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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed-Annotation score: Annotation score: 3 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)DescriptionActionsGraphical viewLength
Binding sitei170GTPUniRule annotation1
Binding sitei174GTPUniRule annotation1
Binding sitei217GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi52 – 56GTPUniRule annotation5
Nucleotide bindingi139 – 141GTPUniRule 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:Ta0072
OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifieri273075 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
Proteomesi
  • UP000001024 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_00001144171 – 395Cell division protein FtsZAdd BLAST395

Proteomic databases

PRIDEiO59635.

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

STRINGi273075.Ta0072.

Structurei

3D structure databases

ProteinModelPortaliO59635.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

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

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.

O59635-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDITDLLSK VSIDDVYDEW EDQASGSLPE DAEIENVYKT LNVKIKVIGC
60 70 80 90 100
GGGGSNTVNR LYDDALKNAD LIAINTDASH LRSIKVKHKL LIGQKTTKGL
110 120 130 140 150
GTGADPKVGE EAAIEEIVAI KKIVQNTDIT FVTAGLGGGT GTGCAPVIAR
160 170 180 190 200
AAKEAGSIVI SVVTLPFESE GPLRMDNAVI GLEKLAQFSD TLVAIPNQKL
210 220 230 240 250
LSEVPNAEMK VAFAYADKVL ADTIRSIVEI ITKTGIINID YSDIKTVMQS
260 270 280 290 300
GGVALIGMGQ SKKGGDRIMT ALEEALKPRL IDVDVSTAKD CVFKIIAPPD
310 320 330 340 350
ITVSEVGKAM DEIKKKINPR SRIIWGLTID KDLDKDVKVL IFMTGVSSAY
360 370 380 390
LVKDVESARK AGEHVHRIIC GRDRHGELDQ PMIRENIFFN LIITT
Length:395
Mass (Da):42,526
Last modified:August 1, 1998 - v1
Checksum:i9211322158445E10
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti199K → R in CAC11220 (PubMed:11029001).Curated1
Sequence conflicti361 – 395AGEHV…LIITT → LASMFTGSYAAEIDTVN in CAC11220 (PubMed:11029001).CuratedAdd BLAST35

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038845 Genomic DNA. Translation: AAC24043.1.
AL445063 Genomic DNA. Translation: CAC11220.1.
PIRiT37331.
RefSeqiWP_010900500.1. NC_002578.1.

Genome annotation databases

EnsemblBacteriaiCAC11220; CAC11220; CAC11220.
GeneIDi1455732.
KEGGitac:Ta0072.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038845 Genomic DNA. Translation: AAC24043.1.
AL445063 Genomic DNA. Translation: CAC11220.1.
PIRiT37331.
RefSeqiWP_010900500.1. NC_002578.1.

3D structure databases

ProteinModelPortaliO59635.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273075.Ta0072.

Proteomic databases

PRIDEiO59635.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC11220; CAC11220; CAC11220.
GeneIDi1455732.
KEGGitac:Ta0072.

Phylogenomic databases

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

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_THEAC
AccessioniPrimary (citable) accession number: O59635
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: November 30, 2016
This is version 95 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

Complete proteome, Reference proteome

Documents

  1. 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.