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H7C794

- H7C794_ENTFA

UniProt

H7C794 - H7C794_ENTFA

Protein

DNA topoisomerase 4 subunit B

Gene

parE

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Status
Unreviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 26 (01 Oct 2014)
      Sequence version 1 (18 Apr 2012)
      Previous versions | rss
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    Functioni

    Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.UniRule annotation

    Catalytic activityi

    ATP-dependent breakage, passage and rejoining of double-stranded DNA.UniRule annotation

    Cofactori

    Magnesium. Binds two Mg2+ per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn2+ and Ca2+.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei9 – 91ATPUniRule annotation
    Binding sitei49 – 491ATPUniRule annotation
    Binding sitei76 – 761ATPUniRule annotation
    Binding sitei343 – 3431ATPUniRule annotation
    Metal bindingi432 – 4321Magnesium 1; catalyticUniRule annotation
    Sitei457 – 4571Interaction with DNAUniRule annotation
    Sitei460 – 4601Interaction with DNAUniRule annotation
    Metal bindingi505 – 5051Magnesium 1; catalyticUniRule annotation
    Metal bindingi505 – 5051Magnesium 2UniRule annotation
    Metal bindingi507 – 5071Magnesium 2UniRule annotation
    Sitei512 – 5121Interaction with DNAUniRule annotation
    Sitei628 – 6281Interaction with DNAUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi116 – 1227ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. DNA binding Source: UniProtKB-HAMAP
    3. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: UniProtKB-HAMAP
    4. magnesium ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. chromosome segregation Source: UniProtKB-HAMAP
    2. DNA topological change Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Isomerase, TopoisomeraseUniRule annotationSAAS annotation

    Keywords - Ligandi

    ATP-bindingUniRule annotationSAAS annotation, DNA-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEFAE226185:GHI1-1599-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA topoisomerase 4 subunit BUniRule annotation (EC:5.99.1.3UniRule annotation)
    Alternative name(s):
    Topoisomerase IV subunit BUniRule annotation
    Gene namesi
    Name:parEUniRule annotationImported
    Ordered Locus Names:EF_1615Imported
    ORF Names:I574_02005Imported, OO5_01863Imported
    OrganismiEnterococcus faecalis (strain ATCC 700802 / V583)Imported
    Taxonomic identifieri226185 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
    ProteomesiUP000001415: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. chromosome Source: InterPro

    Interactioni

    Subunit structurei

    Heterotetramer composed of ParC and ParE.UniRule annotation

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4HZ5X-ray2.70A/B/C/D/E/F/G/H/J19-225[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini426 – 540115ToprimUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the type II topoisomerase family.UniRule annotation
    Belongs to the type II topoisomerase family. ParE type 2 subfamily.UniRule annotation
    Contains 1 Toprim domain.UniRule annotation
    Contains Toprim domain.SAAS annotation

    Phylogenomic databases

    KOiK02622.
    OMAiPVGKHAM.
    OrthoDBiEOG6P334W.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.30.565.10. 1 hit.
    3.40.50.670. 1 hit.
    HAMAPiMF_00939. ParE_type2.
    InterProiIPR002288. DNA_gyrase_B_C.
    IPR003594. HATPase_ATP-bd.
    IPR005740. ParE.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR001241. Topo_IIA.
    IPR013506. Topo_IIA_bsu_dom2.
    IPR013759. Topo_IIA_cen_dom.
    IPR013760. Topo_IIA_like_dom.
    IPR018522. TopoIIA_CS.
    IPR006171. Toprim_domain.
    [Graphical view]
    PfamiPF00204. DNA_gyraseB. 1 hit.
    PF00986. DNA_gyraseB_C. 1 hit.
    PF02518. HATPase_c. 1 hit.
    PF01751. Toprim. 1 hit.
    [Graphical view]
    PRINTSiPR00418. TPI2FAMILY.
    SMARTiSM00387. HATPase_c. 1 hit.
    SM00433. TOP2c. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    SSF56719. SSF56719. 1 hit.
    TIGRFAMsiTIGR01058. parE_Gpos. 1 hit.
    PROSITEiPS00177. TOPOISOMERASE_II. 1 hit.
    PS50880. TOPRIM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    H7C794-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKKINNEYN DASIQVLEGL EAVRKRPGMY IGSTDSRGLH HLVYEIVDNA    50
    VDEALSGYGN EINVTIQKDN SICVADSGRG MPTGMHASGI PTVEVIFTVL 100
    HAGGKFGQGG YKTSGGLHGV GASVVNALSK WLEVHIVRDG VEYMERFEDG 150
    GKPVGTLKKI GKTKKRNGTS VTFLPDDTIF STTNFSYEIL AERLRESAFL 200
    LKGVKITLTD ERGEEPKEEV FHYEEGIKEF VAYLNEEKDT LTPVVYFSGA 250
    KEGIEVELAY QYNDGYSENV LSFVNNVRTK DGGTHEVGMK TSMTKAYNEY 300
    ARKVGLLKEK DKNLEGSDFR EGLAAVLSIR VPENLLQFEG QTKGKLGTPL 350
    ARTVVDNVVG EQMGFYLQEN SEMSQSLIRK AIKAREAREA ARKAREESRN 400
    GKKRKKGESL LSGKLTPAQS RNPKKNELYL VEGDSAGGSA KQGRDRKFQA 450
    ILPLRGKVIN TEKAKMQDIL KNEEINTMIY TIGAGVGPEF SIEDCNYDKI 500
    IIMTDADTDG AHIQVLLLTF FYRYMKPLIE AGKVYIALPP LYKVSKGTGK 550
    KSVIEYAWTD GELAEVIDKV GKGYMLQRYK GLGEMNAEQL WETTMDPETR 600
    TLIRVRIDDA AQAERRVTTL MGDKVEPRRK WIEQHVQFTL EEDGSILDRS 650
    EEDTSAPTGE SLLDAEKTKE AEQTDDTEIS LFDIE 685
    Length:685
    Mass (Da):76,257
    Last modified:April 18, 2012 - v1
    Checksum:iA4C79A5FB0915BFA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016830 Genomic DNA. Translation: AAO81398.1.
    AHYN01000009 Genomic DNA. Translation: EOT50099.1.
    ASWP01000006 Genomic DNA. Translation: EOT84825.1.
    RefSeqiNP_815328.1. NC_004668.1.

    Genome annotation databases

    EnsemblBacteriaiAAO81398; AAO81398; EF_1615.
    EOT50099; EOT50099; OO5_01863.
    EOT84825; EOT84825; I574_02005.
    GeneIDi1200513.
    KEGGiefa:EF1615.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016830 Genomic DNA. Translation: AAO81398.1 .
    AHYN01000009 Genomic DNA. Translation: EOT50099.1 .
    ASWP01000006 Genomic DNA. Translation: EOT84825.1 .
    RefSeqi NP_815328.1. NC_004668.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4HZ5 X-ray 2.70 A/B/C/D/E/F/G/H/J 19-225 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO81398 ; AAO81398 ; EF_1615 .
    EOT50099 ; EOT50099 ; OO5_01863 .
    EOT84825 ; EOT84825 ; I574_02005 .
    GeneIDi 1200513.
    KEGGi efa:EF1615.

    Phylogenomic databases

    KOi K02622.
    OMAi PVGKHAM.
    OrthoDBi EOG6P334W.

    Enzyme and pathway databases

    BioCyci EFAE226185:GHI1-1599-MONOMER.

    Family and domain databases

    Gene3Di 3.30.230.10. 1 hit.
    3.30.565.10. 1 hit.
    3.40.50.670. 1 hit.
    HAMAPi MF_00939. ParE_type2.
    InterProi IPR002288. DNA_gyrase_B_C.
    IPR003594. HATPase_ATP-bd.
    IPR005740. ParE.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR001241. Topo_IIA.
    IPR013506. Topo_IIA_bsu_dom2.
    IPR013759. Topo_IIA_cen_dom.
    IPR013760. Topo_IIA_like_dom.
    IPR018522. TopoIIA_CS.
    IPR006171. Toprim_domain.
    [Graphical view ]
    Pfami PF00204. DNA_gyraseB. 1 hit.
    PF00986. DNA_gyraseB_C. 1 hit.
    PF02518. HATPase_c. 1 hit.
    PF01751. Toprim. 1 hit.
    [Graphical view ]
    PRINTSi PR00418. TPI2FAMILY.
    SMARTi SM00387. HATPase_c. 1 hit.
    SM00433. TOP2c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    SSF56719. SSF56719. 1 hit.
    TIGRFAMsi TIGR01058. parE_Gpos. 1 hit.
    PROSITEi PS00177. TOPOISOMERASE_II. 1 hit.
    PS50880. TOPRIM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700802 / V583Imported and V583Imported.
    2. "Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and topoisomerase IV (ParE). Part I: Structure guided discovery and optimization of dual targeting agents with potent, broad-spectrum enzymatic activity."
      Tari L.W., Trzoss M., Bensen D.C., Li X., Chen Z., Lam T., Zhang J., Creighton C.J., Cunningham M.L., Kwan B., Stidham M., Shaw K.J., Lightstone F.C., Wong S.E., Nguyen T.B., Nix J., Finn J.
      Bioorg. Med. Chem. Lett. 23:1529-1536(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 19-225.
    3. Cited for: NUCLEOTIDE SEQUENCE.
      Strain: V583Imported.
    4. Cited for: NUCLEOTIDE SEQUENCE.
      Strain: V583Imported.

    Entry informationi

    Entry nameiH7C794_ENTFA
    AccessioniPrimary (citable) accession number: H7C794
    Entry historyi
    Integrated into UniProtKB/TrEMBL: April 18, 2012
    Last sequence update: April 18, 2012
    Last modified: October 1, 2014
    This is version 26 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported, Complete proteome, Reference proteomeImported

    External Data

    Dasty 3