ID   PARC_STAAW              Reviewed;         800 AA.
AC   Q8NWU8;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000255|HAMAP-Rule:MF_00937};
DE            EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00937};
DE   AltName: Full=Topoisomerase IV subunit A {ECO:0000255|HAMAP-Rule:MF_00937};
GN   Name=parC {ECO:0000255|HAMAP-Rule:MF_00937}; OrderedLocusNames=MW1242;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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_00937}.
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_00937};
CC   -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000255|HAMAP-
CC       Rule:MF_00937}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00937};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00937}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. ParC type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00937}.
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; BA000033; BAB95107.1; -; Genomic_DNA.
DR   RefSeq; WP_001289561.1; NC_003923.1.
DR   AlphaFoldDB; Q8NWU8; -.
DR   SMR; Q8NWU8; -.
DR   EnsemblBacteria; BAB95107; BAB95107; BAB95107.
DR   KEGG; sam:MW1242; -.
DR   HOGENOM; CLU_002977_6_1_9; -.
DR   OMA; PRSNRID; -.
DR   Proteomes; UP000000418; 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_00937; ParC_type2; 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; IPR005741; TopoIV_A_Gpos.
DR   PANTHER; PTHR43493:SF9; PTHR43493:SF9; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 5.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; SSF101904; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
DR   TIGRFAMs; TIGR01061; parC_Gpos; 1.
PE   3: Inferred from homology;
KW   Cell membrane; DNA-binding; Isomerase; Membrane; Topoisomerase.
FT   CHAIN           1..800
FT                   /note="DNA topoisomerase 4 subunit A"
FT                   /id="PRO_0000145415"
FT   ACT_SITE        119
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            39
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            75
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            77
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            88
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            94
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            118
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
SQ   SEQUENCE   800 AA;  90945 MW;  5D3EFFBEF203973C CRC64;
     MSEIIQDLSL EDVLGDRFGR YSKYIIQERA LPDVRDGLKP VQRRILYAMY SSGNTHDKNF
     RKSAKTVGDV IGQYHPHGDS SVYEAMVRLS QDWKLRHVLI EMHGNNGSID NDPPAAMRYT
     EAKLSLLAEE LLRDINKETV SFIPNYDDTT LEPMVLPSRF PNLLVNGSTG ISAGYATDIP
     PHNLAEVIQA TLKYIDNPDI TVNQLMKYIK GPDFPTGGII QGIDGIKKAY ESGKGRIIVR
     SKVEEETLRN GRKQLIITEI PYEVNKSSLV KRIDELRADK KVDGIVEVRD ETDRTGLRIA
     IELKKDVNSE SIKNYLYKNS DLQISYNFNM VAISDGRPKL MGIRQIIDSY LNHQIEVVAN
     RTKFELDNAE KRMHIVEGLI KALSILDKVI ELIRSSKNKC DAKENLIEVY EFTEEQAEAI
     VMLQLYRLTN TDIVALEGEH KELEALIKQL RHILDNHDAL LNVIKEELNE IKKKFKSERL
     SLIEAEIEEI KIDKEVMVPS EEVILSMTRH GYIKRTSIRS FNASGVEDIG LKDGDSLLKH
     QEVNTQDTVL VFTNKGRYLF IPVHKLADIR WKELGQHVSQ IVPIEEDEVV INVFNEKDFN
     TDAFYVFATQ NGMIKKSTVP LFKTTRFNKP LIATKVKEND DLISVMRFEK DQLITVITNK
     GMSLTYNTSE LSDTGLRAAG VKSINLKAED FVVMTEGVSE NDTILMATQR GSLKRISFKI
     LQVAKRAQRG ITLLKELKKN PHRIVAAHVV TGEHSQYTLY SKSNEEHGLI NDIHKSEQYT
     NGSFIVDTDD FGEVIDMYIS