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P0A9A6 (FTSZ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cell division protein FtsZ
Gene names
Name:ftsZ
Synonyms:sfiB, sulB
Ordered Locus Names:b0095, JW0093
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length383 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00909

Enzyme regulation

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. Ref.16 Ref.24 Ref.25 Ref.26

Subunit structure

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. Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.23 Ref.24 Ref.25 Ref.26

Subcellular location

Cytoplasm. Note: Assembles at midcell at the inner surface of the cytoplasmic membrane. Ref.10 Ref.17

Domain

The central and C-terminal regions are required for dimerization. Ref.19

Sequence similarities

Belongs to the FtsZ family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 383383Cell division protein FtsZ HAMAP-Rule MF_00909
PRO_0000114349

Regions

Nucleotide binding103 – 1119GTP Potential

Experimental info

Mutagenesis1 – 3232Missing: No interaction with MreB or YeeV.
Mutagenesis33 – 4917Missing: No interaction with CtpA.
Mutagenesis1051G → F in FtsZ-84; loss of GTPase-activity and conversion to an ATPase.
Mutagenesis1081T → A in FtsZ-Z3; lethal; greatly reduced GTP binding.
Mutagenesis317 – 38367Missing: No interaction with MreB or CbtA (YeeV).
Sequence conflict32 – 398ERIEGVEF → DALKVLNS in AAA23818. Ref.5
Sequence conflict1581D → N in CAA38872. Ref.1
Sequence conflict2221Y → H in CAA38872. Ref.1

Secondary structure

... 383
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A9A6 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: B3A53340367DBBA0

FASTA38340,324
        10         20         30         40         50         60 
MFEPMELTND AVIKVIGVGG GGGNAVEHMV RERIEGVEFF AVNTDAQALR KTAVGQTIQI 

        70         80         90        100        110        120 
GSGITKGLGA GANPEVGRNA ADEDRDALRA ALEGADMVFI AAGMGGGTGT GAAPVVAEVA 

       130        140        150        160        170        180 
KDLGILTVAV VTKPFNFEGK KRMAFAEQGI TELSKHVDSL ITIPNDKLLK VLGRGISLLD 

       190        200        210        220        230        240 
AFGAANDVLK GAVQGIAELI TRPGLMNVDF ADVRTVMSEM GYAMMGSGVA SGEDRAEEAA 

       250        260        270        280        290        300 
EMAISSPLLE DIDLSGARGV LVNITAGFDL RLDEFETVGN TIRAFASDNA TVVIGTSLDP 

       310        320        330        340        350        360 
DMNDELRVTV VATGIGMDKR PEITLVTNKQ VQQPVMDRYQ QHGMAPLTQE QKPVAKVVND 

       370        380 
NAPQTAKEPD YLDIPAFLRK QAD 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"FtsZ dimerization in vivo."
Di Lallo G., Anderluzzi D., Ghelardini P., Paolozzi L.
Mol. Microbiol. 32:265-274(1999) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRCEECZ. G64731.
RefSeqNP_414637.1. NC_000913.3.
YP_488400.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F47X-ray1.95A367-383[»]
ProteinModelPortalP0A9A6.
SMRP0A9A6. Positions 24-316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-31873N.
IntActP0A9A6. 59 interactions.
MINTMINT-8092601.
STRING511145.b0095.

Chemistry

BindingDBP0A9A6.
ChEMBLCHEMBL3999.

2D gel databases

SWISS-2DPAGEP0A9A6.

Proteomic databases

PaxDbP0A9A6.
PRIDEP0A9A6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73206; AAC73206; b0095.
BAB96663; BAB96663; BAB96663.
GeneID12932893.
944786.
KEGGecj:Y75_p0094.
eco:b0095.
PATRIC32115295. VBIEscCol129921_0099.

Organism-specific databases

EchoBASEEB0343.
EcoGeneEG10347. ftsZ.

Phylogenomic databases

eggNOGCOG0206.
HOGENOMHOG000049094.
KOK03531.
OMAMAMMGIG.
OrthoDBEOG6S7XZG.
PhylomeDBP0A9A6.
ProtClustDBPRK09330.

Enzyme and pathway databases

BioCycEcoCyc:EG10347-MONOMER.
ECOL316407:JW0093-MONOMER.

Gene expression databases

GenevestigatorP0A9A6.

Family and domain databases

Gene3D3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
HAMAPMF_00909. FtsZ.
InterProIPR000158. 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]
PfamPF12327. FtsZ_C. 1 hit.
PF00091. Tubulin. 1 hit.
[Graphical view]
PRINTSPR00423. CELLDVISFTSZ.
SMARTSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
TIGRFAMsTIGR00065. ftsZ. 1 hit.
PROSITEPS01134. FTSZ_1. 1 hit.
PS01135. FTSZ_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A9A6.
PROP0A9A6.

Entry information

Entry nameFTSZ_ECOLI
AccessionPrimary (citable) accession number: P0A9A6
Secondary accession number(s): P06138, P77857, P78047
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 19, 2005
Last modified: April 16, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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