ID   PARC_RICCN              Reviewed;         738 AA.
AC   Q92JH0;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 123.
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=RC0097;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL02635.1; -; Genomic_DNA.
DR   PIR; A97712; A97712.
DR   RefSeq; WP_010976781.1; NC_003103.1.
DR   AlphaFoldDB; Q92JH0; -.
DR   SMR; Q92JH0; -.
DR   EnsemblBacteria; AAL02635; AAL02635; RC0097.
DR   KEGG; rco:RC0097; -.
DR   PATRIC; fig|272944.4.peg.115; -.
DR   HOGENOM; CLU_002977_4_1_5; -.
DR   OMA; PRSNRID; -.
DR   Proteomes; UP000000816; 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..738
FT                   /note="DNA topoisomerase 4 subunit A"
FT                   /id="PRO_0000145405"
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   738 AA;  83246 MW;  C932298ADDC667AF CRC64;
     MKEAKVENID FGNALSERYL AYALSTIMSR SLPDVRDGLK PVHRRLLYAM LQLRLEPNSG
     YKKCARVVGD VIGKYHPHGD VAVYDTLVRL AQHFSLRYPL IDGQGNFGSI DGDNAAAMRY
     TESRMTDICT LLMEDIDKDT VDFRPTYDGS DLEPVIMPAS FPNLLANGSE GIAVGMATNI
     PPHNLHELCD ALIHLINHPK AEINDIINFV KGPDFPTGGI IIDKAEVINA AYTTGRGSLR
     VRSRWEKEEL SYGTYQIVVT EIPYQVQKSK LIEQIAILLK DKKIPLVSNI RDESTDIIRL
     VIEPRDRGCD PQIVMESLFK LTNLESRIQL NMNVIGSNNV PRVMNILEIL QEFLYHRQNI
     VTRRSTYLLN KIKHRLEILK GLRIAYLNLD EIIKIIREED EPKAIMMEWF KLTEIQVEAI
     LNTRLRSLRK LEEQEIINEH SNLQKQQAIL EEILNNPKEL WKIVKKEIKT VQTKFGLNTV
     IGARRTSFEE VTLTNQVVDI TAFITKEPIT IICSKMGWVR SLKGHNTDLS TIKYKEGDAE
     KFILEAYTTD KILIVSSEGR FFTLLADNIS KGKGTGESIK LLVDIGNNDI TNILVYKPDQ
     LLLLASSVGK GFLVNSNEVM AQTKTGKQIM NVPDGHVCIA CLPVNGDSIA CIGESRKLLV
     FNIDEIPEMK KGQGVTLQKF KNAKLLDIKI FNKEDGLGWN NNGKVKLEKN IVAFLGKRGS
     TGKLPPMGFP KNNRFSSY