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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)DescriptionActionsGraphical viewLength
Binding sitei149GTPUniRule annotation1
Binding sitei153GTPUniRule annotation1
Binding sitei197GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi31 – 35GTPUniRule annotation5
Nucleotide bindingi118 – 120GTPUniRule annotation3

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001143911 – 351Cell division protein FtsZAdd BLAST351

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 interactor.
MINTiMINT-8382767.
STRINGi243274.TM0836.

Structurei

Secondary structure

1351
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi24 – 29Combined sources6
Helixi30 – 43Combined sources14
Beta strandi48 – 55Combined sources8
Helixi57 – 61Combined sources5
Beta strandi66 – 70Combined sources5
Turni73 – 78Combined sources6
Helixi85 – 94Combined sources10
Helixi96 – 102Combined sources7
Turni103 – 105Combined sources3
Beta strandi107 – 114Combined sources8
Helixi119 – 133Combined sources15
Beta strandi137 – 144Combined sources8
Helixi147 – 149Combined sources3
Helixi151 – 166Combined sources16
Beta strandi169 – 175Combined sources7
Helixi176 – 180Combined sources5
Helixi189 – 212Combined sources24
Helixi219 – 228Combined sources10
Beta strandi232 – 243Combined sources12
Helixi246 – 255Combined sources10
Helixi264 – 266Combined sources3
Beta strandi268 – 276Combined sources9
Helixi282 – 293Combined sources12
Beta strandi300 – 308Combined sources9
Beta strandi316 – 324Combined sources9
Helixi330 – 333Combined sources4
Helixi341 – 344Combined sources4
Helixi348 – 350Combined sources3

3D structure databases

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

Family and domain databases

CDDicd02201. FtsZ_type1. 1 hit.
Gene3Di3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
HAMAPiMF_00909. FtsZ. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti102V → A in AAC24604 (PubMed:9605973).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W5FX-ray2.00A/B1-351[»]
4A2AX-ray1.80C/D336-351[»]
ProteinModelPortaliO08398.
SMRiO08398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO08398. 1 interactor.
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.

Miscellaneous databases

EvolutionaryTraceiO08398.

Family and domain databases

CDDicd02201. FtsZ_type1. 1 hit.
Gene3Di3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
HAMAPiMF_00909. FtsZ. 1 hit.
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...

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: November 30, 2016
This is version 130 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.