ID   PARC_BORBU              Reviewed;         626 AA.
AC   O51066;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=DNA topoisomerase 4 subunit A;
DE            EC=5.6.2.2;
DE   AltName: Full=Topoisomerase IV subunit A;
GN   Name=parC; OrderedLocusNames=BB_0035;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
CC   -!- FUNCTION: Topoisomerase IV is essential for chromosome segregation. It
CC       relaxes supercoiled DNA. Performs the decatenation events required
CC       during the replication of a circular DNA molecule (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2;
CC   -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {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; AE000783; AAC66419.1; -; Genomic_DNA.
DR   PIR; C70104; C70104.
DR   RefSeq; NP_212169.1; NC_001318.1.
DR   RefSeq; WP_002656217.1; NC_001318.1.
DR   AlphaFoldDB; O51066; -.
DR   SMR; O51066; -.
DR   STRING; 224326.BB_0035; -.
DR   PRIDE; O51066; -.
DR   EnsemblBacteria; AAC66419; AAC66419; BB_0035.
DR   GeneID; 56568180; -.
DR   KEGG; bbu:BB_0035; -.
DR   PATRIC; fig|224326.49.peg.434; -.
DR   HOGENOM; CLU_015760_0_0_12; -.
DR   OMA; GHTMQYH; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   Gene3D; 1.10.268.10; -; 1.
DR   Gene3D; 3.90.199.10; -; 1.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
PE   3: Inferred from homology;
KW   Cell membrane; DNA-binding; Isomerase; Membrane; Reference proteome;
KW   Topoisomerase.
FT   CHAIN           1..626
FT                   /note="DNA topoisomerase 4 subunit A"
FT                   /id="PRO_0000145395"
FT   ACT_SITE        105
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000250"
FT   SITE            32
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            64
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            66
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            104
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   626 AA;  72042 MW;  99DEF5C8EA461D05 CRC64;
     MDIRTVLKDN FLQYSSYVIK DRAIASVVDG FKPVQRRIIH SLFEMHDGNF HKVANVVGNT
     MKYHPHGDTS IYEALVNIAN KDLFIEKQGN FGNLFTGDPA SASRYIECRL TPLAFDVLYS
     KEITIYESSY DGRNNEPLLY PAKIPVILIQ GSEGIAVGMA AKILPHNFNE ILNAVKSELL
     GESYDIYPDF PTGGIVDVNE YADGNGKVLV RAKIETIDEK TIVIRELPFG ETTESLISSI
     EKAIRKNYIK VSSINDFTAE NVAIELSLPR GVYASEVIEK LYHYTNCQIS ISVNLLLLSE
     RYPVVYTIKD LIKFHAAHLQ KILKMELELQ KSKILEKIFY KTLEQIFIEK KIYKLLETIS
     KEENILSIIL SEVLRHKESF SREVLKEDVE NLLKIPIRKI SLFDIDKNSK DIKILNKELK
     SINSNISSIR GYSINFIDLL LAKYSKEHQR KTKISLIKSK NVKEIATKNM KVYLNLAEGF
     AGTSLFDGEF IGNASYYDKI LVFRENSYVL KNIEDKTFID KKNVCALVYD INNSKEQIFS
     IIYFNRLDNF YYVKRFKIDK FITDKVYEFL GENDEFVDFS LNPEFVEFST NKDIVKRIEI
     DNFMVKSRSS IGKRISSNNL KKVKFK