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Protein

Cell division protein FtsZ homolog 2-2, chloroplastic

Gene

FTSZ2-2

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 (By similarity). Component of the plastid division machinery that forms a contractile ring at the division site.By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei244 – 2441GTPBy similarity
Binding sitei248 – 2481GTPBy similarity
Binding sitei292 – 2921GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi124 – 1285GTPBy similarity
Nucleotide bindingi213 – 2153GTPBy similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsZ homolog 2-2, chloroplastic
Short name:
AtFtsZ2-2
Alternative name(s):
Plastid division protein FTSZ2-2
Gene namesi
Name:FTSZ2-2
Ordered Locus Names:At3g52750
ORF Names:F3C22.150
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G52750.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Thylakoid

Pathology & Biotechi

Disruption phenotypei

Slightly reduced number of large chloroplasts due to impaired plastid division.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 473Cell division protein FtsZ homolog 2-2, chloroplasticPRO_0000406891
Transit peptidei1 – ?ChloroplastSequence analysis

Proteomic databases

PaxDbiQ9LXJ0.
PRIDEiQ9LXJ0.

Expressioni

Gene expression databases

GenevisibleiQ9LXJ0. 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. Part of a complex made of ARC3, ARC6, FTSZ1 and FTSZ2. Interacts (via C-terminus) with ARC6.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-2430270,EBI-2430270
FTSZ1Q425456EBI-2430270,EBI-2131124

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein self-association Source: UniProtKB

Protein-protein interaction databases

BioGridi9758. 5 interactions.
IntActiQ9LXJ0. 4 interactions.
STRINGi3702.AT3G52750.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LXJ0.
SMRiQ9LXJ0. Positions 115-420.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FtsZ family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IEJ4. Eukaryota.
COG0206. LUCA.
HOGENOMiHOG000049094.
InParanoidiQ9LXJ0.
KOiK03531.
OMAiGDNSRSH.
PhylomeDBiQ9LXJ0.

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.

Q9LXJ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAYVSPCLT PPDSRVLTVL RKSVLPDHHL GTRVGCLRMS EGTTKRYRVV
60 70 80 90 100
ASHKYESSSI RNSLNSHSTS HFQSQDSFLN LHPEISMLNP RKETSSVPIT
110 120 130 140 150
EDLDELSTPN TYNEARIKVI GVGGGGSNAV NRMIESEMIG VEFWIVNTDI
160 170 180 190 200
QAMRISPVFP DNRLQIGKEL TRGLGAGGNP EIGMNAATES KEAIQEALYG
210 220 230 240 250
SDMVFVTAGM GGGTGTGGAP IIAGVAKAMG ILTVGIVTTP FSFEGRRRAL
260 270 280 290 300
QAQEGIAALR DNVDTLIVIP NDKLLAAVSQ STPVTEAFNL ADDILRQGVR
310 320 330 340 350
GISDIITIPG LVNVDFADVR AIMANAGSSL MGIGTATGKT RARDAALNAI
360 370 380 390 400
QSPLLDIGIE RATGIVWNIT GGSDLTLFEV NAAAEVIYDL VDPTANLIFG
410 420 430 440 450
AVVDPSYSGQ ISITLIATGF KRQEEGEGRP LQATQADASM GATRRPSSSF
460 470
TEGSSIEIPE FLKKKGRSRY PRL
Length:473
Mass (Da):50,317
Last modified:October 1, 2000 - v1
Checksum:i96A32AC96CFCEDB3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti269 – 2691I → N in AAL07180 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF384167 mRNA. Translation: AAK63846.1.
AL353912 Genomic DNA. Translation: CAB89236.1.
CP002686 Genomic DNA. Translation: AEE78989.1.
AY056331 mRNA. Translation: AAL07180.1.
AY150504 mRNA. Translation: AAN13020.1.
PIRiT49028.
RefSeqiNP_190843.1. NM_115135.2.
UniGeneiAt.1742.

Genome annotation databases

EnsemblPlantsiAT3G52750.1; AT3G52750.1; AT3G52750.
GeneIDi824441.
GrameneiAT3G52750.1; AT3G52750.1; AT3G52750.
KEGGiath:AT3G52750.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF384167 mRNA. Translation: AAK63846.1.
AL353912 Genomic DNA. Translation: CAB89236.1.
CP002686 Genomic DNA. Translation: AEE78989.1.
AY056331 mRNA. Translation: AAL07180.1.
AY150504 mRNA. Translation: AAN13020.1.
PIRiT49028.
RefSeqiNP_190843.1. NM_115135.2.
UniGeneiAt.1742.

3D structure databases

ProteinModelPortaliQ9LXJ0.
SMRiQ9LXJ0. Positions 115-420.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9758. 5 interactions.
IntActiQ9LXJ0. 4 interactions.
STRINGi3702.AT3G52750.1.

Proteomic databases

PaxDbiQ9LXJ0.
PRIDEiQ9LXJ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G52750.1; AT3G52750.1; AT3G52750.
GeneIDi824441.
GrameneiAT3G52750.1; AT3G52750.1; AT3G52750.
KEGGiath:AT3G52750.

Organism-specific databases

TAIRiAT3G52750.

Phylogenomic databases

eggNOGiENOG410IEJ4. Eukaryota.
COG0206. LUCA.
HOGENOMiHOG000049094.
InParanoidiQ9LXJ0.
KOiK03531.
OMAiGDNSRSH.
PhylomeDBiQ9LXJ0.

Miscellaneous databases

PROiQ9LXJ0.

Gene expression databases

GenevisibleiQ9LXJ0. 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 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.
  2. "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.
    Strain: cv. Columbia.
  3. "FtsZ2 family member AtFtsZ2-2."
    Stokes K.D., Osteryoung K.W.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  4. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "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.
  7. "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.
  8. "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].
  9. "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.
  10. "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].
  11. "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 nameiFTZ22_ARATH
AccessioniPrimary (citable) accession number: Q9LXJ0
Secondary accession number(s): Q93ZQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 119 of the entry and version 1 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.