PARC_STRP1
ID PARC_STRP1 Reviewed; 819 AA.
AC Q9L7Q4; Q48Z88;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 147.
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};
GN OrderedLocusNames=SPy_0910, M5005_Spy0712;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RA Yan S.S., Gill V.J., Fedorko D.P.;
RT "Resistance to multiple fluoroquinolone antibiotics in a clinical isolate
RT of Streptococcus pyogenes: identification of gyrA and parC genes and point
RT mutations responsible for the resistances.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(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; AF220946; AAF63267.1; -; Genomic_DNA.
DR EMBL; AE004092; AAK33826.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ51330.1; -; Genomic_DNA.
DR RefSeq; NP_269105.1; NC_002737.2.
DR AlphaFoldDB; Q9L7Q4; -.
DR SMR; Q9L7Q4; -.
DR STRING; 1314.HKU360_00722; -.
DR PaxDb; Q9L7Q4; -.
DR EnsemblBacteria; AAK33826; AAK33826; SPy_0910.
DR KEGG; spy:SPy_0910; -.
DR KEGG; spz:M5005_Spy0712; -.
DR PATRIC; fig|160490.10.peg.782; -.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OMA; PRSNRID; -.
DR Proteomes; UP000000750; 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; 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; Reference proteome;
KW Topoisomerase.
FT CHAIN 1..819
FT /note="DNA topoisomerase 4 subunit A"
FT /id="PRO_0000145419"
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"
FT CONFLICT 798
FT /note="I -> T (in Ref. 3; AAZ51330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 819 AA; 92478 MW; E1402D11768347BC CRC64;
MSNIQNMSLE DIMGERFGRY SKYIIQERAL PDIRDGLKPV QRRILYSMNK DGNTFEKGYR
KSAKSVGNIM GNFHPHGDSS IYDAMVRMSQ DWKNREILVE MHGNNGSMDG DPPAAMRYTE
ARLSEIAGYL LQDIEKNTVS FAWNFDDTEK EPTVLPAAFP NLLVNGSSGI SAGYATDIPP
HNLSEVIDAV VYMIDHPKAS LEKLMEFLPG PDFPTGGIIQ GADEIKKAYE TGKGRVVVRS
RTEIEELKGG KQQIIVTEIP YEVNKAVLVK KIDDVRVNNK VPGIVEVRDE SDRTGLRIAI
ELKKEADSQT 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 TLSLSERISN GSFISDTISD QEVLVARTR