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P17865

- FTSZ_BACSU

UniProt

P17865 - FTSZ_BACSU

Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 3 (16 Jun 2009)
      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.2 PublicationsUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi104 – 1129GTPUniRule annotation

    GO - Molecular functioni

    1. GTPase activity Source: CACAO
    2. GTP binding Source: UniProtKB-HAMAP
    3. identical protein binding Source: IntAct
    4. protein binding Source: IntAct

    GO - Biological processi

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

    Keywords - Biological processi

    Cell cycle, Cell division, Septation

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU15290-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cell division protein FtsZUniRule annotation
    Gene namesi
    Name:ftsZUniRule annotation
    Ordered Locus Names:BSU15290
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU15290. [Micado]

    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. cell septum Source: CACAO
    3. cytoplasm Source: UniProtKB-SubCell
    4. protein complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 382382Cell division protein FtsZPRO_0000114341Add
    BLAST

    Proteomic databases

    PaxDbiP17865.

    Interactioni

    Subunit structurei

    Homodimer. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner By similarity. Interacts directly with several other division proteins By similarity. Interacts with FtsA.1 PublicationUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself6EBI-1569853,EBI-1569853
    ezrAO348944EBI-1569853,EBI-1567579
    ftsAP282647EBI-1569853,EBI-2122615
    sepFO317288EBI-1569853,EBI-2122748
    ugtPP541663EBI-1569853,EBI-1567571
    zapAP945424EBI-1569853,EBI-2122911

    Protein-protein interaction databases

    IntActiP17865. 9 interactions.
    MINTiMINT-126054.
    STRINGi224308.BSU15290.

    Structurei

    Secondary structure

    1
    382
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 196
    Helixi20 – 3213
    Beta strandi39 – 468
    Helixi47 – 515
    Beta strandi56 – 605
    Helixi63 – 664
    Helixi75 – 8410
    Helixi86 – 938
    Beta strandi97 – 10812
    Helixi109 – 12315
    Beta strandi127 – 1348
    Helixi137 – 1393
    Helixi141 – 15717
    Beta strandi159 – 1657
    Helixi166 – 1727
    Helixi179 – 19820
    Turni199 – 2013
    Beta strandi205 – 2073
    Helixi211 – 2177
    Beta strandi221 – 23313
    Helixi236 – 24510
    Helixi254 – 2563
    Beta strandi258 – 2669
    Helixi272 – 28514
    Beta strandi291 – 2988
    Beta strandi303 – 31513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RHHX-ray2.00A12-315[»]
    2RHJX-ray1.76A12-315[»]
    2RHLX-ray2.45A/B12-315[»]
    2RHOX-ray2.45A/B12-315[»]
    2VAMX-ray2.50A1-382[»]
    2VXYX-ray1.70A1-382[»]
    ProteinModelPortaliP17865.
    SMRiP17865. Positions 11-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17865.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FtsZ family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0206.
    HOGENOMiHOG000049094.
    KOiK03531.
    OrthoDBiEOG6S7XZG.
    PhylomeDBiP17865.

    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.

    P17865-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLEFETNIDG LASIKVIGVG GGGNNAVNRM IENEVQGVEY IAVNTDAQAL    50
    NLSKAEVKMQ IGAKLTRGLG AGANPEVGKK AAEESKEQIE EALKGADMVF 100
    VTAGMGGGTG TGAAPVIAQI AKDLGALTVG VVTRPFTFEG RKRQLQAAGG 150
    ISAMKEAVDT LIVIPNDRIL EIVDKNTPML EAFREADNVL RQGVQGISDL 200
    IATPGLINLD FADVKTIMSN KGSALMGIGI ATGENRAAEA AKKAISSPLL 250
    EAAIDGAQGV LMNITGGTNL SLYEVQEAAD IVASASDQDV NMIFGSVINE 300
    NLKDEIVVTV IATGFIEQEK DVTKPQRPSL NQSIKTHNQS VPKREPKREE 350
    PQQQNTVSRH TSQPADDTLD IPTFLRNRNK RG 382
    Length:382
    Mass (Da):40,395
    Last modified:June 16, 2009 - v3
    Checksum:i24E908DEC9685614
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti345 – 3462EP → DA in AAA22457. (PubMed:3139638)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22630 Genomic DNA. Translation: AAA22457.1.
    AL009126 Genomic DNA. Translation: CAB13402.2.
    J05400 Genomic DNA. Translation: AAA83361.1.
    PIRiI39848.
    RefSeqiNP_389412.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13402; CAB13402; BSU15290.
    GeneIDi935971.
    KEGGibsu:BSU15290.
    PATRICi18974863. VBIBacSub10457_1623.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22630 Genomic DNA. Translation: AAA22457.1 .
    AL009126 Genomic DNA. Translation: CAB13402.2 .
    J05400 Genomic DNA. Translation: AAA83361.1 .
    PIRi I39848.
    RefSeqi NP_389412.2. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RHH X-ray 2.00 A 12-315 [» ]
    2RHJ X-ray 1.76 A 12-315 [» ]
    2RHL X-ray 2.45 A/B 12-315 [» ]
    2RHO X-ray 2.45 A/B 12-315 [» ]
    2VAM X-ray 2.50 A 1-382 [» ]
    2VXY X-ray 1.70 A 1-382 [» ]
    ProteinModelPortali P17865.
    SMRi P17865. Positions 11-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P17865. 9 interactions.
    MINTi MINT-126054.
    STRINGi 224308.BSU15290.

    Chemistry

    BindingDBi P17865.
    ChEMBLi CHEMBL5690.

    Proteomic databases

    PaxDbi P17865.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13402 ; CAB13402 ; BSU15290 .
    GeneIDi 935971.
    KEGGi bsu:BSU15290.
    PATRICi 18974863. VBIBacSub10457_1623.

    Organism-specific databases

    GenoListi BSU15290. [Micado ]

    Phylogenomic databases

    eggNOGi COG0206.
    HOGENOMi HOG000049094.
    KOi K03531.
    OrthoDBi EOG6S7XZG.
    PhylomeDBi P17865.

    Enzyme and pathway databases

    BioCyci BSUB:BSU15290-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P17865.

    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. "Cloning and characterization of Bacillus subtilis homologs of Escherichia coli cell division genes ftsZ and ftsA."
      Beall B., Lowe M., Lutkenhaus J.
      J. Bacteriol. 170:4855-4864(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 345-346.
    4. "Cloning, genetic organization, and characterization of a structural gene encoding bacillopeptidase F from Bacillus subtilis."
      Wu X.-C., Nathoo S., Pang A.S.-H., Carne T., Wang S.-L.
      J. Biol. Chem. 265:6845-6850(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 371-382.
    5. "Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins."
      Anderson D.E., Gueiros-Filho F.J., Erickson H.P.
      J. Bacteriol. 186:5775-5781(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: JDB401.
    6. "Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly."
      Jensen S.O., Thompson L.S., Harry E.J.
      J. Bacteriol. 187:6536-6544(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FTSA.
      Strain: 168.
    7. "Structural insights into the conformational variability of FtsZ."
      Oliva M.A., Trambaiolo D., Lowe J.
      J. Mol. Biol. 373:1229-1242(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    8. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
    9. "Combined protein construct and synthetic gene engineering for heterologous protein expression and crystallization using Gene Composer."
      Raymond A., Lovell S., Lorimer D., Walchli J., Mixon M., Wallace E., Thompkins K., Archer K., Burgin A., Stewart L.
      BMC Biotechnol. 9:37-37(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 12-315.

    Entry informationi

    Entry nameiFTSZ_BACSU
    AccessioniPrimary (citable) accession number: P17865
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 119 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3