FTZ22_ARATH
ID FTZ22_ARATH Reviewed; 473 AA.
AC Q9LXJ0; Q93ZQ7;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Cell division protein FtsZ homolog 2-2, chloroplastic {ECO:0000303|PubMed:11554751};
DE Short=AtFtsZ2-2 {ECO:0000303|PubMed:11554751};
DE AltName: Full=Plastid division protein FTSZ2-2 {ECO:0000303|PubMed:11554751};
DE Flags: Precursor;
GN Name=FTSZ2-2 {ECO:0000303|PubMed:11554751};
GN OrderedLocusNames=At3g52750 {ECO:0000312|Araport:AT3G52750};
GN ORFNames=F3C22.150 {ECO:0000312|EMBL:CAB89236.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia; TISSUE=Shoot;
RX PubMed=11554751; DOI=10.1006/bbrc.2001.5588;
RA Fujiwara M., Yoshida S.;
RT "Chloroplast targeting of chloroplast division FtsZ2 proteins in
RT Arabidopsis.";
RL Biochem. Biophys. Res. Commun. 287:462-467(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=11743110; DOI=10.1104/pp.010542;
RA McAndrew R.S., Froehlich J.E., Vitha S., Stokes K.D., Osteryoung K.W.;
RT "Colocalization of plastid division proteins in the chloroplast stromal
RT compartment establishes a new functional relationship between FtsZ1 and
RT FtsZ2 in higher plants.";
RL Plant Physiol. 127:1656-1666(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Stokes K.D., Osteryoung K.W.;
RT "FtsZ2 family member AtFtsZ2-2.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=18284374; DOI=10.1042/bj20071354;
RA McAndrew R.S., Olson B.J., Kadirjan-Kalbach D.K., Chi-Ham C.L., Vitha S.,
RA Froehlich J.E., Osteryoung K.W.;
RT "In vivo quantitative relationship between plastid division proteins FtsZ1
RT and FtsZ2 and identification of ARC6 and ARC3 in a native FtsZ complex.";
RL Biochem. J. 412:367-378(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH ARC6.
RX PubMed=19995726; DOI=10.1093/mp/ssp077;
RA Schmitz A.J., Glynn J.M., Olson B.J.S.C., Stokes K.D., Osteryoung K.W.;
RT "Arabidopsis FtsZ2-1 and FtsZ2-2 are functionally redundant, but FtsZ-based
RT plastid division is not essential for chloroplast partitioning or plant
RT growth and development.";
RL Mol. Plant 2:1211-1222(2009).
RN [10]
RP PHOSPHORYLATION AT THR-282, MUTAGENESIS OF THR-282, INTERACTION WITH PGK1;
RP ARC6; FTSZ1-1; FTSZ2-1 AND FTSZ2-2, AND SUBCELLULAR LOCATION.
RX PubMed=22823492; DOI=10.1042/bj20120404;
RA Gargano D., Maple-Groedem J., Moeller S.G.;
RT "In vivo phosphorylation of FtsZ2 in Arabidopsis thaliana.";
RL Biochem. J. 446:517-521(2012).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25731613; DOI=10.1017/s1431927615000082;
RA Johnson C.B., Shaik R., Abdallah R., Vitha S., Holzenburg A.;
RT "FtsZ1/FtsZ2 turnover in chloroplasts and the role of ARC3.";
RL Microsc. Microanal. 21:313-323(2015).
RN [12]
RP SUBUNIT.
RX PubMed=27322658; DOI=10.1038/nplants.2016.95;
RA Yoshida Y., Mogi Y., TerBush A.D., Osteryoung K.W.;
RT "Chloroplast FtsZ assembles into a contractible ring via tubulin-like
RT heteropolymerization.";
RL Nat. Plants 2:16095-16095(2016).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=29920253; DOI=10.1016/j.ydbio.2018.06.010;
RA Swid N., Nevo R., Kiss V., Kapon R., Dagan S., Snir O., Adam Z.,
RA Falconet D., Reich Z., Charuvi D.;
RT "Differential impacts of FtsZ proteins on plastid division in the shoot
RT apex of Arabidopsis.";
RL Dev. Biol. 441:83-94(2018).
RN [14]
RP INTERACTION WITH CDP1/PARC6.
RC STRAIN=cv. Columbia;
RX PubMed=28984364; DOI=10.1111/ppl.12648;
RA Itoh R.D., Ishikawa H., Nakajima K.P., Moriyama S., Fujiwara M.T.;
RT "Isolation and analysis of a stromule-overproducing Arabidopsis mutant
RT suggest the role of PARC6 in plastid morphology maintenance in the leaf
RT epidermis.";
RL Physiol. Plantarum 162:479-494(2018).
CC -!- FUNCTION: Exhibits GTPase activity (By similarity). Component of the
CC plastid division machinery that forms a contractile ring at the
CC division site (PubMed:25731613). Contributes to plastid division in the
CC vegetative shoot apex, at the shoot apical meristem (SAM) where the
CC proplastid-to-chloroplast transition takes place (PubMed:29920253).
CC {ECO:0000250, ECO:0000269|PubMed:18284374, ECO:0000269|PubMed:19995726,
CC ECO:0000269|PubMed:25731613, ECO:0000269|PubMed:29920253}.
CC -!- SUBUNIT: Aggregates to form a contractile ring-like structure;
CC contraction of the ring was accompanied by an increase in the filament
CC turnover rate (PubMed:27322658). Self-interacts and binds to FTSZ1 in
CC heteropolymers to form two morphologically distinct types of filaments,
CC termed type-I (smooth filaments) and -II (rough filaments), in a GTP-
CC dependent manner (PubMed:27322658). Part of a complex made of ARC3,
CC ARC6, FTSZ1 and FTSZ2 (PubMed:22823492). Interacts (via C-terminus)
CC with ARC6. Interacts with CDP1/PARC6 (PubMed:28984364). Binds to PGK1
CC (PubMed:22823492). {ECO:0000269|PubMed:18284374,
CC ECO:0000269|PubMed:19995726, ECO:0000269|PubMed:22823492,
CC ECO:0000269|PubMed:27322658, ECO:0000269|PubMed:28984364}.
CC -!- INTERACTION:
CC Q9LXJ0; Q42545: FTSZ1; NbExp=6; IntAct=EBI-2430270, EBI-2131124;
CC Q9LXJ0; Q9LXJ0: FTSZ2-2; NbExp=4; IntAct=EBI-2430270, EBI-2430270;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:22823492}. Plastid,
CC chloroplast thylakoid membrane {ECO:0000269|PubMed:18431481};
CC Peripheral membrane protein. Note=Forms a contractile ring at the
CC chloroplast midpoint (PubMed:22823492, PubMed:25731613). Exhibits a
CC dynamic trunover in FtsZ ring facilitated by ARC3-mediated
CC destabilization (PubMed:25731613). {ECO:0000269|PubMed:22823492,
CC ECO:0000269|PubMed:25731613}.
CC -!- PTM: Phosphorylation at Thr-282 is required for the formation of
CC contractile ring at the chloroplast midpoint.
CC {ECO:0000269|PubMed:22823492}.
CC -!- DISRUPTION PHENOTYPE: Slightly reduced number of large chloroplasts due
CC to impaired plastid division (PubMed:25731613). Stronger effects on
CC pastid division in the shoot apex, where the proplastid-to-chloroplast
CC transition takes place, than in mature leaves (PubMed:29920253).
CC Increased plastid volume in the shoot apical meristem (SAM), including
CC the central zone as well as peripheral zone of L1, the outermost layer,
CC and the peripheral zone of L3 (PubMed:29920253).
CC {ECO:0000269|PubMed:18284374, ECO:0000269|PubMed:19995726,
CC ECO:0000269|PubMed:25731613, ECO:0000269|PubMed:29920253}.
CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000305}.
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DR EMBL; AF384167; AAK63846.1; -; mRNA.
DR EMBL; AL353912; CAB89236.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78989.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65557.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65558.1; -; Genomic_DNA.
DR EMBL; AY056331; AAL07180.1; -; mRNA.
DR EMBL; AY150504; AAN13020.1; -; mRNA.
DR PIR; T49028; T49028.
DR RefSeq; NP_001327516.1; NM_001339587.1.
DR RefSeq; NP_001327517.1; NM_001339586.1.
DR RefSeq; NP_190843.1; NM_115135.3.
DR AlphaFoldDB; Q9LXJ0; -.
DR SMR; Q9LXJ0; -.
DR BioGRID; 9758; 5.
DR IntAct; Q9LXJ0; 4.
DR STRING; 3702.AT3G52750.1; -.
DR PaxDb; Q9LXJ0; -.
DR PRIDE; Q9LXJ0; -.
DR ProteomicsDB; 228958; -.
DR EnsemblPlants; AT3G52750.1; AT3G52750.1; AT3G52750.
DR EnsemblPlants; AT3G52750.2; AT3G52750.2; AT3G52750.
DR EnsemblPlants; AT3G52750.3; AT3G52750.3; AT3G52750.
DR GeneID; 824441; -.
DR Gramene; AT3G52750.1; AT3G52750.1; AT3G52750.
DR Gramene; AT3G52750.2; AT3G52750.2; AT3G52750.
DR Gramene; AT3G52750.3; AT3G52750.3; AT3G52750.
DR KEGG; ath:AT3G52750; -.
DR Araport; AT3G52750; -.
DR TAIR; locus:2083258; AT3G52750.
DR eggNOG; ENOG502QRFN; Eukaryota.
DR HOGENOM; CLU_024865_3_0_1; -.
DR InParanoid; Q9LXJ0; -.
DR OMA; CDFRERI; -.
DR OrthoDB; 1148979at2759; -.
DR PhylomeDB; Q9LXJ0; -.
DR PRO; PR:Q9LXJ0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LXJ0; baseline and differential.
DR Genevisible; Q9LXJ0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070938; C:contractile ring; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009532; C:plastid stroma; IDA:TAIR.
DR GO; GO:0042651; C:thylakoid membrane; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0010020; P:chloroplast fission; IMP:UniProtKB.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0048285; P:organelle fission; IBA:GO_Central.
DR CDD; cd02201; FtsZ_type1; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR HAMAP; MF_00909; FtsZ; 1.
DR InterPro; IPR000158; Cell_div_FtsZ.
DR InterPro; IPR020805; Cell_div_FtsZ_CS.
DR InterPro; IPR045061; FtsZ/CetZ.
DR InterPro; IPR024757; FtsZ_C.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR30314; PTHR30314; 1.
DR Pfam; PF12327; FtsZ_C; 1.
DR Pfam; PF00091; Tubulin; 1.
DR PRINTS; PR00423; CELLDVISFTSZ.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR TIGRFAMs; TIGR00065; ftsZ; 1.
DR PROSITE; PS01135; FTSZ_2; 1.
PE 1: Evidence at protein level;
KW Chloroplast; GTP-binding; Membrane; Nucleotide-binding; Phosphoprotein;
KW Plastid; Reference proteome; Thylakoid; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..473
FT /note="Cell division protein FtsZ homolog 2-2,
FT chloroplastic"
FT /id="PRO_0000406891"
FT REGION 424..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 213..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 244
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 248
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 292
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT MOD_RES 282
FT /note="Phosphothreonine; by PGK1"
FT /evidence="ECO:0000269|PubMed:22823492"
FT MUTAGEN 282
FT /note="T->V: Normal interaction with FtsZ proteins and with
FT ARC6. Lost ability to form contractile ring at the
FT chloroplast midpoint."
FT /evidence="ECO:0000269|PubMed:22823492"
FT CONFLICT 269
FT /note="I -> N (in Ref. 6; AAL07180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 50317 MW; 96A32AC96CFCEDB3 CRC64;
MAAYVSPCLT PPDSRVLTVL RKSVLPDHHL GTRVGCLRMS EGTTKRYRVV ASHKYESSSI
RNSLNSHSTS HFQSQDSFLN LHPEISMLNP RKETSSVPIT EDLDELSTPN TYNEARIKVI
GVGGGGSNAV NRMIESEMIG VEFWIVNTDI QAMRISPVFP DNRLQIGKEL TRGLGAGGNP
EIGMNAATES KEAIQEALYG SDMVFVTAGM GGGTGTGGAP IIAGVAKAMG ILTVGIVTTP
FSFEGRRRAL QAQEGIAALR DNVDTLIVIP NDKLLAAVSQ STPVTEAFNL ADDILRQGVR
GISDIITIPG LVNVDFADVR AIMANAGSSL MGIGTATGKT RARDAALNAI QSPLLDIGIE
RATGIVWNIT GGSDLTLFEV NAAAEVIYDL VDPTANLIFG AVVDPSYSGQ ISITLIATGF
KRQEEGEGRP LQATQADASM GATRRPSSSF TEGSSIEIPE FLKKKGRSRY PRL
