ID   PARC_RICPR              Reviewed;         738 AA.
AC   Q9ZE79;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 128.
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=RP067;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235270; CAA14538.1; -; Genomic_DNA.
DR   PIR; C71715; C71715.
DR   RefSeq; NP_220461.1; NC_000963.1.
DR   RefSeq; WP_004599725.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZE79; -.
DR   SMR; Q9ZE79; -.
DR   STRING; 272947.gene:17555150; -.
DR   EnsemblBacteria; CAA14538; CAA14538; CAA14538.
DR   GeneID; 57569195; -.
DR   KEGG; rpr:RP067; -.
DR   PATRIC; fig|272947.5.peg.68; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_4_1_5; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000002480; 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; 3.30.1360.40; -; 1.
DR   Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 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   NCBIfam; TIGR01062; parC_Gneg; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   PANTHER; PTHR43493:SF1; DNA TOPOISOMERASE 4 SUBUNIT A; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 3.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR   PROSITE; PS52040; TOPO_IIA; 1.
PE   3: Inferred from homology;
KW   Cell membrane; DNA-binding; Isomerase; Membrane; Reference proteome;
KW   Topoisomerase.
FT   CHAIN           1..738
FT                   /note="DNA topoisomerase 4 subunit A"
FT                   /id="PRO_0000145406"
FT   DOMAIN          32..496
FT                   /note="Topo IIA-type catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01384"
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;  83348 MW;  166B9B88C76E52A8 CRC64;
     MKEAKIENID FGNALSERYL AYALSTIMSR SLPDVRDGLK PVHRRLLYAM LQLRLEPNSG
     YKKCARVVGD VIGKYHPHGD VAVYDTLVRL AQHFSLRYPL IDGQGNFGSI DGDNAAAMRY
     TESRMTEICM LLMEDIDKDT VDFRSTYDDS DLEPVIMPAS FPNLLANGSE GIAVGMATNI
     PPHNLHELCD ALLYLIDNPQ AGINDIMNFI KGPDFPTGGI IIDKAEVINA AYTTGRGSFR
     VRSRWEKEEL SYGTYQIVVT EIPYQIQKSK LIEQIAILLK DKKIPLISSI RDESTDIIRV
     VIEPRDRSCD PQIVMESLFK LTNLESRIQL NMNVIGSNNV PRVMNILEIL QEFLVHRKNI
     IIRRSTYLLN KIKQRLEILK VLRIVYLNLD EIIEIIREED EPKTIIMERF KISAIQVEVI
     LNTRLRSLQK LEEHAIIDEH SNLQKQQAIL EKILKNHKEL WQIVKKEIKA VQTKFGLNTI
     IGARRTSFEE VDLTNQVVDI TAFITKEPIT IICSKMGWVR SLKGHNTDLS TIKYKEGDTE
     KFIIEAYTTD KILIISSKGR FFTLLADNIS KGKGTGGVSI KLLVDIGNND ITNILVYKPN
     QLLLLASSIG KGFLVNSNEV IAQTKTGKQI MNIPEGYSCI ACLPVNGDSI ACIGESRRLL
     VFNIDEIPEM KKGQGVVLQR FKNAKLLDIK IFNKQDGLSW NDGTKIQLEK NIVAFLGKRG
     GFGTFPPIGF PKNNRFSP
//