PARC_MYCPN
ID PARC_MYCPN Reviewed; 789 AA.
AC P75352;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=MPN_123;
GN ORFNames=MP031;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB95679.1; -; Genomic_DNA.
DR PIR; S73357; S73357.
DR RefSeq; NP_109811.1; NC_000912.1.
DR RefSeq; WP_010874480.1; NC_000912.1.
DR AlphaFoldDB; P75352; -.
DR SMR; P75352; -.
DR IntAct; P75352; 1.
DR STRING; 272634.MPN_123; -.
DR EnsemblBacteria; AAB95679; AAB95679; MPN_123.
DR KEGG; mpn:MPN_123; -.
DR PATRIC; fig|272634.6.peg.130; -.
DR HOGENOM; CLU_002977_4_1_14; -.
DR OMA; RILYSMW; -.
DR BioCyc; MPNE272634:G1GJ3-204-MON; -.
DR Proteomes; UP000000808; 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; 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..789
FT /note="DNA topoisomerase 4 subunit A"
FT /id="PRO_0000145402"
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"
SQ SEQUENCE 789 AA; 88669 MW; EE3A7BF9A867BD19 CRC64;
MEKNKQALLL QAIEDVFAFS FSKYAKYIIQ DRALPDLRDG LKPVQRRILY GMYQMGLKPT
SPYKKSARAV GEIMGKYHPH GDASIYDAIV RMSQAWKNNL TTISIHGNNG SIDGDNAAAM
RYTEARLSPY GFELLKDIEK QLVPFVNNFD DSEVEPSVLP TLLPNLFING TSGIAAGYAT
NIAPHNVGEL LDGLSYRIEN PDCDLKAILK IVKGPDFPTG GLVYFEQELA NIYQTGKGKF
VIQAKYETNT AFGQNQIVIT EIPYETVKAN IVKQIEELIS DNKLSALESV IDSSDRSGIR
IIINHKDFLS ADKIMAFLFK HTQLQVNFNL NNTVIANRCP VRVGLLAYFD QFLAFAHELI
INSAKYDLAL ANKRLEIIKG LIKAVSMIDE IIRLIRRATD KQDAKTKLID KYAFTLNQAE
AIVSLRLYQL TNTDIKVLFA EQKELEQTIQ TAERLIAKPQ ARNQLLQAQF FQYKKQFNQP
RRAQIVGLIE KQKVQDSDFI EHKEVGLLIS HDGIYFKFEP EQLAKHLVEF KSEQDQLIFG
GVVQNSDYFF MVTSLGNIIT VPIYKTLSNT KTKMNELLAK KPILMEDEKL VLAGIVNPDK
MEQQLLVLTS QCGMVKRVEL SKVINTKQIK SSCCMALRER DKLVNAFVQT KGEPKLVCLV
SSSNSFATFL AEEIPIISNK GIGVKGIKLK AEEKVRFAMP LQDNDALVVI NSDGGVYNFE
VVELAVASRM SVGKKLIPKT KTPVSCFAAN KHSEIIGHRG KNGSDLFTLN ELNRLPKSTV
SQMRLFKWS
