ID   PARC_RICFE              Reviewed;         737 AA.
AC   Q4UNA0;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 105.
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=RF_0107;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY60958.1; -; Genomic_DNA.
DR   RefSeq; WP_011270461.1; NC_007109.1.
DR   AlphaFoldDB; Q4UNA0; -.
DR   SMR; Q4UNA0; -.
DR   STRING; 315456.RF_0107; -.
DR   EnsemblBacteria; AAY60958; AAY60958; RF_0107.
DR   KEGG; rfe:RF_0107; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_4_1_5; -.
DR   OMA; PRSNRID; -.
DR   OrthoDB; 217468at2; -.
DR   Proteomes; UP000008548; 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..737
FT                   /note="DNA topoisomerase 4 subunit A"
FT                   /id="PRO_0000273114"
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   737 AA;  83127 MW;  1DFAA1F754FC9201 CRC64;
     MKEAKIENID FGNALSERYL AYALSTIMSR SLPDVRDGLK PVHRRLLYAM LQLRLEPNSG
     YKKCARVVGD VIGKYHPHGD VAVYDTLVRL AQHFSLRYPL IDGQGNFGSI DGDNAAAMRY
     TESRMTEICT LLMVDIEKDT VDFRPTYDDS DLEPVIMPAS FPNLLANGSE GIAVGMATNI
     PPHNLHELCD ALVHLIDHPK AEISDMMNFI KGPDFPTGGI IIDKAELINA AYSTGRGSFR
     MRSRWEKEEL SYGTYQIVVT EIPYQVQKSK LIEQIAILLK DKKIPLVSNI RDESTDIIRL
     VIEPRDRGCD PQIVMESLFK LTNLESRIQL NMNVIGSNNV PRVMNILEVL QEFLAHRQNI
     VTRRSTYLLN KIKHRLEILE GLRIAYLNLD EIIKIIREED EPKAIMMERF KLTEIQVEAI
     LNTRLRSLRK LEEQEIINEH SNLQKQQAIL EEILNNPKEL WKIVKKEIKA VQTKFGLNTV
     IGARRTSFEE VTLTNQVVDI TAFITKEPIT IICSKMGWVR SLKGHNTDLS TIKYKEGDAE
     KFIIEAYTTD KILIVSSEGR FFTLLADNIS KGKGTGESIK LLVDIGNNDI TNILVHKSDQ
     LLLLASSIGK GFLVNSNEVM AQTKTGKQIM NVPDGHTCIA CLPVNGDSIA CIGESRKLLV
     FNIDEIPEMK KGQGVTLQKF KNAKLLDIKI FNKEDGLSWN NNGKVKLEKN IIAFLGKRGS
     TGKLPPMGFH KNNRFSS