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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
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

Enzyme regulationi

Calcium ions inhibit the GTPase activity and promote the polymerization of FtsZ.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei29 – 291GTP2 Publications
Binding sitei139 – 1391GTPUniRule annotation2 Publications
Binding sitei143 – 1431GTPUniRule annotation2 Publications
Binding sitei166 – 1661GTP2 Publications
Binding sitei187 – 1871GTPUniRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi21 – 255GTPUniRule annotation2 Publications
Nucleotide bindingi71 – 733GTP1 Publication
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

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-1204-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsZUniRule annotation
Gene namesi
Name:ftsZUniRule annotation
Ordered Locus Names:SAV1186
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000002481 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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi208 – 2081N → A: Lack of GTPase activity. Does not polymerize in the presence of calcium ions. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390Cell division protein FtsZPRO_0000114380Add
BLAST

Proteomic databases

PaxDbiP0A029.

2D gel databases

World-2DPAGE0002:P0A029.

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

Protein-protein interaction databases

MINTiMINT-127973.
STRINGi158878.SAV1186.

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 strandi39 – 457Combined 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 – 2449Combined sources
Helixi248 – 2569Combined sources
Beta strandi259 – 2668Combined sources
Helixi272 – 28615Combined sources
Beta strandi291 – 2988Combined sources
Helixi300 – 3023Combined sources
Beta strandi303 – 31311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VO8X-ray2.26A/B1-390[»]
3VO9X-ray2.71A/B/C/D12-316[»]
3VOAX-ray1.73A12-316[»]
3VOBX-ray2.70A12-316[»]
3VPAX-ray2.49A/B/C/D12-316[»]
3WGJX-ray2.18A/B12-316[»]
3WGKX-ray2.80A/B1-390[»]
3WGLX-ray3.07A/B1-390[»]
3WGMX-ray2.09A/B1-390[»]
3WGNX-ray2.61A/B1-390[»]
ProteinModelPortaliP0A029.
SMRiP0A029. Positions 10-315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
HOGENOMiHOG000049094.
KOiK03531.
OMAiGMAMMGI.
OrthoDBiEOG6S7XZG.
PhylomeDBiP0A029.

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.

P0A029-1 [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
BA000017 Genomic DNA. Translation: BAB57348.1.
RefSeqiWP_000888997.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB57348; BAB57348; SAV1186.
KEGGisav:SAV1186.
PATRICi19563083. VBIStaAur52173_1219.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB57348.1.
RefSeqiWP_000888997.1. NC_002758.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VO8X-ray2.26A/B1-390[»]
3VO9X-ray2.71A/B/C/D12-316[»]
3VOAX-ray1.73A12-316[»]
3VOBX-ray2.70A12-316[»]
3VPAX-ray2.49A/B/C/D12-316[»]
3WGJX-ray2.18A/B12-316[»]
3WGKX-ray2.80A/B1-390[»]
3WGLX-ray3.07A/B1-390[»]
3WGMX-ray2.09A/B1-390[»]
3WGNX-ray2.61A/B1-390[»]
ProteinModelPortaliP0A029.
SMRiP0A029. Positions 10-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-127973.
STRINGi158878.SAV1186.

2D gel databases

World-2DPAGE0002:P0A029.

Proteomic databases

PaxDbiP0A029.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB57348; BAB57348; SAV1186.
KEGGisav:SAV1186.
PATRICi19563083. VBIStaAur52173_1219.

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
HOGENOMiHOG000049094.
KOiK03531.
OMAiGMAMMGI.
OrthoDBiEOG6S7XZG.
PhylomeDBiP0A029.

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-1204-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: Mu50 / ATCC 700699.
  2. "Structural reorganization of the bacterial cell-division protein FtsZ from Staphylococcus aureus."
    Matsui T., Yamane J., Mogi N., Yamaguchi H., Takemoto H., Yao M., Tanaka I.
    Acta Crystallogr. D 68:1175-1188(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 12-316 OF APOPROTEIN AND IN COMPLEXES WITH GDP AND INHIBITOR, ENZYME REGULATION, MUTAGENESIS OF ASN-208.
    Strain: Mu50 / ATCC 700699.
  3. "Structural change in FtsZ induced by intermolecular interactions between bound GTP and the T7 loop."
    Matsui T., Han X., Yu J., Yao M., Tanaka I.
    J. Biol. Chem. 289:3501-3509(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF WILD-TYPE AND OF MUTANTS IN COMPLEXES WITH GTP AND GDP.
    Strain: Mu50 / ATCC 700699.

Entry informationi

Entry nameiFTSZ_STAAM
AccessioniPrimary (citable) accession number: P0A029
Secondary accession number(s): P45498
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: July 6, 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

3D-structure, Complete 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.