ID   PARC_RICBR              Reviewed;         736 AA.
AC   Q1RGX8;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000255|HAMAP-Rule:MF_00936};
DE            EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00936};
DE   AltName: Full=Topoisomerase IV subunit A {ECO:0000255|HAMAP-Rule:MF_00936};
GN   Name=parC {ECO:0000255|HAMAP-Rule:MF_00936}; OrderedLocusNames=RBE_1305;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00936}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00936};
CC   -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000255|HAMAP-
CC       Rule:MF_00936}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00936};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00936}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. ParC type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00936}.
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DR   EMBL; CP000087; ABE05386.1; -; Genomic_DNA.
DR   RefSeq; WP_011477956.1; NC_007940.1.
DR   AlphaFoldDB; Q1RGX8; -.
DR   SMR; Q1RGX8; -.
DR   STRING; 336407.RBE_1305; -.
DR   PRIDE; Q1RGX8; -.
DR   EnsemblBacteria; ABE05386; ABE05386; RBE_1305.
DR   KEGG; rbe:RBE_1305; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_4_1_5; -.
DR   OMA; PRSNRID; -.
DR   OrthoDB; 217468at2; -.
DR   Proteomes; UP000001951; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   CDD; cd00187; TOP4c; 1.
DR   Gene3D; 1.10.268.10; -; 1.
DR   Gene3D; 2.120.10.90; -; 1.
DR   Gene3D; 3.90.199.10; -; 1.
DR   HAMAP; MF_00936; ParC_type1; 1.
DR   InterPro; IPR006691; GyrA/parC_rep.
DR   InterPro; IPR035516; Gyrase/topoIV_suA_C.
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   InterPro; IPR005742; TopoIV_A_Gneg.
DR   Pfam; PF03989; DNA_gyraseA_C; 2.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; SSF101904; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
PE   3: Inferred from homology;
KW   Cell membrane; DNA-binding; Isomerase; Membrane; Topoisomerase.
FT   CHAIN           1..736
FT                   /note="DNA topoisomerase 4 subunit A"
FT                   /id="PRO_0000273113"
FT   ACT_SITE        120
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT   SITE            40
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT   SITE            76
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT   SITE            78
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT   SITE            119
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
SQ   SEQUENCE   736 AA;  82955 MW;  69A5248BFB7182AD CRC64;
     MKEAKIENID FGSALSERYL AYALSTIMSR SLPDVRDGLK PVHRRLLYAM LQLRLEPNSG
     YKKCARVVGD VIGKYHPHGD VAVYDTLVRL AQHFSLRYPL IDGQGNFGSI DGDNAAAMRY
     TESRMTEICT LLMEDIDKDT VDFRSTYDDS DLEPVIMPAS FPNLLANGSE GIAVGMATNI
     PPHNLHELCD ALMHLIDHPK AEISDIMNFI KGPDFPTGGI IIDKSDVITS AYMTGRGSFR
     VRARWEKEEL NYGVYQIVVT EIPYQVQKSK LIEQIAILLK DKKIPLVSNI RDESTDIIRL
     VIEPRDRSCD PQIVMESLFK LTNLESRIQL NMNVIGSNNV PKVMNILEVL QEFLSHRQNI
     ITRRSTYLLN KIKHRLEILE GLRIAYLNLD EIIKIIREED EPKAIMMQRF QLTEIQVEAI
     LNTRLRSLRK LEEQEIITEH SNLQKQQAIL EEILNNPKEL WKVVKKEIKA VQAKFGLNTT
     IGARRTSFEQ VTLTNQVVDI TAFITKEPIT IICSKMGWVR SLKGHNNDLS SIKYKEGDAE
     KFILEAYTTD KILIISSEGR FFTLLADNIS KGKGTGESIK LLVDIGNNDI TEILVYKPDH
     LLLLASSIGK GFVVNSNEVM AQTKSGKQIM NVPDGHTCIA CLPVNGDSVA CIGESRKLLV
     FNIDEIPEMK KGQGVTLQKF KNAKLLDIKI FNREDGLSWN SGGKVKLEKN IIAFLGKRGS
     TGKLPPMGFP KNNRFS