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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Aquifex aeolicus (strain VF5)
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 sitei135 – 1351GTPUniRule annotation1 Publication
Binding sitei139 – 1391GTPUniRule annotation
Binding sitei183 – 1831GTPUniRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 215GTPUniRule annotation1 Publication
Nucleotide bindingi104 – 1063GTPUniRule annotation1 Publication

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

BioCyciAAEO224324:GJBH-389-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsZUniRule annotation
Gene namesi
Name:ftsZUniRule annotation
Ordered Locus Names:aq_525
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 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 – 367367Cell division protein FtsZPRO_0000114338Add
BLAST

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

STRINGi224324.aq_525.

Chemistry

BindingDBiO66809.

Structurei

Secondary structure

1
367
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 156Combined sources
Helixi16 – 2813Combined sources
Beta strandi35 – 428Combined sources
Helixi43 – 475Combined sources
Beta strandi52 – 565Combined sources
Helixi59 – 624Combined sources
Helixi71 – 8010Combined sources
Helixi82 – 898Combined sources
Beta strandi93 – 1008Combined sources
Helixi105 – 11915Combined sources
Beta strandi123 – 1308Combined sources
Helixi133 – 1353Combined sources
Helixi137 – 15216Combined sources
Beta strandi155 – 1617Combined sources
Helixi162 – 1676Combined sources
Helixi175 – 19824Combined sources
Helixi207 – 2148Combined sources
Beta strandi218 – 22912Combined sources
Helixi232 – 24211Combined sources
Beta strandi244 – 2496Combined sources
Helixi251 – 2533Combined sources
Beta strandi255 – 2639Combined sources
Helixi271 – 28212Combined sources
Beta strandi288 – 2958Combined sources
Beta strandi301 – 31010Combined sources
Beta strandi317 – 3193Combined sources
Beta strandi322 – 3243Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R6RX-ray1.7011-331[»]
2R75X-ray1.4011-331[»]
ProteinModelPortaliO66809.
SMRiO66809. Positions 20-330.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO66809.

Family & Domainsi

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
HOGENOMiHOG000049094.
InParanoidiO66809.
KOiK03531.
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.

O66809-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEFVNPCKI KVIGVGGGGS NAVNRMYEDG IEGVELYAIN TDVQHLSTLK
60 70 80 90 100
VPNKIQIGEK VTRGLGAGAK PEVGEEAALE DIDKIKEILR DTDMVFISAG
110 120 130 140 150
LGGGTGTGAA PVIAKTAKEM GILTVAVATL PFRFEGPRKM EKALKGLEKL
160 170 180 190 200
KESSDAYIVI HNDKIKELSN RTLTIKDAFK EVDSVLSKAV RGITSIVVTP
210 220 230 240 250
AVINVDFADV RTTLEEGGLS IIGMGEGRGD EKADIAVEKA VTSPLLEGNT
260 270 280 290 300
IEGARRLLVT IWTSEDIPYD IVDEVMERIH SKVHPEAEII FGAVLEPQEQ
310 320 330 340 350
DFIRVAIVAT DFPEEKFQVG EKEVKFKVIK KEEKEEPKEE PKPLSDTTYL
360
EEEEIPAVIR RKNKRLL
Length:367
Mass (Da):40,161
Last modified:August 1, 1998 - v1
Checksum:i0DEC8A6A865348A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06771.1.
PIRiE70347.
RefSeqiNP_213369.1. NC_000918.1.
WP_010880307.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC06771; AAC06771; aq_525.
GeneIDi1193227.
KEGGiaae:aq_525.
PATRICi20958592. VBIAquAeo85532_0431.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06771.1.
PIRiE70347.
RefSeqiNP_213369.1. NC_000918.1.
WP_010880307.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R6RX-ray1.7011-331[»]
2R75X-ray1.4011-331[»]
ProteinModelPortaliO66809.
SMRiO66809. Positions 20-330.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_525.

Chemistry

BindingDBiO66809.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC06771; AAC06771; aq_525.
GeneIDi1193227.
KEGGiaae:aq_525.
PATRICi20958592. VBIAquAeo85532_0431.

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
HOGENOMiHOG000049094.
InParanoidiO66809.
KOiK03531.
OMAiGMAMMGI.
OrthoDBiEOG6S7XZG.

Enzyme and pathway databases

BioCyciAAEO224324:GJBH-389-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO66809.

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: VF5.
  2. "Structural insights into the conformational variability of FtsZ."
    Oliva M.A., Trambaiolo D., Lowe J.
    J. Mol. Biol. 373:1229-1242(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-331 IN COMPLEX WITH GDP.
  3. "Probing FtsZ and tubulin with C8-substituted GTP analogs reveals differences in their nucleotide binding sites."
    Lappchen T., Pinas V.A., Hartog A.F., Koomen G.J., Schaffner-Barbero C., Andreu J.M., Trambaiolo D., Lowe J., Juhem A., Popov A.V., den Blaauwen T.
    Chem. Biol. 15:189-199(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-331.

Entry informationi

Entry nameiFTSZ_AQUAE
AccessioniPrimary (citable) accession number: O66809
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: January 20, 2016
This is version 112 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, 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.