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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Staphylococcus aureus (strain N315)
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 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

Enzyme and pathway databases

BioCyciSAUR158879:GJCB-1089-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsZUniRule annotation
Gene namesi
Name:ftsZUniRule annotation
Ordered Locus Names:SA1029
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000751 Componenti: Chromosome

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390Cell division protein FtsZPRO_0000114381Add
BLAST

2D gel databases

SWISS-2DPAGEP99108.

Interactioni

Subunit structurei

Homodimer. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner. Interacts directly with several other division proteins.UniRule annotation

Chemistry

BindingDBiP99108.

Structurei

3D structure databases

ProteinModelPortaliP99108.
SMRiP99108. Positions 10-315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000049094.
OMAiGMAMMGI.
OrthoDBiEOG6S7XZG.

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.

P99108-1 [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
BA000018 Genomic DNA. Translation: BAB42281.1.
RefSeqiWP_000888997.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB42281; BAB42281; BAB42281.
PATRICi19574276. VBIStaAur116463_1107.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB42281.1.
RefSeqiWP_000888997.1. NC_002745.2.

3D structure databases

ProteinModelPortaliP99108.
SMRiP99108. Positions 10-315.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP99108.

2D gel databases

SWISS-2DPAGEP99108.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB42281; BAB42281; BAB42281.
PATRICi19574276. VBIStaAur116463_1107.

Phylogenomic databases

HOGENOMiHOG000049094.
OMAiGMAMMGI.
OrthoDBiEOG6S7XZG.

Enzyme and pathway databases

BioCyciSAUR158879:GJCB-1089-MONOMER.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: N315.
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: N315.
  3. "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
    Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
    Submitted (OCT-2007) to UniProtKB
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: N315.

Entry informationi

Entry nameiFTSZ_STAAN
AccessioniPrimary (citable) accession number: P99108
Secondary accession number(s): P45498
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: March 16, 2016
This is version 80 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

Complete proteome

Documents

  1. 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.