PARC_STAAU
ID PARC_STAAU Reviewed; 800 AA.
AC P0C1U9; P50073; P95682; P95683;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
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;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FDA 574;
RX PubMed=7997176; DOI=10.1111/j.1365-2958.1994.tb00458.x;
RA Ferrero L., Cameron B., Manse B., Lagneaux D., Crouzet J., Famechon A.,
RA Blanche F.;
RT "Cloning and primary structure of Staphylococcus aureus DNA topoisomerase
RT IV: a primary target of fluoroquinolones.";
RL Mol. Microbiol. 13:641-653(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KMP9;
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).
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 -!- MISCELLANEOUS: Phe-80 and Lys-84 confer resistance to fluoroquinolones.
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; L25288; AAA53116.1; -; Genomic_DNA.
DR EMBL; D67074; BAA11085.1; -; Genomic_DNA.
DR PIR; S54427; S54427.
DR RefSeq; WP_001289554.1; NZ_QEKA01000042.1.
DR AlphaFoldDB; P0C1U9; -.
DR SMR; P0C1U9; -.
DR BindingDB; P0C1U9; -.
DR ChEMBL; CHEMBL4088; -.
DR DrugBank; DB00537; Ciprofloxacin.
DR DrugCentral; P0C1U9; -.
DR PRIDE; P0C1U9; -.
DR PATRIC; fig|1280.3364.peg.2251; -.
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 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 3: Inferred from homology;
KW Antibiotic resistance; Cell membrane; DNA-binding; Isomerase; Membrane;
KW Topoisomerase.
FT CHAIN 1..800
FT /note="DNA topoisomerase 4 subunit A"
FT /id="PRO_0000145414"
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 VARIANT 80
FT /note="F -> S (in strain: FDA 574)"
FT VARIANT 84
FT /note="K -> E (in strain: FDA 574)"
FT CONFLICT 267
FT /note="S -> G (in Ref. 1; AAA53116)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="F -> Y (in Ref. 1; AAA53116)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="A -> R (in Ref. 1; AAA53116)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="F -> Y (in Ref. 1; AAA53116)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="A -> V (in Ref. 1; AAA53116)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 800 AA; 91041 MW; 01A59C49A81A4148 CRC64;
MSEIIQDLSL EDVLGDRFGR YSKYIIQERA LPDVRDGLKP VQRRILYAMY SSGNTHDKNF
RKSAKTVGDV IGQYHPHGDF SVYKAMVRLS 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 DAKENLIEVF 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
