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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391GTPUniRule annotation
Binding sitei143 – 1431GTPUniRule annotation
Binding sitei187 – 1871GTPUniRule annotation

Regions

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

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi371 – 3711D → A: Does not affect interaction with FtsA and FtsZ. 1 Publication
Mutagenesisi372 – 3721D → A: Does not affect interaction with FtsA and FtsZ. 1 Publication
Mutagenesisi373 – 3731I → P: Does not affect interaction with FtsA and FtsZ. 1 Publication
Mutagenesisi374 – 3741P → A: Does not affect interaction with FtsA and FtsZ. 1 Publication
Mutagenesisi375 – 3751S → A: Does not affect interaction with FtsA and FtsZ. 1 Publication
Mutagenesisi376 – 3761F → A: No interaction with FtsA, but does not affect interaction with FtsZ. 1 Publication
Mutagenesisi377 – 3771I → A: Does not affect interaction with FtsA and FtsZ. 1 Publication
Mutagenesisi378 – 3781R → A: Does not affect interaction with FtsA and FtsZ. 1 Publication
Mutagenesisi379 – 3791N → A: Does not affect interaction with FtsA and FtsZ. 1 Publication
Mutagenesisi380 – 3801R → A: Does not affect interaction with FtsA and FtsZ. 1 Publication

Chemistry

ChEMBLiCHEMBL5096.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390Cell division protein FtsZPRO_0000114385Add
BLAST

Proteomic databases

PRIDEiP0A031.

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

BindingDBiP0A031.

Structurei

Secondary structure

1
390
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 196Combined sources
Helixi20 – 3314Combined sources
Beta strandi37 – 459Combined sources
Helixi47 – 515Combined sources
Beta strandi56 – 605Combined sources
Helixi63 – 664Combined sources
Helixi75 – 8410Combined sources
Helixi86 – 938Combined sources
Beta strandi97 – 1048Combined sources
Helixi109 – 12315Combined sources
Beta strandi127 – 1348Combined sources
Helixi137 – 1393Combined sources
Helixi141 – 15717Combined sources
Beta strandi158 – 1658Combined sources
Helixi166 – 1716Combined sources
Helixi179 – 20224Combined sources
Helixi211 – 2188Combined sources
Beta strandi225 – 2339Combined sources
Helixi236 – 24510Combined sources
Beta strandi259 – 2668Combined sources
Helixi272 – 28615Combined sources
Beta strandi291 – 2988Combined sources
Beta strandi305 – 3139Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DXDX-ray2.01A2-390[»]
ProteinModelPortaliP0A031.
SMRiP0A031. Positions 10-315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni371 – 38010Interaction with FtsA

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.

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.

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_LSMV01000004.1.

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_LSMV01000004.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DXDX-ray2.01A2-390[»]
ProteinModelPortaliP0A031.
SMRiP0A031. Positions 10-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL1199.

Chemistry

BindingDBiP0A031.
ChEMBLiCHEMBL5096.

Proteomic databases

PRIDEiP0A031.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.

Miscellaneous databases

PROiP0A031.

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

  1. "Cloning and sequencing of an ftsZ homologue from Staphylococcus aureus."
    Alessi D.M., Olson E.R.
    Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: SA4.
  2. "A conserved residue at the extreme C-terminus of FtsZ is critical for the FtsA-FtsZ interaction in Staphylococcus aureus."
    Yan K., Pearce K.H., Payne D.J.
    Biochem. Biophys. Res. Commun. 270:387-392(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FTSA, SELF-INTERACTION, MUTAGENESIS OF ASP-371; ASP-372; ILE-373; PRO-374; SER-375; PHE-376; ILE-377; ARG-378; ASN-379 AND ARG-380.
    Strain: WCUH29 / NCIMB 40771.

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: June 8, 2016
This is version 62 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.