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Q8DQB5

- Q8DQB5_STRR6

UniProt

Q8DQB5 - Q8DQB5_STRR6

Protein

DNA topoisomerase 4 subunit B

Gene

parE

Organism
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Status
Unreviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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 sitei11 – 111ATPUniRule annotation
    Binding sitei51 – 511ATPUniRule annotation
    Binding sitei78 – 781ATPUniRule annotation
    Binding sitei344 – 3441ATPUniRule annotation
    Metal bindingi433 – 4331Magnesium 1; catalyticUniRule annotation
    Sitei458 – 4581Interaction with DNAUniRule annotation
    Sitei461 – 4611Interaction with DNAUniRule annotation
    Metal bindingi506 – 5061Magnesium 1; catalyticUniRule annotation
    Metal bindingi506 – 5061Magnesium 2UniRule annotation
    Metal bindingi508 – 5081Magnesium 2UniRule annotation
    Sitei513 – 5131Interaction with DNAUniRule annotation
    Sitei629 – 6291Interaction with DNAUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi118 – 1247ATPUniRule 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

    BioCyciSPNE171101:GJC8-763-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:spr0756Imported
    OrganismiStreptococcus pneumoniae (strain ATCC BAA-255 / R6)Imported
    Taxonomic identifieri171101 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000000586: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. chromosome Source: InterPro

    Interactioni

    Subunit structurei

    Heterotetramer composed of ParC and ParE.UniRule annotation

    Protein-protein interaction databases

    STRINGi171101.spr0756.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4LP0X-ray1.95A1-226[»]
    4LPBX-ray1.75A1-226[»]
    4MOTX-ray1.75A1-226[»]
    ProteinModelPortaliQ8DQB5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini427 – 541115ToprimUniRule 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

    eggNOGiCOG0187.
    HOGENOMiHOG000075154.
    KOiK02622.
    OMAiREEFHYE.
    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.

    Q8DQB5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKKEININN YNDDAIQVLE GLDAVRKRPG MYIGSTDGAG LHHLVWEIVD    50
    NAVDEALSGF GDRIDVTINK DGSLTVQDHG RGMPTGMHAM GIPTVEVIFT 100
    ILHAGGKFGQ GGYKTSGGLH GVGSSVVNAL SSWLEVEITR DGAVYKQRFE 150
    NGGKPVTTLK KIGTALKSKT GTKVTFMPDA TIFSTTDFKY NTISERLNES 200
    AFLLKNVTLS LTDKRTDEAI EFHYENGVQD FVSYLNEDKE ILTPVLYFEG 250
    EDNGFQVEVA LQYNDGFSDN ILSFVNNVRT KDGGTHETGL KSAITKVMND 300
    YARKTGLLKE KDKNLEGSDY REGLAAVLSI LVPEEHLQFE GQTKDKLGSP 350
    LARPVVDGIV ADKLTFFLME NGELASNLIR KAIKARDARE AARKARDESR 400
    NGKKNKKDKG LLSGKLTPAQ SKNPAKNELY LVEGDSAGGS AKQGRDRKFQ 450
    AILPLRGKVI NTAKAKMADI LKNEEINTMI YTIGAGVGAD FSIEDANYDK 500
    IIIMTDADTD GAHIQTLLLT FFYRYMRPLV EAGHVYIALP PLYKMSKGKG 550
    KKEEVAYAWT DGELEELRKQ FGKGATLQRY KGLGEMNADQ LWETTMNPET 600
    RTLIRVTIED LARAERRVNV LMGDKVEPRR KWIEDNVKFT LEEATVF 647
    Length:647
    Mass (Da):71,665
    Last modified:March 1, 2003 - v1
    Checksum:i0AF7382C72772713
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE007317 Genomic DNA. Translation: AAK99560.1.
    PIRiD97966.
    RefSeqiNP_358350.1. NC_003098.1.

    Genome annotation databases

    EnsemblBacteriaiAAK99560; AAK99560; spr0756.
    GeneIDi934298.
    KEGGispr:spr0756.
    PATRICi19701428. VBIStrPne107296_0836.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE007317 Genomic DNA. Translation: AAK99560.1 .
    PIRi D97966.
    RefSeqi NP_358350.1. NC_003098.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4LP0 X-ray 1.95 A 1-226 [» ]
    4LPB X-ray 1.75 A 1-226 [» ]
    4MOT X-ray 1.75 A 1-226 [» ]
    ProteinModelPortali Q8DQB5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 171101.spr0756.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK99560 ; AAK99560 ; spr0756 .
    GeneIDi 934298.
    KEGGi spr:spr0756.
    PATRICi 19701428. VBIStrPne107296_0836.

    Phylogenomic databases

    eggNOGi COG0187.
    HOGENOMi HOG000075154.
    KOi K02622.
    OMAi REEFHYE.
    OrthoDBi EOG6P334W.

    Enzyme and pathway databases

    BioCyci SPNE171101:GJC8-763-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 BAA-255 / R6Imported.
    2. "Fragment-to-hit-to-lead discovery of a novel pyridylurea scaffold of ATP competitive dual targeting type II topoisomerase inhibiting antibacterial agents."
      Basarab G.S., Manchester J.I., Bist S., Boriack-Sjodin P.A., Dangel B., Illingworth R., Sherer B.A., Sriram S., Uria-Nickelsen M., Eakin A.E.
      J. Med. Chem. 56:8712-8735(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-226.
    3. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-226.

    Entry informationi

    Entry nameiQ8DQB5_STRR6
    AccessioniPrimary (citable) accession number: Q8DQB5
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 1, 2003
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 92 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