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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 3 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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391GTPUniRule annotation2 Publications
Binding sitei143 – 1431GTPUniRule annotation2 Publications
Binding sitei187 – 1871GTPUniRule annotation2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi21 – 255GTPUniRule annotation2 Publications
Nucleotide bindingi108 – 1103GTPUniRule annotation2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Septation

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsZUniRule annotation
Gene namesi
Name:ftsZUniRule annotation
Ordered Locus Names:PA4407
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA4407.

Subcellular locationi

  • Cytoplasm UniRule annotation

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075206.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Cell division protein FtsZPRO_0000114371Add
BLAST

Proteomic databases

PaxDbiP47204.
PRIDEiP47204.

Interactioni

Subunit structurei

Homodimer. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner (By similarity). Interacts directly with several other division proteins (By similarity). Interacts with the SulA inhibitor.UniRule annotation1 Publication

Protein-protein interaction databases

IntActiP47204. 1 interaction.
STRINGi208964.PA4407.

Chemistry

BindingDBiP47204.

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni7 – 115Combined sources
Beta strandi14 – 196Combined sources
Helixi20 – 3213Combined sources
Beta strandi37 – 4610Combined sources
Helixi48 – 503Combined sources
Beta strandi56 – 605Combined sources
Helixi63 – 664Combined sources
Beta strandi67 – 693Combined sources
Helixi75 – 8410Combined sources
Helixi86 – 938Combined sources
Beta strandi97 – 1048Combined sources
Helixi109 – 12315Combined sources
Beta strandi127 – 1348Combined sources
Helixi137 – 1393Combined sources
Helixi141 – 15515Combined sources
Beta strandi159 – 1657Combined sources
Helixi166 – 1738Combined sources
Helixi174 – 1763Combined sources
Helixi179 – 20224Combined sources
Beta strandi205 – 2084Combined sources
Helixi211 – 2188Combined sources
Turni219 – 2213Combined sources
Beta strandi222 – 23312Combined sources
Helixi236 – 24510Combined sources
Helixi248 – 2503Combined sources
Helixi255 – 2573Combined sources
Beta strandi259 – 2679Combined sources
Helixi273 – 28614Combined sources
Beta strandi291 – 2999Combined sources
Beta strandi305 – 31511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OFUX-ray2.10A/B1-320[»]
2VAWX-ray2.90A1-394[»]
ProteinModelPortaliP47204.
SMRiP47204. Positions 2-316.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP47204.

Family & Domainsi

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
HOGENOMiHOG000049094.
InParanoidiP47204.
KOiK03531.
OMAiAQVIWGI.
OrthoDBiEOG6S7XZG.
PhylomeDBiP47204.

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.

P47204-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFELVDNIAQ TAVIKVIGVG GGGGNAVNHM AKNNVEGVEF ICANTDAQAL
60 70 80 90 100
KNIAARTVLQ LGPGVTKGLG AGANPEVGRQ AALEDRERIS EVLEGADMVF
110 120 130 140 150
ITTGMGGGTG TGAAPIIAEV AKEMGILTVA VVTRPFPFEG RKRMQIADEG
160 170 180 190 200
IRALAESVDS LITIPNEKLL TILGKDASLL AAFAKADDVL AGAVRGISDI
210 220 230 240 250
IKRPGMINVD FADVKTVMSE MGMAMMGTGC ASGPNRAREA TEAAIRNPLL
260 270 280 290 300
EDVNLQGARG ILVNITAGPD LSLGEYSDVG NIIEQFASEH ATVKVGTVID
310 320 330 340 350
ADMRDELHVT VVATGLGARL EKPVKVVDNT VQGSAAQAAA PAQREQQSVN
360 370 380 390
YRDLDRPTVM RNQSHGSAAT AAKLNPQDDL DYLDIPAFLR RQAD
Length:394
Mass (Da):41,218
Last modified:December 8, 2000 - v2
Checksum:i16ABF06FAB82710F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19797 Genomic DNA. Translation: AAA95993.2.
AE004091 Genomic DNA. Translation: AAG07795.1.
PIRiH83093.
RefSeqiNP_253097.1. NC_002516.2.
WP_003094113.1. NZ_ASJY01000726.1.

Genome annotation databases

EnsemblBacteriaiAAG07795; AAG07795; PA4407.
GeneIDi881296.
KEGGipae:PA4407.
PATRICi19843539. VBIPseAer58763_4616.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19797 Genomic DNA. Translation: AAA95993.2.
AE004091 Genomic DNA. Translation: AAG07795.1.
PIRiH83093.
RefSeqiNP_253097.1. NC_002516.2.
WP_003094113.1. NZ_ASJY01000726.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OFUX-ray2.10A/B1-320[»]
2VAWX-ray2.90A1-394[»]
ProteinModelPortaliP47204.
SMRiP47204. Positions 2-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP47204. 1 interaction.
STRINGi208964.PA4407.

Chemistry

BindingDBiP47204.
ChEMBLiCHEMBL1075206.

Proteomic databases

PaxDbiP47204.
PRIDEiP47204.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG07795; AAG07795; PA4407.
GeneIDi881296.
KEGGipae:PA4407.
PATRICi19843539. VBIPseAer58763_4616.

Organism-specific databases

PseudoCAPiPA4407.

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
HOGENOMiHOG000049094.
InParanoidiP47204.
KOiK03531.
OMAiAQVIWGI.
OrthoDBiEOG6S7XZG.
PhylomeDBiP47204.

Miscellaneous databases

EvolutionaryTraceiP47204.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Physical mapping of 32 genetic markers on the Pseudomonas aeruginosa PAO1 chromosome."
    Liao X., Charlebois I., Ouellet C., Morency M.J., Dewar K., Lightfoot J., Foster J., Siehnel R., Schweizer H., Lam J.S., Hancock R.E., Levesque R.C.
    Microbiology 142:79-86(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  2. "Physical Mapping of 38 loci including aimE, ampC, ampR, arcA, aroK, catR, cypH, dapB, envA, envC, ftsA, ftsZ, groEL, murE, opdE, oprD, oprF, oprH, oprI, oprK, oprP, pbpB, pbpC, pheS, phoA, phoB, phoS, ponA, pyoS1, qin, rpoB, rpoH, sodB, soxR, sucC."
    Levesque R.C., Liao X., Lightfoot J., Charlebois I., Ouellet C., Morency M., Dewar K., Siehnel R., Lam J., Hancock R.E.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 286.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  4. "Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ."
    Cordell S.C., Robinson E.J., Loewe J.
    Proc. Natl. Acad. Sci. U.S.A. 100:7889-7894(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-320 IN COMPLEX WITH SULA AND GDP.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  5. "Structural insights into the conformational variability of FtsZ."
    Oliva M.A., Trambaiolo D., Lowe J.
    J. Mol. Biol. 373:1229-1242(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH GDP.

Entry informationi

Entry nameiFTSZ_PSEAE
AccessioniPrimary (citable) accession number: P47204
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 8, 2000
Last modified: July 6, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Formation of the FtsZ ring is inhibited by SulA.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.