ID   PARC_MYCGE              Reviewed;         781 AA.
AC   P47446; Q49377;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 133.
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=MG204;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-479.
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RA   Bailey C.C., Younkins R., Huang W.M., Bott K.F.;
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L43967; AAC71422.1; -; Genomic_DNA.
DR   EMBL; U25549; AAC43991.1; -; Genomic_DNA.
DR   PIR; E64222; E64222.
DR   RefSeq; WP_010869372.1; NC_000908.2.
DR   AlphaFoldDB; P47446; -.
DR   SMR; P47446; -.
DR   STRING; 243273.MG_204; -.
DR   EnsemblBacteria; AAC71422; AAC71422; MG_204.
DR   KEGG; mge:MG_204; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_4_1_14; -.
DR   OMA; RILYSMW; -.
DR   OrthoDB; 217468at2; -.
DR   BioCyc; MGEN243273:G1GJ2-237-MON; -.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IBA:GO_Central.
DR   GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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; IBA:GO_Central.
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; 3.
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..781
FT                   /note="DNA topoisomerase 4 subunit A"
FT                   /id="PRO_0000145401"
FT   ACT_SITE        122
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            42
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            78
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            80
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            91
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            97
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   SITE            121
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT   CONFLICT        261
FT                   /note="P -> R (in Ref. 2; AAC43991)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   781 AA;  88513 MW;  F14319CEE305B437 CRC64;
     MDQKNNNLFQ KAIEEVFAVS FSKYAKYIIQ DRALPDLRDG LKPVQRRILY GMFQMGLKPT
     TPYKKSARAV GEIMGKYHPH GDSSIYDAII RMSQSWKNNW TTVSIHGNNG SVDGDNAAAM
     RYTETRLSLY GFELLKDIDK KLVSFINNFD DSEKEPTVLP TLLPNLFING ASGIAAGYAT
     NIAPHNTNEL LDSLCLRIDQ PNCELKQILK IVKGPDFPTG GNVYFEKSLS DIYQAGKGKF
     IIQAKYEVNK NLNQIEITQI PYETLKANIV KQIEEIIFDN KLSAIESVID SSDRNGIRII
     IKHKDFLPAE KIMAFLFKHT QLQVNFNLNN TVIANRFPIQ IGLLSYLDHF LKFCHELIIN
     KAKYELELAS KRLEIILGLI KAISIIDKII KLIRSAVDKS DAREKLIDNF KFTFNQAEAI
     VSLRLYQLTN TDIFELNQEQ NELEKTVISS EQLIASEKAR NKLLKKQFEG YKKQFHQQRR
     SQICGFINQK KVEESELIEN KTYGVLITKA GNYHKFESNQ LLKSTTDFKS ESDTIIFAQT
     IANTDQIFIV TSLGNIINIP VYKLAFNSKN KLASLVSKKP ILLEYETIVF VGTMNSVNQP
     ILVLTSKLGM VKRIDLTKLN IKPLKATLCI SLRDKDHLVS AFLQQDDKLI CLVSDHNYYT
     VFHTNEIPLI SSKGMGVKGM KLKLEDQIKF VVAFEANEPL VMICSDGSVI NLKQTELVVV
     SRMATAKKLP VKKAINYCFS DATNTQLINF QGKNGSKLIT TSELNQMSKT AISQTRFNKL
     N