ID PARE_ENTFA Reviewed; 685 AA.
AC H7C794;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000255|HAMAP-Rule:MF_00938};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00938};
DE AltName: Full=Topoisomerase IV subunit B {ECO:0000255|HAMAP-Rule:MF_00938};
GN Name=parE {ECO:0000255|HAMAP-Rule:MF_00938}; OrderedLocusNames=EF_1615;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 19-225 IN COMPLEX WITH INHIBITOR,
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=23352267; DOI=10.1016/j.bmcl.2012.11.032;
RA Tari L.W., Trzoss M., Bensen D.C., Li X., Chen Z., Lam T., Zhang J.,
RA Creighton C.J., Cunningham M.L., Kwan B., Stidham M., Shaw K.J.,
RA Lightstone F.C., Wong S.E., Nguyen T.B., Nix J., Finn J.;
RT "Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and topoisomerase IV
RT (ParE). Part I: Structure guided discovery and optimization of dual
RT targeting agents with potent, broad-spectrum enzymatic activity.";
RL Bioorg. Med. Chem. Lett. 23:1529-1536(2013).
CC -!- FUNCTION: Topoisomerase IV is essential for chromosome segregation. It
CC relaxes supercoiled DNA (PubMed:23352267). Performs the decatenation
CC events required during the replication of a circular DNA molecule.
CC {ECO:0000255|HAMAP-Rule:MF_00938, ECO:0000269|PubMed:23352267}.
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_00938};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00938};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00938};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00938};
CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges
CC with both the protein and the DNA. Can also accept other divalent metal
CC cations, such as Mn(2+) or Ca(2+). {ECO:0000255|HAMAP-Rule:MF_00938};
CC -!- ACTIVITY REGULATION: Pyrrolopyrimidines inhibit both GyrB and its
CC paralog in topoisomerase IV (parE) (PubMed:23352267).
CC {ECO:0000269|PubMed:23352267}.
CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000255|HAMAP-
CC Rule:MF_00938}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00938}.
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DR EMBL; AE016830; AAO81398.1; -; Genomic_DNA.
DR RefSeq; NP_815328.1; NC_004668.1.
DR RefSeq; WP_002381887.1; NZ_KE136528.1.
DR PDB; 4HZ5; X-ray; 2.70 A; A/B/C/D/E/F/G/H/J=19-225.
DR PDBsum; 4HZ5; -.
DR AlphaFoldDB; H7C794; -.
DR SMR; H7C794; -.
DR STRING; 226185.EF_1615; -.
DR EnsemblBacteria; AAO81398; AAO81398; EF_1615.
DR GeneID; 60893917; -.
DR KEGG; efa:EF1615; -.
DR PATRIC; fig|226185.45.peg.1892; -.
DR eggNOG; COG0187; Bacteria.
DR HOGENOM; CLU_006146_4_1_9; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd16928; HATPase_GyrB-like; 1.
DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_00939; ParE_type2; 1.
DR InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005740; ParE_type2.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR000565; Topo_IIA_B.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR006171; TOPRIM_domain.
DR NCBIfam; TIGR01058; parE_Gpos; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR PANTHER; PTHR45866:SF12; DNA TOPOISOMERASE 4 SUBUNIT B; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00986; DNA_gyraseB_C; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00433; TOP2c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..685
FT /note="DNA topoisomerase 4 subunit B"
FT /id="PRO_0000435622"
FT DOMAIN 426..540
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 389..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 432
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 505
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 505
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 507
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 457
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 460
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT HELIX 20..25
FT /evidence="ECO:0007829|PDB:4HZ5"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:4HZ5"
FT HELIX 36..56
FT /evidence="ECO:0007829|PDB:4HZ5"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:4HZ5"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:4HZ5"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4HZ5"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:4HZ5"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:4HZ5"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:4HZ5"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:4HZ5"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:4HZ5"
FT STRAND 152..162
FT /evidence="ECO:0007829|PDB:4HZ5"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:4HZ5"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:4HZ5"
FT HELIX 187..199
FT /evidence="ECO:0007829|PDB:4HZ5"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:4HZ5"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:4HZ5"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:4HZ5"
SQ SEQUENCE 685 AA; 76257 MW; A4C79A5FB0915BFA CRC64;
MAKKINNEYN DASIQVLEGL EAVRKRPGMY IGSTDSRGLH HLVYEIVDNA VDEALSGYGN
EINVTIQKDN SICVADSGRG MPTGMHASGI PTVEVIFTVL HAGGKFGQGG YKTSGGLHGV
GASVVNALSK WLEVHIVRDG VEYMERFEDG GKPVGTLKKI GKTKKRNGTS VTFLPDDTIF
STTNFSYEIL AERLRESAFL LKGVKITLTD ERGEEPKEEV FHYEEGIKEF VAYLNEEKDT
LTPVVYFSGA KEGIEVELAY QYNDGYSENV LSFVNNVRTK DGGTHEVGMK TSMTKAYNEY
ARKVGLLKEK DKNLEGSDFR EGLAAVLSIR VPENLLQFEG QTKGKLGTPL ARTVVDNVVG
EQMGFYLQEN SEMSQSLIRK AIKAREAREA ARKAREESRN GKKRKKGESL LSGKLTPAQS
RNPKKNELYL VEGDSAGGSA KQGRDRKFQA ILPLRGKVIN TEKAKMQDIL KNEEINTMIY
TIGAGVGPEF SIEDCNYDKI IIMTDADTDG AHIQVLLLTF FYRYMKPLIE AGKVYIALPP
LYKVSKGTGK KSVIEYAWTD GELAEVIDKV GKGYMLQRYK GLGEMNAEQL WETTMDPETR
TLIRVRIDDA AQAERRVTTL MGDKVEPRRK WIEQHVQFTL EEDGSILDRS EEDTSAPTGE
SLLDAEKTKE AEQTDDTEIS LFDIE
//
