PARC_STRPQ
ID PARC_STRPQ Reviewed; 819 AA.
AC P0DG07; Q878K1; Q8K7U6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 25-MAY-2022, entry version 54.
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=SPs1228;
OS Streptococcus pyogenes serotype M3 (strain SSI-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=193567;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSI-1;
RX PubMed=12799345; DOI=10.1101/gr.1096703;
RA Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA Hattori M., Hamada S.;
RT "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT scale genomic rearrangement in invasive strains and new insights into phage
RT evolution.";
RL Genome Res. 13:1042-1055(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC64323.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000034; BAC64323.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041174279.1; NC_004606.1.
DR AlphaFoldDB; P0DG07; -.
DR SMR; P0DG07; -.
DR KEGG; sps:SPs1228; -.
DR HOGENOM; CLU_002977_6_1_9; -.
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_0000411593"
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; 92526 MW; 199B37BBDD5C4C80 CRC64;
MSNIQNMSLE DIMGERFGRY SKYIIQERAL PDIRDGLKPV QRRILYSMNK DGNTFEKGYR
KSAKSVGNIM GNFHPHGDFS 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 TLSLSERTSN GSFISDTISD QEVLVARTR
