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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Staphylococcus aureus
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.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei139GTPUniRule annotation1
Binding sitei143GTPUniRule annotation1
Binding sitei187GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi21 – 25GTPUniRule annotation5
Nucleotide bindingi108 – 110GTPUniRule annotation3

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
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi371D → A: Does not affect interaction with FtsA and FtsZ. 1 Publication1
Mutagenesisi372D → A: Does not affect interaction with FtsA and FtsZ. 1 Publication1
Mutagenesisi373I → P: Does not affect interaction with FtsA and FtsZ. 1 Publication1
Mutagenesisi374P → A: Does not affect interaction with FtsA and FtsZ. 1 Publication1
Mutagenesisi375S → A: Does not affect interaction with FtsA and FtsZ. 1 Publication1
Mutagenesisi376F → A: No interaction with FtsA, but does not affect interaction with FtsZ. 1 Publication1
Mutagenesisi377I → A: Does not affect interaction with FtsA and FtsZ. 1 Publication1
Mutagenesisi378R → A: Does not affect interaction with FtsA and FtsZ. 1 Publication1
Mutagenesisi379N → A: Does not affect interaction with FtsA and FtsZ. 1 Publication1
Mutagenesisi380R → A: Does not affect interaction with FtsA and FtsZ. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5096.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001143851 – 390Cell division protein FtsZAdd BLAST390

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi93062.SACOL1199.

Chemistry databases

BindingDBiP0A031.

Structurei

Secondary structure

1390
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 19Combined sources6
Helixi20 – 33Combined sources14
Beta strandi37 – 45Combined sources9
Helixi47 – 51Combined sources5
Beta strandi56 – 60Combined sources5
Helixi63 – 66Combined sources4
Helixi75 – 84Combined sources10
Helixi86 – 93Combined sources8
Beta strandi97 – 104Combined sources8
Helixi109 – 123Combined sources15
Beta strandi127 – 134Combined sources8
Helixi137 – 139Combined sources3
Helixi141 – 157Combined sources17
Beta strandi158 – 165Combined sources8
Helixi166 – 171Combined sources6
Helixi179 – 202Combined sources24
Helixi211 – 218Combined sources8
Beta strandi225 – 233Combined sources9
Helixi236 – 245Combined sources10
Beta strandi259 – 266Combined sources8
Helixi272 – 286Combined sources15
Beta strandi291 – 298Combined sources8
Beta strandi305 – 313Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DXDX-ray2.01A2-390[»]
ProteinModelPortaliP0A031.
SMRiP0A031.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni371 – 380Interaction with FtsA10

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.

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.

P0A031-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEFEQGFNH LATLKVIGVG GGGNNAVNRM IDHGMNNVEF IAINTDGQAL
60 70 80 90 100
NLSKAESKIQ IGEKLTRGLG AGANPEIGKK AAEESREQIE DAIQGADMVF
110 120 130 140 150
VTSGMGGGTG TGAAPVVAKI AKEMGALTVG VVTRPFSFEG RKRQTQAAAG
160 170 180 190 200
VEAMKAAVDT LIVIPNDRLL DIVDKSTPMM EAFKEADNVL RQGVQGISDL
210 220 230 240 250
IAVSGEVNLD FADVKTIMSN QGSALMGIGV SSGENRAVEA AKKAISSPLL
260 270 280 290 300
ETSIVGAQGV LMNITGGESL SLFEAQEAAD IVQDAADEDV NMIFGTVINP
310 320 330 340 350
ELQDEIVVTV IATGFDDKPT SHGRKSGSTG FGTSVNTSSN ATSKDESFTS
360 370 380 390
NSSNAQATDS VSERTHTTKE DDIPSFIRNR EERRSRRTRR
Length:390
Mass (Da):41,037
Last modified:March 1, 2005 - v1
Checksum:iA1E97FCC5C232440
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06462 Unassigned DNA. Translation: AAA16512.1.
PIRiS58814.
RefSeqiWP_000888997.1. NZ_MCFM01000018.1.

Genome annotation databases

GeneIDi28381257.

Cross-referencesi

Web resourcesi

Protein Spotlight

Becoming two - Issue 171 of July 2015

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06462 Unassigned DNA. Translation: AAA16512.1.
PIRiS58814.
RefSeqiWP_000888997.1. NZ_MCFM01000018.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DXDX-ray2.01A2-390[»]
ProteinModelPortaliP0A031.
SMRiP0A031.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL1199.

Chemistry databases

BindingDBiP0A031.
ChEMBLiCHEMBL5096.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi28381257.

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.

Miscellaneous databases

PROiP0A031.

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_STAAU
AccessioniPrimary (citable) accession number: P0A031
Secondary accession number(s): P45498
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: November 30, 2016
This is version 66 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. 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.