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Entry: A0A1E5G7X0_9ENTE
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ID   A0A1E5G7X0_9ENTE        Unreviewed;       689 AA.
AC   A0A1E5G7X0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000256|HAMAP-Rule:MF_00939};
DE            EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00939};
DE   AltName: Full=Topoisomerase IV subunit B {ECO:0000256|HAMAP-Rule:MF_00939};
GN   Name=parE {ECO:0000256|HAMAP-Rule:MF_00939};
GN   ORFNames=BCR25_12790 {ECO:0000313|EMBL:OEG08804.1};
OS   Enterococcus termitis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=332950 {ECO:0000313|EMBL:OEG08804.1, ECO:0000313|Proteomes:UP000095094};
RN   [1] {ECO:0000313|EMBL:OEG08804.1, ECO:0000313|Proteomes:UP000095094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 8895 {ECO:0000313|EMBL:OEG08804.1,
RC   ECO:0000313|Proteomes:UP000095094};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) 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:0000256|HAMAP-
CC       Rule:MF_00939}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185,
CC         ECO:0000256|HAMAP-Rule:MF_00939};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000256|HAMAP-
CC       Rule:MF_00939}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type 2
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00939}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OEG08804.1}.
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DR   EMBL; MIJY01000046; OEG08804.1; -; Genomic_DNA.
DR   RefSeq; WP_069665125.1; NZ_MIJY01000046.1.
DR   AlphaFoldDB; A0A1E5G7X0; -.
DR   PATRIC; fig|332950.4.peg.3727; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000095094; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00939};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00939};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00939};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00939};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00939}.
FT   DOMAIN          426..540
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          389..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..689
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   COMPBIAS        646..681
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         9
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   BINDING         49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   BINDING         76
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   BINDING         116..122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   BINDING         343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   SITE            460
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   SITE            512
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   SITE            628
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
SQ   SEQUENCE   689 AA;  76971 MW;  5D6CEA9CFB335B0D CRC64;
     MAKKVNNEYN DASIQVLEGL EAVRKRPGMY IGSTDGRGLH HLVYEIVDNA VDEALSGYGN
     EIKVVIQKDN SIKIADSGRG MPVGMHASGI PTVEVIFTVL HAGGKFGQGG YKTSGGLHGV
     GASVVNALSS WLEVTIVRDG VEYKQRFENG GKPVGTLKKI GKTNKKNGTT VTFLPDDTIF
     STIHFSYETL AERLRESAFL LKGVKISLTD LRGEEPKEEV FHYEEGIKEF VAYLNEEKDT
     LTPVVYFSGE KEGIEVELAY QYNDGYSENV LSFVNNVRTK DGGTHEVGMK ASMTKAYNEY
     ARKVGLLKEK DKNLEGSDFR EGLAAVLSIR VPENLLQFEG QTKEKLGTPQ ARNAVDNVVG
     EQMGFYLQEN SEMSQQLVRK AIKAREAREA ARKAREESRN GKKRKKGESL LSGKLTPAQS
     RNPKKNELYL VEGDSAGGSA KQGRDRKFQA ILPLRGKVLN TEKAKMQDIL KNEEINTMIY
     TIGAGVGPEF SVEDCNYDKV IIMTDADTDG AHIQVLLLTF FYRYMKPLIE AGKVYIALPP
     LYKVSKGLGK KAVTEYAWTD EELANVTQQV GKGYMLQRYK GLGEMNADQL WETTMDPETR
     TLIRVRIDDA AQAERRVTTL MGDKVEPRRK WIERHVQFTM EEDGSILDRK DGETDISPSI
     SNEVLDEEKE AEKRQTNEET EEISLFDLE
//
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