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P0A9A6

- FTSZ_ECOLI

UniProt

P0A9A6 - FTSZ_ECOLI

Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (19 Jul 2005)
      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. Polymerization and bundle formation is enhanced by CbeA.

    Enzyme regulationi

    Formation of the FtsZ ring is inhibited by SulA, MinCD, DicB and toxins CbtA and CptA. Inhibition by toxin CbtA, SulA or DicB overexpression is neutralized by cytoskeleton bundling-enhancing protein CbeA, while inhibition by toxin CptA is neutralized by antitoxin CptB.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi103 – 1119GTPUniRule annotation

    GO - Molecular functioni

    1. GTPase activity Source: EcoliWiki
    2. GTP binding Source: EcoliWiki
    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: EcoliWiki

    Keywords - Biological processi

    Cell cycle, Cell division, Septation

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10347-MONOMER.
    ECOL316407:JW0093-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cell division protein FtsZUniRule annotation
    Gene namesi
    Name:ftsZUniRule annotation
    Synonyms:sfiB, sulB
    Ordered Locus Names:b0095, JW0093
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10347. ftsZ.

    Subcellular locationi

    Cytoplasm 2 PublicationsUniRule annotation
    Note: Assembles at midcell at the inner surface of the cytoplasmic membrane.

    GO - Cellular componenti

    1. cell division site Source: EcoliWiki
    2. cytoplasm Source: EcoliWiki
    3. protein complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1 – 3232Missing: No interaction with MreB or YeeV. Add
    BLAST
    Mutagenesisi33 – 4917Missing: No interaction with CtpA. Add
    BLAST
    Mutagenesisi105 – 1051G → F in FtsZ-84; loss of GTPase-activity and conversion to an ATPase.
    Mutagenesisi108 – 1081T → A in FtsZ-Z3; lethal; greatly reduced GTP binding.
    Mutagenesisi317 – 38367Missing: No interaction with MreB or CbtA (YeeV). Add
    BLAST

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 383383Cell division protein FtsZPRO_0000114349Add
    BLAST

    Proteomic databases

    PaxDbiP0A9A6.
    PRIDEiP0A9A6.

    2D gel databases

    SWISS-2DPAGEP0A9A6.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A9A6.

    Interactioni

    Subunit structurei

    Homodimer. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner. Polymers persist as long as GTP is present and disappear rapidly as soon as it is consumed. Interacts directly with several other division proteins, including FtsA and ZipA. Interacts with polymerization inhibitors SulA, CbtA and CptA. Interacts with MreB and polymerization bundling-enhancing factor CbeA.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself7EBI-370963,EBI-370963
    cbeAP763642EBI-370963,EBI-1126877
    ftsAP0ABH06EBI-370963,EBI-550562
    ftsEP0A9R72EBI-370963,EBI-550637
    mreBP0A9X46EBI-370963,EBI-371008
    rlmNP369793EBI-370963,EBI-559071
    zapCP758624EBI-370963,EBI-552519
    zapDP366803EBI-370963,EBI-1113728
    zipAP771734EBI-370963,EBI-1029213

    Protein-protein interaction databases

    DIPiDIP-31873N.
    IntActiP0A9A6. 59 interactions.
    MINTiMINT-8092601.
    STRINGi511145.b0095.

    Structurei

    Secondary structure

    1
    383
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi374 – 3829

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F47X-ray1.95A367-383[»]
    ProteinModelPortaliP0A9A6.
    SMRiP0A9A6. Positions 24-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A9A6.

    Family & Domainsi

    Domaini

    The central and C-terminal regions are required for dimerization.1 Publication

    Sequence similaritiesi

    Belongs to the FtsZ family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0206.
    HOGENOMiHOG000049094.
    KOiK03531.
    OMAiQIGNGIT.
    OrthoDBiEOG6S7XZG.
    PhylomeDBiP0A9A6.

    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.

    P0A9A6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFEPMELTND AVIKVIGVGG GGGNAVEHMV RERIEGVEFF AVNTDAQALR    50
    KTAVGQTIQI GSGITKGLGA GANPEVGRNA ADEDRDALRA ALEGADMVFI 100
    AAGMGGGTGT GAAPVVAEVA KDLGILTVAV VTKPFNFEGK KRMAFAEQGI 150
    TELSKHVDSL ITIPNDKLLK VLGRGISLLD AFGAANDVLK GAVQGIAELI 200
    TRPGLMNVDF ADVRTVMSEM GYAMMGSGVA SGEDRAEEAA EMAISSPLLE 250
    DIDLSGARGV LVNITAGFDL RLDEFETVGN TIRAFASDNA TVVIGTSLDP 300
    DMNDELRVTV VATGIGMDKR PEITLVTNKQ VQQPVMDRYQ QHGMAPLTQE 350
    QKPVAKVVND NAPQTAKEPD YLDIPAFLRK QAD 383
    Length:383
    Mass (Da):40,324
    Last modified:July 19, 2005 - v1
    Checksum:iB3A53340367DBBA0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 398ERIEGVEF → DALKVLNS in AAA23818. (PubMed:6094474)Curated
    Sequence conflicti158 – 1581D → N in CAA38872. (PubMed:3000876)Curated
    Sequence conflicti222 – 2221Y → H in CAA38872. (PubMed:3000876)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC73206.1.
    AP009048 Genomic DNA. Translation: BAB96663.2.
    X55034 Genomic DNA. Translation: CAA38872.1.
    K02668 Genomic DNA. Translation: AAA23818.1.
    M19211 Genomic DNA. Translation: AAA83848.1.
    PIRiG64731. CEECZ.
    RefSeqiNP_414637.1. NC_000913.3.
    YP_488400.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73206; AAC73206; b0095.
    BAB96663; BAB96663; BAB96663.
    GeneIDi12932893.
    944786.
    KEGGiecj:Y75_p0094.
    eco:b0095.
    PATRICi32115295. VBIEscCol129921_0099.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC73206.1 .
    AP009048 Genomic DNA. Translation: BAB96663.2 .
    X55034 Genomic DNA. Translation: CAA38872.1 .
    K02668 Genomic DNA. Translation: AAA23818.1 .
    M19211 Genomic DNA. Translation: AAA83848.1 .
    PIRi G64731. CEECZ.
    RefSeqi NP_414637.1. NC_000913.3.
    YP_488400.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F47 X-ray 1.95 A 367-383 [» ]
    ProteinModelPortali P0A9A6.
    SMRi P0A9A6. Positions 24-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-31873N.
    IntActi P0A9A6. 59 interactions.
    MINTi MINT-8092601.
    STRINGi 511145.b0095.

    Chemistry

    BindingDBi P0A9A6.
    ChEMBLi CHEMBL3999.

    2D gel databases

    SWISS-2DPAGE P0A9A6.

    Proteomic databases

    PaxDbi P0A9A6.
    PRIDEi P0A9A6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73206 ; AAC73206 ; b0095 .
    BAB96663 ; BAB96663 ; BAB96663 .
    GeneIDi 12932893.
    944786.
    KEGGi ecj:Y75_p0094.
    eco:b0095.
    PATRICi 32115295. VBIEscCol129921_0099.

    Organism-specific databases

    EchoBASEi EB0343.
    EcoGenei EG10347. ftsZ.

    Phylogenomic databases

    eggNOGi COG0206.
    HOGENOMi HOG000049094.
    KOi K03531.
    OMAi QIGNGIT.
    OrthoDBi EOG6S7XZG.
    PhylomeDBi P0A9A6.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10347-MONOMER.
    ECOL316407:JW0093-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A9A6.
    PROi P0A9A6.

    Gene expression databases

    Genevestigatori P0A9A6.

    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. "The nucleotide sequence of the essential cell-division gene ftsZ of Escherichia coli."
      Yi Q.-M., Lutkenhaus J.
      Gene 36:241-247(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
      Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
      Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 158 AND 222.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "DNA sequence and transcriptional organization of essential cell division genes ftsQ and ftsA of Escherichia coli: evidence for overlapping transcriptional units."
      Robinson A.C., Kenan D.J., Hatfull G.F., Sullivan N.F., Spiegelberg R., Donachie W.D.
      J. Bacteriol. 160:546-555(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
    6. "Structure and expression of the cell division genes ftsQ, ftsA and ftsZ."
      Yi Q.-M., Rockenbach S., Ward J.E. Jr., Lutkenhaus J.
      J. Mol. Biol. 184:399-412(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
      Strain: K12.
    7. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
      Submitted (FEB-1996) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-12.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12.
      Strain: K12 / EMG2.
    9. "Sequence analysis, transcriptional organization, and insertional mutagenesis of the envA gene of Escherichia coli."
      Beall B., Lutkenhaus J.
      J. Bacteriol. 169:5408-5415(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-383.
      Strain: K12.
    10. "FtsZ ring structure associated with division in Escherichia coli."
      Bi E., Lutkenhaus J.
      Nature 354:161-164(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, RING-LIKE STRUCTURE.
    11. "Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein."
      Raychaudhuri D., Park J.T.
      Nature 359:251-254(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: GTPASE ACTIVITY.
    12. "The essential bacterial cell-division protein FtsZ is a GTPase."
      de Boer P., Crossley R., Rothfield L.
      Nature 359:254-256(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: GTPASE ACTIVITY.
    13. "Guanine nucleotide-dependent assembly of FtsZ into filaments."
      Mukherjee A., Lutkenhaus J.
      J. Bacteriol. 176:2754-2758(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: GTP-DEPENDENT FILAMENT FORMATION.
    14. "GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubules."
      Bramhill D., Thompson C.M.
      Proc. Natl. Acad. Sci. U.S.A. 91:5813-5817(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: GTP-DEPENDENT FILAMENT FORMATION.
    15. "A point mutation converts Escherichia coli FtsZ septation GTPase to an ATPase."
      Raychaudhuri D., Park J.T.
      J. Biol. Chem. 269:22941-22944(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTANTS.
    16. "Interaction between FtsZ and inhibitors of cell division."
      Huang J., Cao C., Lutkenhaus J.
      J. Bacteriol. 178:5080-5085(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, INTERACTION WITH SULA.
    17. "Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein."
      Ma X., Ehrhardt D.W., Margolin W.
      Proc. Natl. Acad. Sci. U.S.A. 93:12998-13003(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH FTSA.
    18. "Dynamic assembly of FtsZ regulated by GTP hydrolysis."
      Mukherjee A., Lutkenhaus J.
      EMBO J. 17:462-469(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, GTPASE ACTIVITY.
    19. Cited for: SUBUNIT, DOMAIN.
      Strain: K12.
    20. "Rate-limiting guanosine 5'-triphosphate hydrolysis during nucleotide turnover by FtsZ, a prokaryotic tubulin homologue involved in bacterial cell division."
      Romberg L., Mitchison T.J.
      Biochemistry 43:282-288(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, GTPASE ACTIVITY.
    21. "Molecular evolution of FtsZ protein sequences encoded within the genomes of archaea, bacteria, and eukaryota."
      Vaughan S., Wickstead B., Gull K., Addinall S.G.
      J. Mol. Evol. 58:19-29(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHYLOGENETIC STUDY.
    22. "Bacterial cell division and the septal ring."
      Weiss D.S.
      Mol. Microbiol. 54:588-597(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    23. "Interaction between cell division proteins FtsE and FtsZ."
      Corbin B.D., Wang Y., Beuria T.K., Margolin W.
      J. Bacteriol. 189:3026-3035(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FTSE.
      Strain: K12 / MG1655 / ATCC 47076.
    24. "YeeV is an Escherichia coli toxin that inhibits cell division by targeting the cytoskeleton proteins, FtsZ and MreB."
      Tan Q., Awano N., Inouye M.
      Mol. Microbiol. 79:109-118(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, INTERACTION WITH MREB AND CBTA.
      Strain: K12 / BW25113.
    25. "A novel membrane-bound toxin for cell division, CptA (YgfX), inhibits polymerization of cytoskeleton proteins, FtsZ and MreB, in Escherichia coli."
      Masuda H., Tan Q., Awano N., Yamaguchi Y., Inouye M.
      FEMS Microbiol. Lett. 328:174-181(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, INTERACTION WITH CPTA.
      Strain: B / BL21-DE3 and K12 / BW25113.
    26. "YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, antagonizing the CbtA (YeeV) toxicity in Escherichia coli."
      Masuda H., Tan Q., Awano N., Wu K.P., Inouye M.
      Mol. Microbiol. 84:979-989(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, INTERACTION WITH CBEA.
      Strain: K12 / BW25113.
    27. "The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography."
      Mosyak L., Zhang Y., Glasfeld E., Haney S., Stahl M., Seehra J., Somers W.S.
      EMBO J. 19:3179-3191(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 367-383 IN COMPLEX WITH ZIPA.

    Entry informationi

    Entry nameiFTSZ_ECOLI
    AccessioniPrimary (citable) accession number: P0A9A6
    Secondary accession number(s): P06138, P77857, P78047
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    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