RefSeq; WP_058288562.1; NZ_JAQIPA010000004.1.
DR AlphaFoldDB; A0A0P1G168; -.
DR STRING; 928856.SAMN04488049_103359; -.
DR OrthoDB; 9804262at2; -.
DR Proteomes; UP000052022; Unassembled WGS sequence.
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-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; 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 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; IPR013498; Topo_IA_Znf.
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:SF1; DNA TOPOISOMERASE; 1.
DR PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF13368; Toprim_C_rpt; 3.
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, 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:UP000052022};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00952}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..112
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 166..171
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT REGION 679..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..871
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 296
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 31
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 142
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 143
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 146
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 158
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 298
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 511
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ SEQUENCE 888 AA; 98143 MW; 45A4D937227C6C07 CRC64;
MPVVVVESPA KAKTINKYLG KNYTVLASYG HVRDLPRKDG SVQPDDDFAM TWEVGNDSKK
HVRAIADALK DDDALILATD PDREGEAISW HLQEALTKRR AIKKSTAVSR VTFNAITKEA
VTQAMQNPRD VDMPLVEAYL ARRALDYLVG FNLSPVLWRK LPGARSAGRV QSVCLRLIVE
REMEIEAFNP VEYWSVKAQM TTPRGQDFEA RLTVLGGEKL DKFSLANSTA AELAVQAVAS
RAYSAISVEA KPAARNPSAP FMTSTLQQEA SRKFGMGARQ CMNAAQRLYE AGLITYMRTD
GIDMAPEAVT EARAEIATRY GPEYVPSEPR VYKNKAKNAQ EAHECIRPTD MSRDAASLKV
SEDDQRKLYD LIWKRTLACQ MEGARLERTT VDLGSDDKQV VLRATGQVVL FDGFMRVYEE
GRDDVVDEDD KRLPQIMQGD AVKFAGGLAA QAEKAGKDAC VLSENAAVLS LQHHTQPPPR
YTEATLVKRM EELGIGRPST YASVITTIQD REYVRKDKNR LFPEERGRIV TIFLLNFFRT
YVGYEFTANL ENQLDDVSAG DRDYKELLGN FWRDFHAAIA ETSDLRISEV LDVLDDALAP
QLYPPREDGS DPRICPKCGT GQLHLKTSRT GGFVGCGNYP ECNYTRPIAG EGAEGEEKLL
GEDGGDEIWL KDGRYGPYVQ RGEATPENKK PKRSSLPAPR NGGWAKEETT LDKAVQLLSL
PRNVGDHPEG GRISANLGRF GPYLMHKLPG DEKPVYVSLK QWTEMFEVGM NHAVEMLADK
RANPGRGRSA AKALKELGEH PSEGGAVQIM DGRYGPYVKW GKVNATLPKD VEPANVTMDQ
AVALIAEKAP KKKAPAKKKA PAKKTAAKKT TTKKTATKTP TKEAGAEE
//
