Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Nostoc sp. (strain PCC 7120 / UTEX 2576)
Status
Reviewed-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 sitei191 – 1911GTPUniRule annotation
Binding sitei195 – 1951GTPUniRule annotation
Binding sitei239 – 2391GTPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi73 – 775GTPUniRule annotation
Nucleotide bindingi160 – 1623GTPUniRule 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:alr3858
OrganismiNostoc sp. (strain PCC 7120 / UTEX 2576)
Taxonomic identifieri103690 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
Proteomesi
  • UP000002483 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 – 428428Cell division protein FtsZPRO_0000114337Add
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

STRINGi103690.alr3858.

Structurei

3D structure databases

ProteinModelPortaliP45482.
SMRiP45482. Positions 64-367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
HOGENOMiHOG000049094.
KOiK03531.
OMAiIWGTSVD.
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.

P45482-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLDNNQELT YRNSQSLGQP GFSLAVNSSN PFNHSGLNFG QNNDSKKISV
60 70 80 90 100
ENNRIGEIVP GRVANIKVIG VGGGGGNAVN RMIESDVSGV EFWSINTDAQ
110 120 130 140 150
ALTLAGAPSR LQIGQKLTRG LGAGGNPAIG QKAAEESRDE IATALEGADL
160 170 180 190 200
VFITAGMGGG TGTGAAPIVA EVAKEMGALT VGVVTRPFVF EGRRRTSQAE
210 220 230 240 250
QGIEGLKSRV DTLIIIPNNK LLEVIPEQTP VQEAFRYADD VLRQGVQGIS
260 270 280 290 300
DIITIPGLVN VDFADVRAVM ADAGSALMGI GVSSGKSRAR EAAIAAISSP
310 320 330 340 350
LLECSIEGAR GVVFNITGGS DLTLHEVNAA AETIYEVVDP NANIIFGAVI
360 370 380 390 400
DDRLQGEVRI TVIATGFTGE IQAAPQQNAA NARVVSAPPK RTPTQTPLTN
410 420
SPAPTPEPKE KSGLDIPDFL QRRRPPKN
Length:428
Mass (Da):44,730
Last modified:January 23, 2002 - v2
Checksum:i853642CA7ACB53D3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti386 – 3861S → A (PubMed:8525061).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z31371 Genomic DNA. Translation: CAA83241.1.
BA000019 Genomic DNA. Translation: BAB75557.1.
U14408 Genomic DNA. Translation: AAA85526.1.
PIRiAC2288.
JC4289.
RefSeqiWP_010997999.1. NC_003272.1.

Genome annotation databases

EnsemblBacteriaiBAB75557; BAB75557; BAB75557.
KEGGiana:alr3858.
PATRICi22778202. VBINosSp37423_4555.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z31371 Genomic DNA. Translation: CAA83241.1.
BA000019 Genomic DNA. Translation: BAB75557.1.
U14408 Genomic DNA. Translation: AAA85526.1.
PIRiAC2288.
JC4289.
RefSeqiWP_010997999.1. NC_003272.1.

3D structure databases

ProteinModelPortaliP45482.
SMRiP45482. Positions 64-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi103690.alr3858.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB75557; BAB75557; BAB75557.
KEGGiana:alr3858.
PATRICi22778202. VBINosSp37423_4555.

Phylogenomic databases

eggNOGiENOG4105CDK. Bacteria.
COG0206. LUCA.
HOGENOMiHOG000049094.
KOiK03531.
OMAiIWGTSVD.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of genes encoding the cell division protein FtsZ and a glutathione synthetase homologue in the cyanobacterium Anabaena sp. PCC 7120."
    Zhang C.C., Huguenin S., Friry A.
    Res. Microbiol. 146:445-455(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7120 / UTEX 2576.
  3. "Cloning and sequence of ftsZ and flanking regions from the cyanobacterium Anabaena PCC 7120."
    Doherty H.M., Adams D.G.
    Gene 163:93-96(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-428.

Entry informationi

Entry nameiFTSZ_NOSS1
AccessioniPrimary (citable) accession number: P45482
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2002
Last modified: July 6, 2016
This is version 108 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

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.