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Q82AD5

- Q82AD5_STRAW

UniProt

Q82AD5 - Q82AD5_STRAW

Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.UniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi101 – 1099GTPUniRule annotation

    GO - Molecular functioni

    1. GTPase activity Source: UniProtKB-HAMAP
    2. GTP binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. barrier septum assembly Source: UniProtKB-KW
    2. FtsZ-dependent cytokinesis Source: UniProtKB-HAMAP
    3. protein polymerization Source: UniProtKB-HAMAP

    Keywords - Biological processi

    Cell cycle, Cell division, SeptationUniRule annotation

    Keywords - Ligandi

    GTP-bindingUniRule annotation, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciSAVE227882:GJU1-6204-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cell division protein FtsZUniRule annotation
    Gene namesi
    Name:ftsZUniRule annotationImported
    Ordered Locus Names:SAV_6124Imported
    OrganismiStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)Imported
    Taxonomic identifieri227882 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces
    ProteomesiUP000000428: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation
    Note: Assembles at midcell at the inner surface of the cytoplasmic membrane.UniRule annotation

    GO - Cellular componenti

    1. cell division site Source: UniProtKB-HAMAP
    2. cytoplasm Source: UniProtKB-SubCell
    3. protein complex Source: InterPro

    Keywords - Cellular componenti

    CytoplasmUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner.UniRule annotation
    Homodimer. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner. Interacts directly with several other division proteins.UniRule annotation

    Protein-protein interaction databases

    STRINGi227882.SAV_6124.

    Structurei

    3D structure databases

    ProteinModelPortaliQ82AD5.
    SMRiQ82AD5. Positions 22-312.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FtsZ family.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000049094.
    KOiK03531.
    OMAiNNAREEL.
    OrthoDBiEOG6S7XZG.

    Family and domain databases

    Gene3Di3.30.1330.20. 1 hit.
    3.40.50.1440. 1 hit.
    HAMAPiMF_00909. FtsZ.
    InterProiIPR000158. Cell_div_FtsZ.
    IPR020805. Cell_div_FtsZ_CS.
    IPR024757. FtsZ_C.
    IPR008280. Tub_FtsZ_C.
    IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
    IPR003008. Tubulin_FtsZ_GTPase.
    [Graphical view]
    PfamiPF12327. FtsZ_C. 1 hit.
    PF00091. Tubulin. 1 hit.
    [Graphical view]
    PRINTSiPR00423. CELLDVISFTSZ.
    SMARTiSM00864. Tubulin. 1 hit.
    SM00865. Tubulin_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF52490. SSF52490. 1 hit.
    SSF55307. SSF55307. 1 hit.
    TIGRFAMsiTIGR00065. ftsZ. 1 hit.
    PROSITEiPS01134. FTSZ_1. 1 hit.
    PS01135. FTSZ_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q82AD5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAPQNYLAV IKVIGVGGGG VNAINRMIEV GLKGVEFIAI NTDAQALLMS    50
    DADVKLDVGR ELTRGLGAGA NPAVGRKAAE DHREEIEEVL KGADMVFVTA 100
    GEGGGTGTGG APVVANIARS LGALTIGVVT RPFTFEGRRR ANQAEDGIAE 150
    LREEVDTLIV IPNDRLLSIS DRQVSVLDAF KSADQVLLSG VQGITDLITT 200
    PGLINLDFAD VKSVMSEAGS ALMGIGSARG DDRAVAAAEM AISSPLLEAS 250
    IDGARGVLLS ISGGSDLGLF EINEAAQLVS EAAHPEANII FGAVIDDALG 300
    DEVRVTVIAA GFDGGQPPSK RDTVLGSSSA KRDEPTPARP AESRPSFGSL 350
    GSVTPKEAPE PAPEPVNELP VSPPVPPSRT YSDSAAEELD VPDFLK 396
    Length:396
    Mass (Da):40,731
    Last modified:June 1, 2003 - v1
    Checksum:i406FBD03D389A523
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000030 Genomic DNA. Translation: BAC73835.1.
    RefSeqiNP_827300.1. NC_003155.4.

    Genome annotation databases

    EnsemblBacteriaiBAC73835; BAC73835; SAV_6124.
    GeneIDi1211412.
    KEGGisma:SAV_6124.
    PATRICi23726282. VBIStrAve112782_6494.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000030 Genomic DNA. Translation: BAC73835.1 .
    RefSeqi NP_827300.1. NC_003155.4.

    3D structure databases

    ProteinModelPortali Q82AD5.
    SMRi Q82AD5. Positions 22-312.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 227882.SAV_6124.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC73835 ; BAC73835 ; SAV_6124 .
    GeneIDi 1211412.
    KEGGi sma:SAV_6124.
    PATRICi 23726282. VBIStrAve112782_6494.

    Phylogenomic databases

    HOGENOMi HOG000049094.
    KOi K03531.
    OMAi NNAREEL.
    OrthoDBi EOG6S7XZG.

    Enzyme and pathway databases

    BioCyci SAVE227882:GJU1-6204-MONOMER.

    Family and domain databases

    Gene3Di 3.30.1330.20. 1 hit.
    3.40.50.1440. 1 hit.
    HAMAPi MF_00909. FtsZ.
    InterProi IPR000158. Cell_div_FtsZ.
    IPR020805. Cell_div_FtsZ_CS.
    IPR024757. FtsZ_C.
    IPR008280. Tub_FtsZ_C.
    IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
    IPR003008. Tubulin_FtsZ_GTPase.
    [Graphical view ]
    Pfami PF12327. FtsZ_C. 1 hit.
    PF00091. Tubulin. 1 hit.
    [Graphical view ]
    PRINTSi PR00423. CELLDVISFTSZ.
    SMARTi SM00864. Tubulin. 1 hit.
    SM00865. Tubulin_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52490. SSF52490. 1 hit.
    SSF55307. SSF55307. 1 hit.
    TIGRFAMsi TIGR00065. ftsZ. 1 hit.
    PROSITEi PS01134. FTSZ_1. 1 hit.
    PS01135. FTSZ_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
      Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
      Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680Imported.
    2. "Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
      Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
      Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiQ82AD5_STRAW
    AccessioniPrimary (citable) accession number: Q82AD5
    Entry historyi
    Integrated into UniProtKB/TrEMBL: June 1, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

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