TOP1_BACAN
ID TOP1_BACAN Reviewed; 870 AA.
AC P40114; Q8KYH4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 25-MAY-2022, entry version 156.
DE RecName: Full=DNA topoisomerase 1;
DE EC=5.6.2.1 {ECO:0000255|PROSITE-ProRule:PRU10131};
DE AltName: Full=DNA topoisomerase I;
DE AltName: Full=Omega-protein;
DE AltName: Full=Relaxing enzyme;
DE AltName: Full=Swivelase;
DE AltName: Full=Untwisting enzyme;
GN Name=topX; Synonyms=top1;
GN OrderedLocusNames=pXO1-142, BXA0213, GBAA_pXO1_0213;
OS Bacillus anthracis.
OG Plasmid pXO1.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=7702;
RX PubMed=8152371; DOI=10.1111/j.1365-2958.1994.tb00328.x;
RA Fouet A., Sirard J.-C., Mock M.;
RT "Bacillus anthracis pXO1 virulence plasmid encodes a type 1 DNA
RT topoisomerase.";
RL Mol. Microbiol. 11:471-479(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RX PubMed=10515943; DOI=10.1128/jb.181.20.6509-6515.1999;
RA Okinaka R.T., Cloud K., Hampton O., Hoffmaster A.R., Hill K.K., Keim P.,
RA Koehler T.M., Lamke G., Kumano S., Mahillon J., Manter D., Martinez Y.,
RA Ricke D., Svensson R., Jackson P.J.;
RT "Sequence and organization of pXO1, the large Bacillus anthracis plasmid
RT harboring the anthrax toxin genes.";
RL J. Bacteriol. 181:6509-6515(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ames / isolate Florida / A2012;
RX PubMed=12004073; DOI=10.1126/science.1071837;
RA Read T.D., Salzberg S.L., Pop M., Shumway M.F., Umayam L., Jiang L.,
RA Holtzapple E., Busch J.D., Smith K.L., Schupp J.M., Solomon D., Keim P.,
RA Fraser C.M.;
RT "Comparative genome sequencing for discovery of novel polymorphisms in
RT Bacillus anthracis.";
RL Science 296:2028-2033(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(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 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10131};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA22859.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD32445.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM26155.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; M97227; AAA22859.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF065404; AAD32445.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE011190; AAM26155.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE017336; AAT35502.1; -; Genomic_DNA.
DR PIR; S41543; S41543.
DR RefSeq; NP_052837.1; NC_001496.1.
DR RefSeq; WP_000520727.1; NZ_VTZH01000012.1.
DR AlphaFoldDB; P40114; -.
DR SMR; P40114; -.
DR PRIDE; P40114; -.
DR EnsemblBacteria; AAT35502; AAT35502; GBAA_pXO1_0213.
DR GeneID; 45025541; -.
DR KEGG; bar:GBAA_pXO1_0213; -.
DR HOGENOM; CLU_002929_5_6_9; -.
DR OMA; FVIWKTI; -.
DR Proteomes; UP000000594; Plasmid pXO1.
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; 1.10.290.10; -; 1.
DR Gene3D; 1.10.460.10; -; 1.
DR Gene3D; 2.70.20.10; -; 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; IPR025589; Toprim_C_rpt.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR PANTHER; PTHR11390; PTHR11390; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF13342; Toprim_Crpt; 3.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56712; SSF56712; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA-binding; Isomerase; Metal-binding; Plasmid; Reference proteome; Repeat;
KW Topoisomerase; Virulence; Zinc; Zinc-finger.
FT CHAIN 1..870
FT /note="DNA topoisomerase 1"
FT /id="PRO_0000145139"
FT DOMAIN 1..128
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT ZN_FING 603..627
FT /note="C4-type 1"
FT ZN_FING 693..717
FT /note="C4-type 2"
FT ZN_FING 784..807
FT /note="C4-type 3"
FT REGION 180..185
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT ACT_SITE 299
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT SITE 35
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 153
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 157
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 301
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
SQ SEQUENCE 870 AA; 100092 MW; CA5E6F00219AB9D4 CRC64;
MKSPRFRHSQ KYIGSKPYYG YYENDHYIVS WCRGHLLELK NPEEMDPKYK LFQLEHLPLI
FQPSYKVIQE NAEQLQILVK LLQRPDVDHA VNICDADREG ELIYREVYEY AGVNKKQSRV
YKSSFEAAEL EAALNRLESA SKYDGLAYSA KARQYLDYLL GMNITRGCTT KLAQNKFLLS
SGRVQMCLLH EIRQRELAIE NYREQSYYHL QLITDLGLKP VMKTEDQVLN PSPLKSLGEN
LKDQYLTVED FKEGTRKQNP KLLYNLTDLY KDAHAQLQIN AETAKKHIQN LYEEGFITYP
RSSSRHLPTE QVDRVKGVMQ ALAKSRYSLL VQSVDIDAID IKHKTFDDDL VSSHFAIIPT
TKQYQEEGRP EIEKQLYSLV VKRFVGNFMR PAVYLVRDVS LIDAMGNTYQ IKESVLREKG
FLEVFQEEVK EESVETFKVP ILQKGQELQI YDFELQESKT KKPALHTESS ILTFMETAGR
KIDDEHLKEL MKGKRIGTVA TEAAFIPVLH EKNFIDIEKG KIITTPIGRA FIEQFPVQQI
KDPLYTAEME GMIHRIEKNE MSYENFIAQT NAFVQKITQE IIRIPDTVSY NLIETWKKQI
EVCQCPCGNG IILDRGKFFG CSNHPNCNKG LPKRVKEKTI PTAQVKKLFE ENKTDIIKGF
KSNGKEFSAY LAFVNGEVSF NLPSVEELSL GQCPKCQKGK ILNRKTFFGC SEYQNGCDFM
LPAKIKGKKL SDSQIKKLVN NHVTDFINGF SGEKGEFTAA IRLKTDLSIC FEFPTTDDRT
VGKCPLCQSR VIIGKTNYLC EQYKRGCDFI VSGMILEKRI TASQIKKLLE KNMTDTVKGF
VSKKTGKSFD AKLTYDSTQK RVTFIYEKKK
