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PARC_STRP8
ID   PARC_STRP8              Reviewed;         819 AA.
AC   Q8P1B3;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 124.
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=spyM18_0968;
OS   Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232;
RX   PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA   Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA   Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18 group
RT   A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
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; AE009949; AAL97609.1; -; Genomic_DNA.
DR   RefSeq; WP_011017692.1; NC_003485.1.
DR   AlphaFoldDB; Q8P1B3; -.
DR   SMR; Q8P1B3; -.
DR   KEGG; spm:spyM18_0968; -.
DR   HOGENOM; CLU_002977_6_1_9; -.
DR   OMA; PRSNRID; -.
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; 4.
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..819
FT                   /note="DNA topoisomerase 4 subunit A"
FT                   /id="PRO_0000145422"
FT   ACT_SITE        118
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            38
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            74
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            76
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            87
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            93
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            117
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
SQ   SEQUENCE   819 AA;  92462 MW;  7A9215CCDA382431 CRC64;
     MSNIQNMSLE DIMGERFGRY SKYIIQERAL PDIRDGLKPV QRRILYSMNK DGNTFEKGYR
     KSAKSVGNIM GNFHPHGDSS IYDAMVRMSQ DWKNREILVE MHGNNGSMDG DPPAAMRYTE
     ARLSEIAGYL LQDIEKNTVP FAWNFDDTEK EPTVLPAAFP NLLVNGSSGI SAGYATDIPP
     HNLSEVIDAV VYMIDHPKAS LEKLMEFLPG PDFPTGGIIQ GADEIKKAYE TGKGRVVVRS
     RTEIEELKGG KQQIIVTEIP YEVNKAVLVK KIDDVRVNNK VPGIVEVRDE SDRTGLRIAI
     ELKKDADSQT ILNYLLKYTD LQVNYNFNMV AIDHFTPRQV GLQKILSSYI SHRKDIIIER
     SKFDKAKAEK RLHIVEGLIR VLSILDEIIA LIRSSDNKAD AKENLKVSYD FSEEQAEAIV
     TLQLYRLTNT DIVTLQNEEN DLRDLITTLS AIIGDEATMY NVMKRELREV KKKFANPRLS
     ELQAESQIIE IDTASLIAEE ETFVSVTRGG YLKRTSPRSF NASSLEEVGK RDDDELIFVK
     QAKTTEHLLL FTTLGNVIYR PIHELTDLRW KDIGEHLSQT ISNFATEEEI LYADIVTSFD
     QGLYVAVTQN GFIKRFDRKE LSPWRTYKSK STKYVKLKDD KDRVVTLSPV IMEDLLLVTK
     NGYALRFSSQ EVPIQGLKSA GVKGINLKND DSLASAFAVT SNSFFVLTQR GSLKRMAVDD
     IPQTSRANRG LLVLRELKTK PHRVFLAGGV QSDTSAEQFD LFTDIPEEET NQQMLEVISK
     TGQTYEIALE TLSLSERTSN GSFISDTISD QEVLVARTR
 
 
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