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Q2A1P5

- Q2A1P5_FRATH

UniProt

Q2A1P5 - Q2A1P5_FRATH

Protein

DNA topoisomerase 4 subunit B

Gene

parE

Organism
Francisella tularensis subsp. holarctica (strain LVS)
Status
Unreviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (04 Apr 2006)
      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 sitei4 – 41ATPUniRule annotation
    Binding sitei41 – 411ATPUniRule annotation
    Binding sitei68 – 681ATPUniRule annotation
    Binding sitei333 – 3331ATPUniRule annotation
    Metal bindingi418 – 4181Magnesium 1; catalyticUniRule annotation
    Sitei443 – 4431Interaction with DNAUniRule annotation
    Sitei446 – 4461Interaction with DNAUniRule annotation
    Metal bindingi490 – 4901Magnesium 1; catalyticUniRule annotation
    Metal bindingi490 – 4901Magnesium 2UniRule annotation
    Metal bindingi492 – 4921Magnesium 2UniRule annotation
    Sitei497 – 4971Interaction with DNAUniRule annotation
    Sitei613 – 6131Interaction with DNAUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi109 – 1157ATPUniRule 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

    BioCyciFTUL376619:GI22-1770-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 annotation
    Ordered Locus Names:FTL_1726Imported
    OrganismiFrancisella tularensis subsp. holarctica (strain LVS)Imported
    Taxonomic identifieri376619 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
    ProteomesiUP000001944: 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
    4HXZX-ray2.70A/B1-382[»]
    4HY1X-ray1.90A/B1-382[»]
    4HYMX-ray1.90A/B1-382[»]
    4KQVX-ray2.38A/B1-382[»]
    ProteinModelPortaliQ2A1P5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini412 – 525114ToprimUniRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000075154.
    KOiK02622.
    OMAiQSYNADA.
    OrthoDBiEOG6P334W.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.30.565.10. 1 hit.
    3.40.50.670. 1 hit.
    HAMAPiMF_00938. ParE_type1.
    InterProiIPR002288. DNA_gyrase_B_C.
    IPR003594. HATPase_ATP-bd.
    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.
    IPR005737. TopoIV_B_Gneg.
    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.
    TIGRFAMsiTIGR01055. parE_Gneg. 1 hit.
    PROSITEiPS00177. TOPOISOMERASE_II. 1 hit.
    PS50880. TOPRIM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q2A1P5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQNYNAKSIE VLTGLDPVKK RPGMYTNIEN PNHLIQEIID NSVDEVLAGF    50
    ASKINITLYE DNSIEVADDG RGMPVDIHPE HKMSGIELIM TKLHSGGKFS 100
    NKNYTHSGGL HGVGVSVVNA LSTRLEAEIK RDGNVYHIVF EDGFKTKDLE 150
    IIDNVGKKNT GTKIRFWPNK KYFDDIKVNF KALKNLLEAK AILCKALTIK 200
    YSNEIKKEKL TWHFETGLKG YLDHKLEAET LPAEPFIIDN FSNGDSYLDA 250
    VFCWCEDLSE SIKNSYVNLI PTPQDGTHVT GLKNGIYDAI KAYIEKNSLS 300
    VKNIKITAND SFAQLNYVIS VKITNPQFAG QTKEKLSNKD VTNFVATAVK 350
    DLLTIWLNQN PDEARQIVEN ISKVAQKRIN ADKKTTRKRI MNTTIRLPGK 400
    LTDCISSDVN STELFIVEGD SAGGSAKQAR DKNFQAVLPL KGKILNSWEL 450
    DADTIMNSQE IHNIATAIGV DPDSDDISAL RYNKICILAD ADSDGLHIAT 500
    LLCAMFLKHF RKLIENGHIY IAQPPLFRID IGKSTFYALD ENERDTILTK 550
    NSKLPGKVNI MRFKGLGEMN PAQLRESAMD VSSRRLLQLT ISDVYDDTEM 600
    LDMLLAKKRA KDRRDWLENY GDRASVE 627
    Length:627
    Mass (Da):70,355
    Last modified:April 4, 2006 - v1
    Checksum:i4BA9C405648B7393
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM233362 Genomic DNA. Translation: CAJ80165.1.
    RefSeqiYP_514357.1. NC_007880.1.

    Genome annotation databases

    EnsemblBacteriaiCAJ80165; CAJ80165; FTL_1726.
    GeneIDi3951577.
    KEGGiftl:FTL_1726.
    PATRICi17944687. VBIFraTul90181_1881.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM233362 Genomic DNA. Translation: CAJ80165.1 .
    RefSeqi YP_514357.1. NC_007880.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4HXZ X-ray 2.70 A/B 1-382 [» ]
    4HY1 X-ray 1.90 A/B 1-382 [» ]
    4HYM X-ray 1.90 A/B 1-382 [» ]
    4KQV X-ray 2.38 A/B 1-382 [» ]
    ProteinModelPortali Q2A1P5.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAJ80165 ; CAJ80165 ; FTL_1726 .
    GeneIDi 3951577.
    KEGGi ftl:FTL_1726.
    PATRICi 17944687. VBIFraTul90181_1881.

    Phylogenomic databases

    HOGENOMi HOG000075154.
    KOi K02622.
    OMAi QSYNADA.
    OrthoDBi EOG6P334W.

    Enzyme and pathway databases

    BioCyci FTUL376619:GI22-1770-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_00938. ParE_type1.
    InterProi IPR002288. DNA_gyrase_B_C.
    IPR003594. HATPase_ATP-bd.
    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.
    IPR005737. TopoIV_B_Gneg.
    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 TIGR01055. parE_Gneg. 1 hit.
    PROSITEi PS00177. TOPOISOMERASE_II. 1 hit.
    PS50880. TOPRIM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete genome sequence of Francisella tularensis LVS (Live Vaccine Strain)."
      Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S., Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R., Garcia E.
      Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LVSImported.
    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 (1.90 ANGSTROMS) OF 1-382.
    3. "A new class of type iia topoisomerase inhibitors withbroad-spectrum antibacterial activity."
      Tari L.W., Bensen D.C., Finn J.
      Submitted (MAY-2013) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 1-382.

    Entry informationi

    Entry nameiQ2A1P5_FRATH
    AccessioniPrimary (citable) accession number: Q2A1P5
    Entry historyi
    Integrated into UniProtKB/TrEMBL: April 4, 2006
    Last sequence update: April 4, 2006
    Last modified: October 1, 2014
    This is version 65 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported, Complete proteomeImported

    External Data

    Dasty 3