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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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 annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei149 – 1491GTPUniRule annotation
Binding sitei153 – 1531GTPUniRule annotation
Binding sitei197 – 1971GTPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 355GTPUniRule annotation
Nucleotide bindingi118 – 1203GTPUniRule 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
Ordered Locus Names:TM_0836
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 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 – 351351Cell division protein FtsZPRO_0000114391Add
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 (By similarity). Interacts with FtsA (PubMed:22473211).UniRule annotation1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ftsAQ9WZU04EBI-7808310,EBI-7808292

Protein-protein interaction databases

IntActiO08398. 1 interaction.
MINTiMINT-8382767.
STRINGi243274.TM0836.

Structurei

Secondary structure

1
351
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 296Combined sources
Helixi30 – 4314Combined sources
Beta strandi48 – 558Combined sources
Helixi57 – 615Combined sources
Beta strandi66 – 705Combined sources
Turni73 – 786Combined sources
Helixi85 – 9410Combined sources
Helixi96 – 1027Combined sources
Turni103 – 1053Combined sources
Beta strandi107 – 1148Combined sources
Helixi119 – 13315Combined sources
Beta strandi137 – 1448Combined sources
Helixi147 – 1493Combined sources
Helixi151 – 16616Combined sources
Beta strandi169 – 1757Combined sources
Helixi176 – 1805Combined sources
Helixi189 – 21224Combined sources
Helixi219 – 22810Combined sources
Beta strandi232 – 24312Combined sources
Helixi246 – 25510Combined sources
Helixi264 – 2663Combined sources
Beta strandi268 – 2769Combined sources
Helixi282 – 29312Combined sources
Beta strandi300 – 3089Combined sources
Beta strandi316 – 3249Combined sources
Helixi330 – 3334Combined sources
Helixi341 – 3444Combined sources
Helixi348 – 3503Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W5FX-ray2.00A/B1-351[»]
4A2AX-ray1.80C/D336-351[»]
ProteinModelPortaliO08398.
SMRiO08398. Positions 22-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO08398.

Family & Domainsi

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
InParanoidiO08398.
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.

O08398-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFDLDVEKK KENRNIPQAN NLKIKVIGVG GAGNNAINRM IEIGIHGVEF
60 70 80 90 100
VAVNTDLQVL EASNADVKIQ IGENITRGLG AGGRPEIGEQ AALESEEKIR
110 120 130 140 150
EVLQDTHMVF ITAGFGGGTG TGASPVIAKI AKEMGILTVA IVTTPFYFEG
160 170 180 190 200
PERLKKAIEG LKKLRKHVDT LIKISNNKLM EELPRDVKIK DAFLKADETL
210 220 230 240 250
HQGVKGISEL ITKRGYINLD FADIESVMKD AGAAILGIGV GKGEHRAREA
260 270 280 290 300
AKKAMESKLI EHPVENASSI VFNITAPSNI RMEEVHEAAM IIRQNSSEDA
310 320 330 340 350
DVKFGLIFDD EVPDDEIRVI FIATRFPDED KILFPEGDIP AIYRYGLEGL

L
Length:351
Mass (Da):38,307
Last modified:May 30, 2000 - v2
Checksum:i5F2E11FDAA92AFE7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021V → A in AAC24604 (PubMed:9605973).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65944 Genomic DNA. Translation: AAC24604.1.
AE000512 Genomic DNA. Translation: AAD35918.1.
PIRiH72328.
RefSeqiNP_228645.1. NC_000853.1.
WP_004080800.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD35918; AAD35918; TM_0836.
GeneIDi898507.
KEGGitma:TM0836.
PATRICi23936598. VBITheMar51294_0849.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65944 Genomic DNA. Translation: AAC24604.1.
AE000512 Genomic DNA. Translation: AAD35918.1.
PIRiH72328.
RefSeqiNP_228645.1. NC_000853.1.
WP_004080800.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W5FX-ray2.00A/B1-351[»]
4A2AX-ray1.80C/D336-351[»]
ProteinModelPortaliO08398.
SMRiO08398. Positions 22-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO08398. 1 interaction.
MINTiMINT-8382767.
STRINGi243274.TM0836.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35918; AAD35918; TM_0836.
GeneIDi898507.
KEGGitma:TM0836.
PATRICi23936598. VBITheMar51294_0849.

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
InParanoidiO08398.
KOiK03531.
OMAiGMAMMGI.
OrthoDBiEOG6S7XZG.

Miscellaneous databases

EvolutionaryTraceiO08398.

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. "FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima -- quantitation, GTP hydrolysis, and assembly."
    Lu C., Stricker J., Erickson H.P.
    Cell Motil. Cytoskeleton 40:71-86(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CHARACTERIZATION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  3. "Structural insights into FtsZ protofilament formation."
    Oliva M.A., Cordell S.C., Lowe J.
    Nat. Struct. Mol. Biol. 11:1243-1250(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  4. Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 336-351 IN COMPLEX WITH FTSA.

Entry informationi

Entry nameiFTSZ_THEMA
AccessioniPrimary (citable) accession number: O08398
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 30, 2000
Last modified: May 11, 2016
This is version 125 of the entry and version 2 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.