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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 4 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)DescriptionActionsGraphical viewLength
Binding sitei139GTPUniRule annotation2 Publications1
Binding sitei143GTPUniRule annotation2 Publications1
Binding sitei187GTPUniRule annotation2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi21 – 25GTPUniRule annotation2 Publications5
Nucleotide bindingi108 – 110GTPUniRule annotation2 Publications3

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 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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 databases

ChEMBLiCHEMBL1075206.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001143711 – 394Cell division protein FtsZAdd BLAST394

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 interactor.
STRINGi208964.PA4407.

Chemistry databases

BindingDBiP47204.

Structurei

Secondary structure

1394
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni7 – 11Combined sources5
Beta strandi14 – 19Combined sources6
Helixi20 – 32Combined sources13
Beta strandi37 – 46Combined sources10
Helixi48 – 50Combined sources3
Beta strandi56 – 60Combined sources5
Helixi63 – 66Combined sources4
Beta strandi67 – 69Combined sources3
Helixi75 – 84Combined sources10
Helixi86 – 93Combined sources8
Beta strandi97 – 104Combined sources8
Helixi109 – 123Combined sources15
Beta strandi127 – 134Combined sources8
Helixi137 – 139Combined sources3
Helixi141 – 155Combined sources15
Beta strandi159 – 165Combined sources7
Helixi166 – 173Combined sources8
Helixi174 – 176Combined sources3
Helixi179 – 202Combined sources24
Beta strandi205 – 208Combined sources4
Helixi211 – 218Combined sources8
Turni219 – 221Combined sources3
Beta strandi222 – 233Combined sources12
Helixi236 – 245Combined sources10
Helixi248 – 250Combined sources3
Helixi255 – 257Combined sources3
Beta strandi259 – 267Combined sources9
Helixi273 – 286Combined sources14
Beta strandi291 – 299Combined sources9
Beta strandi305 – 315Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OFUX-ray2.10A/B1-320[»]
2VAWX-ray2.90A1-394[»]
ProteinModelPortaliP47204.
SMRiP47204.
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.
PhylomeDBiP47204.

Family and domain databases

CDDicd02201. FtsZ_type1. 1 hit.
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.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OFUX-ray2.10A/B1-320[»]
2VAWX-ray2.90A1-394[»]
ProteinModelPortaliP47204.
SMRiP47204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP47204. 1 interactor.
STRINGi208964.PA4407.

Chemistry databases

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.
PhylomeDBiP47204.

Miscellaneous databases

EvolutionaryTraceiP47204.

Family and domain databases

CDDicd02201. FtsZ_type1. 1 hit.
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_PSEAE
AccessioniPrimary (citable) accession number: P47204
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 8, 2000
Last modified: November 30, 2016
This is version 117 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.