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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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 (PubMed:21166897, PubMed:22239607, PubMed:22515815, PubMed:8752322). Either FtsA or ZipA is required for Z ring formation and stabilization (PubMed:11847116).5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei138 – 1381GTPUniRule annotation
Binding sitei142 – 1421GTPUniRule annotation
Binding sitei186 – 1861GTPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 245GTPUniRule annotation
Nucleotide bindingi107 – 1093GTPUniRule annotation

GO - Molecular functioni

  • GTPase activity Source: EcoliWiki
  • GTP binding Source: EcoliWiki
  • identical protein binding Source: IntAct

GO - Biological processi

  • cell division Source: CACAO
  • FtsZ-dependent cytokinesis Source: UniProtKB-HAMAP
  • 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
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10347. ftsZ.

Subcellular locationi

  • Cytoplasm UniRule annotation2 Publications

  • Note: Assembles at midcell at the inner surface of the cytoplasmic membrane.

GO - Cellular componenti

  • cell division site Source: EcoliWiki
  • cytoplasm Source: EcoliWiki
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

Chemistry

ChEMBLiCHEMBL3999.

PTM / Processingi

Molecule processing

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

Proteomic databases

EPDiP0A9A6.
PaxDbiP0A9A6.
PRIDEiP0A9A6.

2D gel databases

SWISS-2DPAGEP0A9A6.

Expressioni

Inductioni

Repressed 1.3-fold by hydroxyurea (at protein level).1 Publication

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
zapCP758625EBI-370963,EBI-552519
zapDP366803EBI-370963,EBI-1113728
zipAP771734EBI-370963,EBI-1029213

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4261887. 545 interactions.
DIPiDIP-31873N.
IntActiP0A9A6. 59 interactions.
MINTiMINT-8092601.
STRINGi511145.b0095.

Chemistry

BindingDBiP0A9A6.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F47X-ray1.95A367-383[»]
5HAWX-ray1.89K/L370-379[»]
5HBUX-ray2.60K370-379[»]
5HSZX-ray2.30K372-382[»]
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

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
HOGENOMiHOG000049094.
InParanoidiP0A9A6.
KOiK03531.
OMAiGMAMMGI.
PhylomeDBiP0A9A6.

Family and domain databases

Gene3Di3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
HAMAPiMF_00909. FtsZ. 1 hit.
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:
EMBLi
GenBanki
DDBJi
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.
WP_000462776.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73206; AAC73206; b0095.
BAB96663; BAB96663; BAB96663.
GeneIDi944786.
KEGGiecj:JW0093.
eco:b0095.
PATRICi32115295. VBIEscCol129921_0099.

Cross-referencesi

Web resourcesi

Protein Spotlight

Becoming two - Issue 171 of July 2015

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000462776.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F47X-ray1.95A367-383[»]
5HAWX-ray1.89K/L370-379[»]
5HBUX-ray2.60K370-379[»]
5HSZX-ray2.30K372-382[»]
ProteinModelPortaliP0A9A6.
SMRiP0A9A6. Positions 24-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261887. 545 interactions.
DIPiDIP-31873N.
IntActiP0A9A6. 59 interactions.
MINTiMINT-8092601.
STRINGi511145.b0095.

Chemistry

BindingDBiP0A9A6.
ChEMBLiCHEMBL3999.

2D gel databases

SWISS-2DPAGEP0A9A6.

Proteomic databases

EPDiP0A9A6.
PaxDbiP0A9A6.
PRIDEiP0A9A6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73206; AAC73206; b0095.
BAB96663; BAB96663; BAB96663.
GeneIDi944786.
KEGGiecj:JW0093.
eco:b0095.
PATRICi32115295. VBIEscCol129921_0099.

Organism-specific databases

EchoBASEiEB0343.
EcoGeneiEG10347. ftsZ.

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
HOGENOMiHOG000049094.
InParanoidiP0A9A6.
KOiK03531.
OMAiGMAMMGI.
PhylomeDBiP0A9A6.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A9A6.
PROiP0A9A6.

Family and domain databases

Gene3Di3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
HAMAPiMF_00909. FtsZ. 1 hit.
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]
ProtoNetiSearch...

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: September 7, 2016
This is version 105 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.