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Protein

Cell division protein FtsZ homolog 2-1, chloroplastic

Gene

FTSZ2-1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits GTPase activity. Component of the plastid division machinery that forms a contractile ring at the division site. Required for plastid division in a dose-dependent manner.7 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei248 – 2481GTPBy similarity
Binding sitei252 – 2521GTPBy similarity
Binding sitei296 – 2961GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi128 – 1325GTPBy similarity
Nucleotide bindingi217 – 2193GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB
  • protein self-association Source: UniProtKB

GO - Biological processi

  • chloroplast fission Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsZ homolog 2-1, chloroplastic
Short name:
AtFtsZ2-1
Alternative name(s):
Plastid division protein FTSZ2-1
Gene namesi
Name:FTSZ2-1
Ordered Locus Names:At2g36250
ORF Names:F2H17.14
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G36250.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • chloroplast thylakoid Source: TAIR
  • chloroplast thylakoid membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Thylakoid

Pathology & Biotechi

Disruption phenotypei

Reduced number of heterogeneous large chloroplast population (small and large plastids) due to impaired plastid division.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi322 – 3221D → A: Impaired GTPase activity. 1 Publication
Mutagenesisi466 – 4661F → A: Impaired ARC6 binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 478Cell division protein FtsZ homolog 2-1, chloroplasticPRO_0000406890
Transit peptidei1 – ?ChloroplastSequence analysis

Proteomic databases

PaxDbiO82533.
PRIDEiO82533.

Expressioni

Gene expression databases

GenevisibleiO82533. AT.

Interactioni

Subunit structurei

Aggregates to form a contractile ring-like structure. Self-interacts and binds to FTSZ1 in heteropolymers to form two morphologically distinct types of filaments, termed type-I (smooth filaments) and -II (rough filaments), in a GTP-dependent manner. Interacts (via C-terminus) with ARC6. Part of a complex made of ARC3, ARC6, FTSZ1 and FTSZ2.5 Publications

GO - Molecular functioni

  • protein self-association Source: UniProtKB

Protein-protein interaction databases

BioGridi3541. 7 interactions.
IntActiO82533. 1 interaction.
STRINGi3702.AT2G36250.1.

Structurei

3D structure databases

ProteinModelPortaliO82533.
SMRiO82533. Positions 119-424.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FtsZ family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IEJ4. Eukaryota.
COG0206. LUCA.
HOGENOMiHOG000049094.
InParanoidiO82533.
KOiK03531.
OMAiAQVIWGI.
PhylomeDBiO82533.

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.
PROSITEiPS01135. FTSZ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O82533-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATYVSPCFT PSDSRLLTVL RKNVLPENHL GRLNSIRTID SKKNRVVVAA
60 70 80 90 100
QKSESSPIRN SPRHYQSQAQ DPFLNLHPEI SMLRGEGTST IVNPRKETSS
110 120 130 140 150
GPVVEDFEEP SAPSNYNEAR IKVIGVGGGG SNAVNRMIES EMSGVEFWIV
160 170 180 190 200
NTDIQAMRMS PVLPDNRLQI GKELTRGLGA GGNPEIGMNA ARESKEVIEE
210 220 230 240 250
ALYGSDMVFV TAGMGGGTGT GAAPVIAGIA KAMGILTVGI ATTPFSFEGR
260 270 280 290 300
RRTVQAQEGL ASLRDNVDTL IVIPNDKLLT AVSQSTPVTE AFNLADDILR
310 320 330 340 350
QGVRGISDII TIPGLVNVDF ADVRAIMANA GSSLMGIGTA TGKSRARDAA
360 370 380 390 400
LNAIQSPLLD IGIERATGIV WNITGGSDLT LFEVNAAAEV IYDLVDPTAN
410 420 430 440 450
LIFGAVVDPA LSGQVSITLI ATGFKRQEEG EGRTVQMVQA DAASVGATRR
460 470
PSSSFRESGS VEIPEFLKKK GSSRYPRV
Length:478
Mass (Da):50,722
Last modified:June 1, 2002 - v2
Checksum:iA5CE7F111C962044
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF089738 mRNA. Translation: AAC35987.2.
AB052757 mRNA. Translation: BAB68127.1.
AC006921 Genomic DNA. Translation: AAD21440.2.
CP002685 Genomic DNA. Translation: AEC09221.1.
CP002685 Genomic DNA. Translation: AEC09222.1.
AY050844 mRNA. Translation: AAK92779.1.
AY091183 mRNA. Translation: AAM14122.1.
PIRiE84778.
JC7770.
RefSeqiNP_565839.1. NM_129183.2.
NP_973612.1. NM_201883.1.
UniGeneiAt.14112.

Genome annotation databases

EnsemblPlantsiAT2G36250.1; AT2G36250.1; AT2G36250.
AT2G36250.2; AT2G36250.2; AT2G36250.
GeneIDi818197.
GrameneiAT2G36250.1; AT2G36250.1; AT2G36250.
AT2G36250.2; AT2G36250.2; AT2G36250.
KEGGiath:AT2G36250.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF089738 mRNA. Translation: AAC35987.2.
AB052757 mRNA. Translation: BAB68127.1.
AC006921 Genomic DNA. Translation: AAD21440.2.
CP002685 Genomic DNA. Translation: AEC09221.1.
CP002685 Genomic DNA. Translation: AEC09222.1.
AY050844 mRNA. Translation: AAK92779.1.
AY091183 mRNA. Translation: AAM14122.1.
PIRiE84778.
JC7770.
RefSeqiNP_565839.1. NM_129183.2.
NP_973612.1. NM_201883.1.
UniGeneiAt.14112.

3D structure databases

ProteinModelPortaliO82533.
SMRiO82533. Positions 119-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi3541. 7 interactions.
IntActiO82533. 1 interaction.
STRINGi3702.AT2G36250.1.

Proteomic databases

PaxDbiO82533.
PRIDEiO82533.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G36250.1; AT2G36250.1; AT2G36250.
AT2G36250.2; AT2G36250.2; AT2G36250.
GeneIDi818197.
GrameneiAT2G36250.1; AT2G36250.1; AT2G36250.
AT2G36250.2; AT2G36250.2; AT2G36250.
KEGGiath:AT2G36250.

Organism-specific databases

TAIRiAT2G36250.

Phylogenomic databases

eggNOGiENOG410IEJ4. Eukaryota.
COG0206. LUCA.
HOGENOMiHOG000049094.
InParanoidiO82533.
KOiK03531.
OMAiAQVIWGI.
PhylomeDBiO82533.

Miscellaneous databases

PROiO82533.

Gene expression databases

GenevisibleiO82533. AT.

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.
PROSITEiPS01135. FTSZ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Chloroplast division in higher plants requires members of two functionally divergent gene families with homology to bacterial ftsZ."
    Osteryoung K.W., Stokes K.D., Rutherford S.M., Percival A.L., Lee W.Y.
    Plant Cell 10:1991-2004(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: cv. Columbia.
  2. Osteryoung K.W.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Chloroplast targeting of chloroplast division FtsZ2 proteins in Arabidopsis."
    Fujiwara M., Yoshida S.
    Biochem. Biophys. Res. Commun. 287:462-467(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
    Tissue: Shoot.
  4. "Colocalization of plastid division proteins in the chloroplast stromal compartment establishes a new functional relationship between FtsZ1 and FtsZ2 in higher plants."
    McAndrew R.S., Froehlich J.E., Vitha S., Stokes K.D., Osteryoung K.W.
    Plant Physiol. 127:1656-1666(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, FUNCTION.
    Strain: cv. Columbia.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  6. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  7. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  8. "Chloroplast division and morphology are differentially affected by overexpression of FtsZ1 and FtsZ2 genes in Arabidopsis."
    Stokes K.D., McAndrew R.S., Figueroa R., Vitha S., Osteryoung K.W.
    Plant Physiol. 124:1668-1677(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "FtsZ ring formation at the chloroplast division site in plants."
    Vitha S., McAndrew R.S., Osteryoung K.W.
    J. Cell Biol. 153:111-120(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
  10. "Plastid division is mediated by combinatorial assembly of plastid division proteins."
    Maple J., Aldridge C., Moeller S.G.
    Plant J. 43:811-823(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARC6 AND FTSZ1, SELF-INTERACTION, MUTAGENESIS OF PHE-466.
  11. "Effects of mutations in Arabidopsis FtsZ1 on plastid division, FtsZ ring formation and positioning, and FtsZ filament morphology in vivo."
    Yoder D.W., Kadirjan-Kalbach D., Olson B.J.S.C., Miyagishima S.-Y., Deblasio S.L., Hangarter R.P., Osteryoung K.W.
    Plant Cell Physiol. 48:775-791(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
  12. "In vivo quantitative relationship between plastid division proteins FtsZ1 and FtsZ2 and identification of ARC6 and ARC3 in a native FtsZ complex."
    McAndrew R.S., Olson B.J., Kadirjan-Kalbach D.K., Chi-Ham C.L., Vitha S., Froehlich J.E., Osteryoung K.W.
    Biochem. J. 412:367-378(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
  13. "Sorting signals, N-terminal modifications and abundance of the chloroplast proteome."
    Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J.
    PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  14. "Arabidopsis FtsZ2-1 and FtsZ2-2 are functionally redundant, but FtsZ-based plastid division is not essential for chloroplast partitioning or plant growth and development."
    Schmitz A.J., Glynn J.M., Olson B.J.S.C., Stokes K.D., Osteryoung K.W.
    Mol. Plant 2:1211-1222(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ARC6.
  15. "Plant FtsZ1 and FtsZ2 expressed in a eukaryotic host: GTPase activity and self-assembly."
    Smith A.G., Johnson C.B., Vitha S., Holzenburg A.
    FEBS Lett. 584:166-172(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS GTPASE, SUBUNIT.
  16. "GTP-dependent heteropolymer formation and bundling of chloroplast FtsZ1 and FtsZ2."
    Olson B.J.S.C., Wang Q., Osteryoung K.W.
    J. Biol. Chem. 285:20634-20643(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS GTPASE, SUBUNIT, MUTAGENESIS OF ASP-322.
  17. "AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins."
    Ferro M., Brugiere S., Salvi D., Seigneurin-Berny D., Court M., Moyet L., Ramus C., Miras S., Mellal M., Le Gall S., Kieffer-Jaquinod S., Bruley C., Garin J., Joyard J., Masselon C., Rolland N.
    Mol. Cell. Proteomics 9:1063-1084(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  18. "Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clustering."
    Olinares P.D., Ponnala L., van Wijk K.J.
    Mol. Cell. Proteomics 9:1594-1615(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.

Entry informationi

Entry nameiFTZ21_ARATH
AccessioniPrimary (citable) accession number: O82533
Secondary accession number(s): Q93VK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: June 1, 2002
Last modified: February 17, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.