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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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 sitei155 – 1551GTPUniRule annotation
Binding sitei158 – 1581GTPUniRule annotation
Binding sitei201 – 2011GTPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi37 – 415GTPUniRule annotation
Nucleotide bindingi124 – 1263GTPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, SeptationUniRule annotation

Keywords - Ligandi

GTP-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciMVAN406327:GI04-821-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsZUniRule annotation
Gene namesi
Name:ftsZUniRule annotation
Ordered Locus Names:Mevan_0809Imported
OrganismiMethanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)Imported
Taxonomic identifieri406327 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
Proteomesi
  • UP000001107 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

CytoplasmUniRule annotation

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

STRINGi406327.Mevan_0809.

Structurei

3D structure databases

ProteinModelPortaliA6UQE3.
SMRiA6UQE3. Positions 27-346.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 219191TubulinInterPro annotationAdd
BLAST
Domaini221 – 341121Tubulin_CInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG02201. Archaea.
COG0206. LUCA.
HOGENOMiHOG000049094.
KOiK03531.
OMAiIMNQGGV.

Family and domain databases

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.

A6UQE3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLVKEALAK NNDEMYNTQM AKDDFGNAKI LVVGCGGAGN NTIHRLTEIG
60 70 80 90 100
IEGAETIAIN TDKQHLENIS ADKKILIGST LTRGLGAGGY PEIGKKSAEL
110 120 130 140 150
AKNVLEDVIK SADLVFVSAG MGGGTGTGSA PVVAEIAKEN SAVVIGVVTY
160 170 180 190 200
PFKIERARLK KADEGLKRLT ESCDTVIVID NNRLVDFVPN LPMNEAFRIA
210 220 230 240 250
DEIIAQAVKG ITETISLKSL INIDYADVKA VMTNGGVAMI GVGEVDFDSK
260 270 280 290 300
GDRVDKVVKD TLQCPLLDID YKGATGALIH ITGGPDLTLG EANRIGEGIT
310 320 330 340 350
NSMDANANVI WGARLDPEME GAIRVMAIIT GVKSPNIIGG GKSPQKIIPK
360
SANRTKGSLG IDYIV
Length:365
Mass (Da):38,486
Last modified:August 21, 2007 - v1
Checksum:iD2CF25CA4DCB4438
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000742 Genomic DNA. Translation: ABR54715.1.
RefSeqiWP_011972617.1. NC_009634.1.

Genome annotation databases

EnsemblBacteriaiABR54715; ABR54715; Mevan_0809.
GeneIDi5324574.
KEGGimvn:Mevan_0809.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000742 Genomic DNA. Translation: ABR54715.1.
RefSeqiWP_011972617.1. NC_009634.1.

3D structure databases

ProteinModelPortaliA6UQE3.
SMRiA6UQE3. Positions 27-346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi406327.Mevan_0809.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABR54715; ABR54715; Mevan_0809.
GeneIDi5324574.
KEGGimvn:Mevan_0809.

Phylogenomic databases

eggNOGiarCOG02201. Archaea.
COG0206. LUCA.
HOGENOMiHOG000049094.
KOiK03531.
OMAiIMNQGGV.

Enzyme and pathway databases

BioCyciMVAN406327:GI04-821-MONOMER.

Family and domain databases

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 nameiA6UQE3_METVS
AccessioniPrimary (citable) accession number: A6UQE3
Entry historyi
Integrated into UniProtKB/TrEMBL: August 21, 2007
Last sequence update: August 21, 2007
Last modified: September 7, 2016
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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.