PARC_ECO57
ID PARC_ECO57 Reviewed; 752 AA.
AC P0AFI3; O69154; P20082;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000255|HAMAP-Rule:MF_00936};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00936};
DE AltName: Full=Topoisomerase IV subunit A {ECO:0000255|HAMAP-Rule:MF_00936};
GN Name=parC {ECO:0000255|HAMAP-Rule:MF_00936};
GN OrderedLocusNames=Z4373, ECs3903;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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_00936}.
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_00936};
CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000255|HAMAP-
CC Rule:MF_00936}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00936};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00936}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. ParC type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00936}.
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; AE005174; AAG58155.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37326.1; -; Genomic_DNA.
DR PIR; G85961; G85961.
DR PIR; G91116; G91116.
DR RefSeq; NP_311930.1; NC_002695.1.
DR RefSeq; WP_001281881.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AFI3; -.
DR SMR; P0AFI3; -.
DR STRING; 155864.EDL933_4242; -.
DR EnsemblBacteria; AAG58155; AAG58155; Z4373.
DR EnsemblBacteria; BAB37326; BAB37326; ECs_3903.
DR GeneID; 66673087; -.
DR GeneID; 916274; -.
DR KEGG; ece:Z4373; -.
DR KEGG; ecs:ECs_3903; -.
DR PATRIC; fig|386585.9.peg.4071; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_6; -.
DR OMA; PRSNRID; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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_00936; ParC_type1; 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; IPR005742; TopoIV_A_Gneg.
DR Pfam; PF03989; DNA_gyraseA_C; 2.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; SSF101904; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
PE 3: Inferred from homology;
KW Cell membrane; DNA-binding; Isomerase; Membrane; Reference proteome;
KW Topoisomerase.
FT CHAIN 1..752
FT /note="DNA topoisomerase 4 subunit A"
FT /id="PRO_0000145398"
FT REGION 472..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT SITE 39
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT SITE 75
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT SITE 77
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT SITE 119
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
SQ SEQUENCE 752 AA; 83831 MW; 0D4907E96CEE7086 CRC64;
MSDMAERLAL HEFTENAYLN YSMYVIMDRA LPFIGDGLKP VQRRIVYAMS ELGLNASAKF
KKSARTVGDV LGKYHPHGDS ACYEAMVLMA QPFSYRYPLV DGQGNWGAPD DPKSFAAMRY
TESRLSKYSE LLLSELGQGT ADWVPNFDGT LQEPKMLPAR LPNILLNGTT GIAVGMATDI
PPHNLREVAQ AAIALIDQPK TTLDQLLDIV QGPDYPTEAE IITSRAEIRK IYENGRGSVR
MRAVWKKEDG AVVISALPHQ VSGARVLEQI AAQMRNKKLP MVDDLRDESD HENPTRLVIV
PRSNRVDMDQ VMNHLFATTD LEKSYRINLN MIGLDGRPAV KNLLEILSEW LVFRRDTVRR
RLNYRLEKVL KRLHILEGLL VAFLNIDEVI EIIRNEDEPK PALMSRFGLT ETQAEAILEL
KLRHLAKLEE MKIRGEQSEL EKERDQLQGI LASERKMNNL LKKELQADAQ AYGDDRRSPL
QEREEAKAMS EHDMLPSEPV TIVLSQMGWV RSAKGHDIDA PGLNYKAGDS FKAAVKGKSN
QPVVFVDSTG RSYAIDPITL PSARGQGEPL TGKLTLPPGA TVDHMLMESD DQKLLMASDA
GYGFVCTFND LVARNRAGKA LITLPENAHV MPPVVIEDAS DMLLAITQAG RMLMFPVSDL
PQLSKGKGNK IINIPSAEAA RGEDGLAQLY VLPPQSTLTI HVGKRKIKLR PEELQKVTGE
RGRRGTLMRG LQRIDRVEID SPRRASSGDS EE
