FTZ21_ARATH
ID FTZ21_ARATH Reviewed; 478 AA.
AC O82533; Q93VK3;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cell division protein FtsZ homolog 2-1, chloroplastic {ECO:0000303|PubMed:9836740};
DE Short=AtFtsZ2-1 {ECO:0000303|PubMed:9836740};
DE AltName: Full=Plastid division protein FTSZ2-1 {ECO:0000303|PubMed:9836740};
DE Flags: Precursor;
GN Name=FTSZ2-1 {ECO:0000303|PubMed:9836740};
GN OrderedLocusNames=At2g36250 {ECO:0000312|Araport:AT2G36250};
GN ORFNames=F2H17.14 {ECO:0000312|EMBL:AAD21440.2};
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 FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9836740; DOI=10.2307/3870779;
RA Osteryoung K.W., Stokes K.D., Rutherford S.M., Percival A.L., Lee W.Y.;
RT "Chloroplast division in higher plants requires members of two functionally
RT divergent gene families with homology to bacterial ftsZ.";
RL Plant Cell 10:1991-2004(1998).
RN [2]
RP SEQUENCE REVISION.
RA Osteryoung K.W.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [6]
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 [7]
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 [8]
RP FUNCTION.
RX PubMed=11115884; DOI=10.1104/pp.124.4.1668;
RA Stokes K.D., McAndrew R.S., Figueroa R., Vitha S., Osteryoung K.W.;
RT "Chloroplast division and morphology are differentially affected by
RT overexpression of FtsZ1 and FtsZ2 genes in Arabidopsis.";
RL Plant Physiol. 124:1668-1677(2000).
RN [9]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=11285278; DOI=10.1083/jcb.153.1.111;
RA Vitha S., McAndrew R.S., Osteryoung K.W.;
RT "FtsZ ring formation at the chloroplast division site in plants.";
RL J. Cell Biol. 153:111-120(2001).
RN [10]
RP INTERACTION WITH ARC6 AND FTSZ1, SELF-INTERACTION, AND MUTAGENESIS OF
RP PHE-466.
RX PubMed=16146521; DOI=10.1111/j.1365-313x.2005.02493.x;
RA Maple J., Aldridge C., Moeller S.G.;
RT "Plastid division is mediated by combinatorial assembly of plastid division
RT proteins.";
RL Plant J. 43:811-823(2005).
RN [11]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=17468127; DOI=10.1093/pcp/pcm049;
RA Yoder D.W., Kadirjan-Kalbach D., Olson B.J.S.C., Miyagishima S.-Y.,
RA Deblasio S.L., Hangarter R.P., Osteryoung K.W.;
RT "Effects of mutations in Arabidopsis FtsZ1 on plastid division, FtsZ ring
RT formation and positioning, and FtsZ filament morphology in vivo.";
RL Plant Cell Physiol. 48:775-791(2007).
RN [12]
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 [13]
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 [14]
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 [15]
RP FUNCTION AS GTPASE, AND SUBUNIT.
RX PubMed=19925792; DOI=10.1016/j.febslet.2009.11.044;
RA Smith A.G., Johnson C.B., Vitha S., Holzenburg A.;
RT "Plant FtsZ1 and FtsZ2 expressed in a eukaryotic host: GTPase activity and
RT self-assembly.";
RL FEBS Lett. 584:166-172(2010).
RN [16]
RP FUNCTION AS GTPASE, SUBUNIT, AND MUTAGENESIS OF ASP-322.
RX PubMed=20421292; DOI=10.1074/jbc.m110.122614;
RA Olson B.J.S.C., Wang Q., Osteryoung K.W.;
RT "GTP-dependent heteropolymer formation and bundling of chloroplast FtsZ1
RT and FtsZ2.";
RL J. Biol. Chem. 285:20634-20643(2010).
RN [17]
RP PHOSPHORYLATION AT SER-143, MUTAGENESIS OF SER-143 AND THR-286, INTERACTION
RP WITH PGK1; ARC6; FTSZ1-1; FTSZ2-1 AND FTSZ2-2, PTM, AND SUBCELLULAR
RP 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 [18]
RP INDUCTION BY GIBBERELLIC ACID.
RX PubMed=23020316; DOI=10.1111/j.1365-313x.2012.05118.x;
RA Jiang X., Li H., Wang T., Peng C., Wang H., Wu H., Wang X.;
RT "Gibberellin indirectly promotes chloroplast biogenesis as a means to
RT maintain the chloroplast population of expanded cells.";
RL Plant J. 72:768-780(2012).
RN [19]
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 [20]
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 [21]
RP MUTAGENESIS OF PHE-466, AND INTERACTION WITH ARC6 AND CDP1/PARC6.
RC STRAIN=cv. Columbia;
RX PubMed=26527658; DOI=10.1104/pp.15.01460;
RA Zhang M., Chen C., Froehlich J.E., TerBush A.D., Osteryoung K.W.;
RT "Roles of Arabidopsis PARC6 in Coordination of the Chloroplast Division
RT Complex and Negative Regulation of FtsZ Assembly.";
RL Plant Physiol. 170:250-262(2016).
RN [22]
RP PTM, SUBUNIT, INTERACTION WITH ARC3 AND ARC6, AND ACTIVITY REGULATION.
RX PubMed=29138260; DOI=10.1042/bcj20170697;
RA Shaik R.S., Sung M.W., Vitha S., Holzenburg A.;
RT "Chloroplast division protein ARC3 acts on FtsZ2 by preventing filament
RT bundling and enhancing GTPase activity.";
RL Biochem. J. 475:99-115(2018).
RN [23]
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 [24]
RP FUNCTION, MUTAGENESIS OF ASP-322, SUBUNIT, INTERACTION WITH ARC6, AND
RP SUBCELLULAR LOCATION.
RX PubMed=29769312; DOI=10.1074/jbc.ra117.000999;
RA Sung M.W., Shaik R., TerBush A.D., Osteryoung K.W., Vitha S.,
RA Holzenburg A.;
RT "The chloroplast division protein ARC6 acts to inhibit disassembly of GDP-
RT bound FtsZ2.";
RL J. Biol. Chem. 293:10692-10706(2018).
RN [25]
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).
RN [26]
RP INTERACTION WITH MCD1 AND ARC6.
RC STRAIN=cv. Columbia;
RX PubMed=29967285; DOI=10.1105/tpc.18.00189;
RA Chen L., Sun B., Gao W., Zhang Q.Y., Yuan H., Zhang M.;
RT "MCD1 associates with FtsZ filaments via the membrane-tethering protein
RT ARC6 to guide chloroplast division.";
RL Plant Cell 30:1807-1823(2018).
RN [27]
RP SUBUNIT, AND INTERACTION WITH ARC3.
RC STRAIN=cv. Columbia;
RX PubMed=30824505; DOI=10.1105/tpc.18.00948;
RA Chen C., Cao L., Yang Y., Porter K.J., Osteryoung K.W.;
RT "ARC3 activation by PARC6 promotes FtsZ-ring remodeling at the chloroplast
RT division site.";
RL Plant Cell 31:862-885(2019).
CC -!- FUNCTION: Exhibits GTPase activity which converts GTP ligands to GDP
CC (PubMed:29769312). Component of the plastid division machinery
CC consisting in a binary fission accomplished by the simultaneous
CC constriction of the FtsZ ring on the stromal side of the inner envelope
CC membrane, and the ARC5 ring on the cytosolic side of the outer envelope
CC membrane (PubMed:25731613). Required for plastid division in a dose-
CC dependent manner. In the vegetative shoot apex, at the shoot apical
CC meristem (SAM), where the proplastid-to-chloroplast transition takes
CC place, major contributor of plastid division in the L1 and L3 layers
CC and contributes equally with FTSZ1 in the L2 layer (PubMed:29920253).
CC {ECO:0000269|PubMed:11115884, ECO:0000269|PubMed:11743110,
CC ECO:0000269|PubMed:18284374, ECO:0000269|PubMed:19925792,
CC ECO:0000269|PubMed:19995726, ECO:0000269|PubMed:20421292,
CC ECO:0000269|PubMed:25731613, ECO:0000269|PubMed:29769312,
CC ECO:0000269|PubMed:29920253, ECO:0000269|PubMed:9836740}.
CC -!- ACTIVITY REGULATION: GTPase activity is enhanced by ARC3.
CC {ECO:0000269|PubMed:29138260}.
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:29769312, PubMed:27322658). Self-interacts and
CC binds to FTSZ1 in heteromers to form two morphologically distinct types
CC of filaments, termed type-I (smooth filaments) and -II (rough
CC filaments), in a GTP-dependent manner; the GDP-induced disassembly is
CC inhibited by ARC6 (PubMed:29769312, PubMed:27322658). Interacts (via C-
CC terminus) with ARC6; this interaction enables ARC3 binding to FTSZ2
CC (PubMed:29967285, PubMed:29769312, PubMed:29138260). Part of a complex
CC made of ARC3, ARC6, FTSZ1 and FTSZ2 (PubMed:22823492). Binds to MCD1 in
CC an ARC6-dependent manner (PubMed:29967285). Binds to CDP1/PARC6
CC (PubMed:26527658, PubMed:28984364). Part of a complex made of
CC CDP1/PARC6, ARC3 and FtsZ proteins in the middle of the plastid; this
CC complex enhances the dynamics of Z rings during chloroplast division
CC (PubMed:30824505). Binds to PGK1 (PubMed:22823492).
CC {ECO:0000269|PubMed:16146521, ECO:0000269|PubMed:18284374,
CC ECO:0000269|PubMed:19925792, ECO:0000269|PubMed:19995726,
CC ECO:0000269|PubMed:20421292, ECO:0000269|PubMed:22823492,
CC ECO:0000269|PubMed:26527658, ECO:0000269|PubMed:27322658,
CC ECO:0000269|PubMed:28984364, ECO:0000269|PubMed:29138260,
CC ECO:0000269|PubMed:29769312, ECO:0000269|PubMed:29967285,
CC ECO:0000269|PubMed:30824505}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:22823492,
CC ECO:0000269|PubMed:29769312}. Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:18431481}; Peripheral membrane protein. Note=Forms
CC a contractile ring at the chloroplast midpoint that coaligns with FTSZ1
CC rings (PubMed:18431481, PubMed:29769312, PubMed:22823492,
CC PubMed:25731613). Exhibits a dynamic trunover in FtsZ ring facilitated
CC by ARC3-mediated destabilization (PubMed:25731613).
CC {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:22823492,
CC ECO:0000269|PubMed:25731613, ECO:0000269|PubMed:29769312}.
CC -!- INDUCTION: Slightly induced by gibberellic acid (GA).
CC {ECO:0000269|PubMed:23020316}.
CC -!- PTM: Filaments containing FTSZ2-1 are stabilized when in complex with
CC GTP but destabilized after conversion of GTP into GDP; ARC6 conteracts
CC this destabilisation by preventing the dissociation of GDP-bound FTSZ2
CC molecules thus inhibiting filament disassembly whereas ARC3 promotes
CC GTPase activity thus accelerating the conversion of GTP into GDP and
CC triggering FtsZ2 filaments disassembly. {ECO:0000269|PubMed:29138260,
CC ECO:0000269|PubMed:29769312}.
CC -!- PTM: Phosphorylation at Ser-143 is necessary for interactions with
CC ARC3, ARC6, FTSZ1 and FTSZ2-2. Phosphorylations at Ser-143 and Thr-286
CC are required for the formation of contractile ring at the chloroplast
CC midpoint. {ECO:0000269|PubMed:22823492}.
CC -!- DISRUPTION PHENOTYPE: Reduced number of heterogeneous large chloroplast
CC population (small and large plastids) due to impaired plastid division
CC (PubMed:25731613). Increased plastid volume in young leaf primordia and
CC in the shoot apical meristem (SAM), including the central zone as well
CC as peripheral zone of L1, the outermost layer, the peripheral zone of
CC L2, 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; AF089738; AAC35987.2; -; mRNA.
DR EMBL; AB052757; BAB68127.1; -; mRNA.
DR EMBL; AC006921; AAD21440.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09221.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09222.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61304.1; -; Genomic_DNA.
DR EMBL; AY050844; AAK92779.1; -; mRNA.
DR EMBL; AY091183; AAM14122.1; -; mRNA.
DR PIR; E84778; E84778.
DR PIR; JC7770; JC7770.
DR RefSeq; NP_001323530.1; NM_001336588.1.
DR RefSeq; NP_565839.1; NM_129183.2.
DR RefSeq; NP_973612.1; NM_201883.1.
DR AlphaFoldDB; O82533; -.
DR SMR; O82533; -.
DR BioGRID; 3541; 9.
DR IntAct; O82533; 2.
DR STRING; 3702.AT2G36250.2; -.
DR PaxDb; O82533; -.
DR PRIDE; O82533; -.
DR ProteomicsDB; 230003; -.
DR EnsemblPlants; AT2G36250.1; AT2G36250.1; AT2G36250.
DR EnsemblPlants; AT2G36250.2; AT2G36250.2; AT2G36250.
DR EnsemblPlants; AT2G36250.3; AT2G36250.3; AT2G36250.
DR GeneID; 818197; -.
DR Gramene; AT2G36250.1; AT2G36250.1; AT2G36250.
DR Gramene; AT2G36250.2; AT2G36250.2; AT2G36250.
DR Gramene; AT2G36250.3; AT2G36250.3; AT2G36250.
DR KEGG; ath:AT2G36250; -.
DR Araport; AT2G36250; -.
DR TAIR; locus:2049455; AT2G36250.
DR eggNOG; ENOG502QRFN; Eukaryota.
DR HOGENOM; CLU_024865_3_0_1; -.
DR InParanoid; O82533; -.
DR OrthoDB; 1148979at2759; -.
DR PhylomeDB; O82533; -.
DR PRO; PR:O82533; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82533; baseline and differential.
DR Genevisible; O82533; 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:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0010020; P:chloroplast fission; IMP:UniProtKB.
DR GO; GO:0048285; P:organelle fission; IBA:GO_Central.
DR GO; GO:0009739; P:response to gibberellin; IEP:UniProtKB.
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 ?..478
FT /note="Cell division protein FtsZ homolog 2-1,
FT chloroplastic"
FT /id="PRO_0000406890"
FT REGION 86..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128..132
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 217..219
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 252
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 296
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT MOD_RES 143
FT /note="Phosphoserine; by PGK1"
FT /evidence="ECO:0000269|PubMed:22823492"
FT MOD_RES 286
FT /note="Phosphothreonine; by PGK1"
FT /evidence="ECO:0000250|UniProtKB:Q9LXJ0"
FT MUTAGEN 143
FT /note="S->A: Reduced interaction with FTSZ1-1 and FTSZ2-2
FT and inpaired interaction with FTSZ2-1 and ARC6. Lost
FT ability to form contractile ring at the chloroplast
FT midpoint."
FT /evidence="ECO:0000269|PubMed:22823492"
FT MUTAGEN 286
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 MUTAGEN 322
FT /note="D->A: Impaired GTPase activity leading to the lack
FT of GDP binding and the formation of aster-shaped structures
FT of more stable filaments associated with a weaker ARC6-
FT binding."
FT /evidence="ECO:0000269|PubMed:20421292,
FT ECO:0000269|PubMed:29769312"
FT MUTAGEN 466
FT /note="F->A: Reduced ARC6 binding and abolished CDP1/PARC6
FT binding."
FT /evidence="ECO:0000269|PubMed:16146521,
FT ECO:0000269|PubMed:26527658"
SQ SEQUENCE 478 AA; 50722 MW; A5CE7F111C962044 CRC64;
MATYVSPCFT PSDSRLLTVL RKNVLPENHL GRLNSIRTID SKKNRVVVAA QKSESSPIRN
SPRHYQSQAQ DPFLNLHPEI SMLRGEGTST IVNPRKETSS GPVVEDFEEP SAPSNYNEAR
IKVIGVGGGG SNAVNRMIES EMSGVEFWIV NTDIQAMRMS PVLPDNRLQI GKELTRGLGA
GGNPEIGMNA ARESKEVIEE ALYGSDMVFV TAGMGGGTGT GAAPVIAGIA KAMGILTVGI
ATTPFSFEGR RRTVQAQEGL ASLRDNVDTL IVIPNDKLLT AVSQSTPVTE AFNLADDILR
QGVRGISDII TIPGLVNVDF ADVRAIMANA GSSLMGIGTA TGKSRARDAA LNAIQSPLLD
IGIERATGIV WNITGGSDLT LFEVNAAAEV IYDLVDPTAN LIFGAVVDPA LSGQVSITLI
ATGFKRQEEG EGRTVQMVQA DAASVGATRR PSSSFRESGS VEIPEFLKKK GSSRYPRV
