PARC_STAAN
ID PARC_STAAN Reviewed; 800 AA.
AC Q93KF4;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 122.
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=SA1189;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB42447.1; -; Genomic_DNA.
DR PIR; C89911; C89911.
DR RefSeq; WP_001289562.1; NC_002745.2.
DR AlphaFoldDB; Q93KF4; -.
DR SMR; Q93KF4; -.
DR EnsemblBacteria; BAB42447; BAB42447; BAB42447.
DR KEGG; sau:SA1189; -.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OMA; PRSNRID; -.
DR Proteomes; UP000000751; 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 1: Evidence at protein level;
KW Cell membrane; DNA-binding; Isomerase; Membrane; Topoisomerase.
FT CHAIN 1..800
FT /note="DNA topoisomerase 4 subunit A"
FT /id="PRO_0000145411"
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; 90982 MW; 81B6F16463E86029 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 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
