PARC_STAEQ
ID PARC_STAEQ Reviewed; 800 AA.
AC Q5HPI5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 109.
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=SERP0926;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(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_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; CP000029; AAW54308.1; -; Genomic_DNA.
DR RefSeq; WP_002439655.1; NC_002976.3.
DR AlphaFoldDB; Q5HPI5; -.
DR SMR; Q5HPI5; -.
DR STRING; 176279.SERP0926; -.
DR ChEMBL; CHEMBL3706563; -.
DR EnsemblBacteria; AAW54308; AAW54308; SERP0926.
DR GeneID; 50018836; -.
DR KEGG; ser:SERP0926; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OMA; PRSNRID; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000000531; 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; Reference proteome;
KW Topoisomerase.
FT CHAIN 1..800
FT /note="DNA topoisomerase 4 subunit A"
FT /id="PRO_0000145417"
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; 91145 MW; AE8EBCD25C5205CA 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 KRIDELRADK 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
