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P0A9A6

- FTSZ_ECOLI

UniProt

P0A9A6 - FTSZ_ECOLI

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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

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

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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiP0A9A6.
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

        10         20         30         40         50
MFEPMELTND AVIKVIGVGG GGGNAVEHMV RERIEGVEFF AVNTDAQALR
60 70 80 90 100
KTAVGQTIQI GSGITKGLGA GANPEVGRNA ADEDRDALRA ALEGADMVFI
110 120 130 140 150
AAGMGGGTGT GAAPVVAEVA KDLGILTVAV VTKPFNFEGK KRMAFAEQGI
160 170 180 190 200
TELSKHVDSL ITIPNDKLLK VLGRGISLLD AFGAANDVLK GAVQGIAELI
210 220 230 240 250
TRPGLMNVDF ADVRTVMSEM GYAMMGSGVA SGEDRAEEAA EMAISSPLLE
260 270 280 290 300
DIDLSGARGV LVNITAGFDL RLDEFETVGN TIRAFASDNA TVVIGTSLDP
310 320 330 340 350
DMNDELRVTV VATGIGMDKR PEITLVTNKQ VQQPVMDRYQ QHGMAPLTQE
360 370 380
QKPVAKVVND NAPQTAKEPD YLDIPAFLRK QAD
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.
InParanoidi P0A9A6.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 90 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