ID C7MGF4_BRAFD Unreviewed; 904 AA.
AC C7MGF4;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 24-JAN-2024, entry version 90.
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 OrderedLocusNames=Bfae_26120 {ECO:0000313|EMBL:ACU86387.1};
OS Brachybacterium faecium (strain ATCC 43885 / DSM 4810 / JCM 11609 / LMG
OS 19847 / NBRC 14762 / NCIMB 9860 / 6-10).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=446465 {ECO:0000313|EMBL:ACU86387.1, ECO:0000313|Proteomes:UP000001919};
RN [1] {ECO:0000313|EMBL:ACU86387.1, ECO:0000313|Proteomes:UP000001919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43885 / DSM 4810 / JCM 11609 / LMG 19847 / NBRC 14762 /
RC NCIMB 9860 / 6-10 {ECO:0000313|Proteomes:UP000001919};
RX PubMed=21304631; DOI=10.4056/sigs.492;
RA Lapidus A., Pukall R., Labuttii K., Copeland A., Del Rio T.G., Nolan M.,
RA Chen F., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA Rohde M., Goker M., Pati A., Ivanova N., Mavrommatis K., Chen A.,
RA Palaniappan K., D'haeseleer P., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Brachybacterium faecium type strain
RT (Schefferle 6-10).";
RL Stand. Genomic Sci. 1:3-11(2009).
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; CP001643; ACU86387.1; -; Genomic_DNA.
DR RefSeq; WP_015776591.1; NC_013172.1.
DR RefSeq; YP_003155977.1; NC_013172.1.
DR AlphaFoldDB; C7MGF4; -.
DR STRING; 446465.Bfae_26120; -.
DR KEGG; bfa:Bfae_26120; -.
DR PATRIC; fig|446465.5.peg.2575; -.
DR eggNOG; COG0550; Bacteria.
DR eggNOG; COG1754; Bacteria.
DR HOGENOM; CLU_002929_2_0_11; -.
DR OMA; YAQPKQR; -.
DR OrthoDB; 9804262at2; -.
DR Proteomes; UP000001919; 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:UP000001919};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00952}.
FT DOMAIN 5..130
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 179..184
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT REGION 460..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..904
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 328
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 35
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 155
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 159
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 171
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 330
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 532
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ SEQUENCE 904 AA; 99425 MW; D07EF91FBE3A52F4 CRC64;
MTGGRHLVIV ESPAKARTIG RYLGEEYDVK ASVGHIRDIP VPRDLPAEMK KGPYGKFGVD
VENGFDPYYI VSPDKKKTVA ELKKALKDAD TLYLATDEDR EGEAIAWHLL ETLKPKKSLP
VKRMVFHEIT KDAIRAALEN TRDIDASLVD AQETRRILDR LVGFELSPVL WRKIKPSLSA
GRVQSVATRL VVERERERMA FVAADYWDIT GTFAAEGGAD GTQFTAKIAT VDGARVATGS
DFADDGTLKP RAKNAAVLTA ESTQTLVEVL GDAPATVTAL ESKPYTRRPA APFTTSSLQQ
EASRKLRLGA RQAMRVAQSL YENGYITYMR TDSVTLSGEA IRASRAQAAE LYGSQFVPDK
PRYYQNKSQA AQEAHEAIRP AGDHFRTPAE VAGQLSGDEF RLYELIWKRT IASQMADAKG
TTSTVELLLE NEGRAATFRA AGTVITFRGF LAAYEEGRDA SRYKDDEEKG GDKRLPQMEE
GQTLDTRALT PDGHTTTPPP RYTEASLVRA LEDRGIGRPS TYASTVATVQ DRGYVLRRGT
ALVPSWTAFA VVRLLEEHFG PFIDYDFTAQ MEQQLDRMAQ GDLARSEYLK NFYLSDGTDG
PIGLKPMVDD LGEIDARAIN SIEIGEGITL RVGRYGAYVE QFPRDEDGEL IEGADPRRAN
VSDEVAPDEL TVEKAKEMLE RAKDDGRVLG TDPETGHEIV AKDGRYGPYV TEVLPEAQTA
DGKKVPKSKQ PKPRTGSLLK SMDLSTVTLE DALKLLSLPR VVGTAADGTE ITAQNGRYGP
YMKKGTDSRS LETEEQIFSI TLEEAEKIYA QPKTRGRAAA KPPLKELGTD PTSEKPIVIK
DGRFGPYITD GTTNVSLRAT EKVEEITEKV AIEKLAEKRA KGPAKKKAPA KRTTTRKKST
TTKK
//