GenomeNet

Database: UniProt
Entry: C7MGF4_BRAFD
LinkDB: C7MGF4_BRAFD
Original site: C7MGF4_BRAFD 
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}.
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; 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
//
DBGET integrated database retrieval system