PARC_STAAC
ID PARC_STAAC Reviewed; 800 AA.
AC Q5HG64;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 106.
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=SACOL1390;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
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; CP000046; AAW36639.1; -; Genomic_DNA.
DR RefSeq; WP_001289569.1; NC_002951.2.
DR AlphaFoldDB; Q5HG64; -.
DR SMR; Q5HG64; -.
DR EnsemblBacteria; AAW36639; AAW36639; SACOL1390.
DR KEGG; sac:SACOL1390; -.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OMA; PRSNRID; -.
DR Proteomes; UP000000530; 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_0000145409"
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; 90998 MW; ABE9273684755D87 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 ELIRSSKNKR 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
