PARC_STAA8
ID PARC_STAA8 Reviewed; 800 AA.
AC Q2FYS4; P50073; P95682; P95683;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 99.
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}; Synonyms=grlA;
GN OrderedLocusNames=SAOUHSC_01352;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8723458; DOI=10.1128/aac.40.5.1157;
RA Yamagishi J., Kojima T., Oyamada Y., Fujimoto K., Hattori H., Nakamura S.,
RA Inoue M.;
RT "Alterations in the DNA topoisomerase IV grlA gene responsible for
RT quinolone resistance in Staphylococcus aureus.";
RL Antimicrob. Agents Chemother. 40:1157-1163(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP MUTAGENESIS OF SER-80 AND GLU-84.
RX PubMed=7492103; DOI=10.1128/aac.39.7.1554;
RA Ferrero L., Cameron B., Crouzet J.;
RT "Analysis of gyrA and grlA mutations in stepwise-selected ciprofloxacin-
RT resistant mutants of Staphylococcus aureus.";
RL Antimicrob. Agents Chemother. 39:1554-1558(1995).
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.
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; D67075; BAA11087.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD30448.1; -; Genomic_DNA.
DR RefSeq; WP_001289569.1; NZ_LS483365.1.
DR RefSeq; YP_499880.1; NC_007795.1.
DR AlphaFoldDB; Q2FYS4; -.
DR SMR; Q2FYS4; -.
DR STRING; 1280.SAXN108_1372; -.
DR BindingDB; Q2FYS4; -.
DR PRIDE; Q2FYS4; -.
DR EnsemblBacteria; ABD30448; ABD30448; SAOUHSC_01352.
DR GeneID; 3920058; -.
DR KEGG; sao:SAOUHSC_01352; -.
DR PATRIC; fig|93061.5.peg.1238; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OMA; PRSNRID; -.
DR PRO; PR:Q2FYS4; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Antibiotic resistance; Cell membrane; DNA-binding; Isomerase; Membrane;
KW Reference proteome; Topoisomerase.
FT CHAIN 1..800
FT /note="DNA topoisomerase 4 subunit A"
FT /id="PRO_0000249334"
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"
FT MUTAGEN 80
FT /note="S->F,Y: Resistant to fluoroquinolones."
FT /evidence="ECO:0000269|PubMed:7492103"
FT MUTAGEN 84
FT /note="E->K,L: Resistant to fluoroquinolones."
FT /evidence="ECO:0000269|PubMed:7492103"
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
