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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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.

Activity 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)DescriptionActionsGraphical viewLength
Binding sitei138GTPUniRule annotation1
Binding sitei142GTPUniRule annotation1
Binding sitei186GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi20 – 24GTPUniRule annotation5
Nucleotide bindingi107 – 109GTPUniRule annotation3

GO - Molecular functioni

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

GO - Biological processi

  • cell division Source: EcoliWiki
  • cell septum assembly Source: UniProtKB-UniRule
  • FtsZ-dependent cytokinesis Source: UniProtKB-UniRule
  • protein polymerization Source: EcoliWiki

Keywordsi

Biological processCell cycle, Cell division, Septation
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10347-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10347 ftsZ

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1 – 32Missing : No interaction with MreB or YeeV. Add BLAST32
Mutagenesisi33 – 49Missing : No interaction with CtpA. Add BLAST17
Mutagenesisi105G → S in FtsZ-84; loss of GTPase-activity and conversion to an ATPase. 1 Publication1
Mutagenesisi108T → A in FtsZ-Z3; lethal; greatly reduced GTP binding. 1
Mutagenesisi317 – 383Missing : No interaction with MreB or CbtA (YeeV). Add BLAST67

Chemistry databases

ChEMBLiCHEMBL3999

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001143491 – 383Cell division protein FtsZAdd BLAST383

Proteomic databases

EPDiP0A9A6
PaxDbiP0A9A6
PRIDEiP0A9A6

2D gel databases

SWISS-2DPAGEiP0A9A6

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi4261887, 577 interactors
DIPiDIP-31873N
IntActiP0A9A6, 61 interactors
MINTiP0A9A6
STRINGi316385.ECDH10B_0077

Chemistry databases

BindingDBiP0A9A6

Structurei

Secondary structure

1383
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0A9A6
SMRiP0A9A6
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
OMAiMRAVKGI
PhylomeDBiP0A9A6

Family and domain databases

CDDicd02201 FtsZ_type1, 1 hit
Gene3Di3.40.50.1440, 1 hit
HAMAPiMF_00909 FtsZ, 1 hit
InterProiView protein in InterPro
IPR000158 Cell_div_FtsZ
IPR020805 Cell_div_FtsZ_CS
IPR024757 FtsZ_C
IPR008280 Tub_FtsZ_C
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR003008 Tubulin_FtsZ_GTPase
PfamiView protein in Pfam
PF12327 FtsZ_C, 1 hit
PF00091 Tubulin, 1 hit
PRINTSiPR00423 CELLDVISFTSZ
SMARTiView protein in SMART
SM00864 Tubulin, 1 hit
SM00865 Tubulin_C, 1 hit
SUPFAMiSSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit
TIGRFAMsiTIGR00065 ftsZ, 1 hit
PROSITEiView protein in PROSITE
PS01134 FTSZ_1, 1 hit
PS01135 FTSZ_2, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti32 – 39ERIEGVEF → DALKVLNS in AAA23818 (PubMed:6094474).Curated8
Sequence conflicti158D → N in CAA38872 (PubMed:3000876).Curated1
Sequence conflicti222Y → H in CAA38872 (PubMed:3000876).Curated1

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
PATRICifig|1411691.4.peg.2185

Similar proteinsi

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F47X-ray1.95A367-383[»]
5HAWX-ray1.89K/L370-379[»]
5HBUX-ray2.60K370-379[»]
5HSZX-ray2.30K372-382[»]
5K58X-ray2.77K/L/M/N372-379[»]
5KOAX-ray2.67D370-381[»]
ProteinModelPortaliP0A9A6
SMRiP0A9A6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261887, 577 interactors
DIPiDIP-31873N
IntActiP0A9A6, 61 interactors
MINTiP0A9A6
STRINGi316385.ECDH10B_0077

Chemistry databases

BindingDBiP0A9A6
ChEMBLiCHEMBL3999

2D gel databases

SWISS-2DPAGEiP0A9A6

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
PATRICifig|1411691.4.peg.2185

Organism-specific databases

EchoBASEiEB0343
EcoGeneiEG10347 ftsZ

Phylogenomic databases

eggNOGiENOG4105CDK Bacteria
COG0206 LUCA
HOGENOMiHOG000049094
InParanoidiP0A9A6
KOiK03531
OMAiMRAVKGI
PhylomeDBiP0A9A6

Enzyme and pathway databases

BioCyciEcoCyc:EG10347-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A9A6
PROiPR:P0A9A6

Family and domain databases

CDDicd02201 FtsZ_type1, 1 hit
Gene3Di3.40.50.1440, 1 hit
HAMAPiMF_00909 FtsZ, 1 hit
InterProiView protein in InterPro
IPR000158 Cell_div_FtsZ
IPR020805 Cell_div_FtsZ_CS
IPR024757 FtsZ_C
IPR008280 Tub_FtsZ_C
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR003008 Tubulin_FtsZ_GTPase
PfamiView protein in Pfam
PF12327 FtsZ_C, 1 hit
PF00091 Tubulin, 1 hit
PRINTSiPR00423 CELLDVISFTSZ
SMARTiView protein in SMART
SM00864 Tubulin, 1 hit
SM00865 Tubulin_C, 1 hit
SUPFAMiSSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit
TIGRFAMsiTIGR00065 ftsZ, 1 hit
PROSITEiView protein in PROSITE
PS01134 FTSZ_1, 1 hit
PS01135 FTSZ_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiFTSZ_ECOLI
AccessioniPrimary (citable) accession number: P0A9A6
Secondary accession number(s): P06138, P77857, P78047
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 19, 2005
Last modified: October 10, 2018
This is version 123 of the entry and version 1 of the sequence. See 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  4. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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