PARC_STAES
ID PARC_STAES Reviewed; 800 AA.
AC Q8CSN8;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 117.
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=SE_1037;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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}.
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DR EMBL; AE015929; AAO04634.1; -; Genomic_DNA.
DR RefSeq; NP_764592.1; NC_004461.1.
DR RefSeq; WP_001831210.1; NZ_WBME01000040.1.
DR AlphaFoldDB; Q8CSN8; -.
DR SMR; Q8CSN8; -.
DR STRING; 176280.SE_1037; -.
DR EnsemblBacteria; AAO04634; AAO04634; SE_1037.
DR KEGG; sep:SE_1037; -.
DR PATRIC; fig|176280.10.peg.1012; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OMA; PRSNRID; -.
DR Proteomes; UP000001411; 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_0000145416"
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; 91117 MW; A9FA4FF7AC5205CA CRC64;
MSEIIQDLSL EDVIGDRFGR YSKYIIQERA LPDVRDGLKP VQRRILFAMY SSGNTYDKNF
RKSAKTVGDV IGQYHPHGDS SVYDAMVRLS QDWKLRHVLI EMHGNNGSID NDPPAAMRYT
EAKLSQLSEE LLRDINKETV SFIPNYDDTT LEPMVLPARF PNLLINGSTG ISSGYATDIP
PHNLAEVIQG TLKYIDQPDI TINQLMKYIK GPDFPTGGII QGIEGIKKAY ETGKGKVVVR
SRVDEEPLRS GRKQLIVTEI PYEVNKSSLV KKIDELRADK KVDGIVEVRD ETDRTGLRIA
IELKKDANSE SIKNYLYKNS DLQISYNFNM VAISEGRPKL MGLREIIESY LNHQIEVVTN
RTRYDLEQAE KRMHIVEGLM KALSILDEVI ALIRNSKNKK DAKDNLVAEY DFTEAQAEAI
VMLQLYRLTN TDIEALKKEH EELEALIKEL RNILDNHEAL LAVIKDELNE IKKKFKVDRL
STIEAEISEI KIDKEVMVPS EEVILSLTQH GYIKRTSTRS FNASGVTEIG LKDGDRLLKH
ESVNTQDTVL VFTNKGRYLF IPVHKLADIR WKELGQHISQ IVPIDEDEEV VNVYNEKDFK
NEAFYIMATK NGMIKKSSAS QFKTTRFNKP LINMKVKDKD ELINVVRLES DQLITVLTHK
GMSLTYSTNE LSDTGLRAAG VKSINLKDED YVVMTEDVND SDSIIMVTQR GAMKRIDFNV
LQEAKRAQRG ITLLKELKKK PHRIVAGAVV KENHTKYIVF SQHHEEYGNI DDVHLSEQYT
NGSFIIDTDD FGEVESMILE
