FTSZ1_ARATH
ID FTSZ1_ARATH Reviewed; 433 AA.
AC Q42545; Q9FLN6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Cell division protein FtsZ homolog 1, chloroplastic {ECO:0000303|PubMed:11115884};
DE Short=AtFtsZ1 {ECO:0000303|PubMed:11115884};
DE Short=AtFtsZ1-1 {ECO:0000303|PubMed:9836740};
DE Short=Chloroplast FtsZ {ECO:0000303|PubMed:7637778};
DE Short=CpFtsZ {ECO:0000303|PubMed:7637778};
DE AltName: Full=Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 10 {ECO:0000303|PubMed:10213777};
DE AltName: Full=Protein PLASTID MOVEMENT IMPAIRED4 {ECO:0000303|PubMed:16113226};
DE Flags: Precursor;
GN Name=FTSZ1 {ECO:0000303|PubMed:11115884};
GN Synonyms=ARC10 {ECO:0000303|PubMed:10213777},
GN FTSZ1-1 {ECO:0000303|PubMed:9836740}, PMI4 {ECO:0000303|PubMed:16113226};
GN OrderedLocusNames=At5g55280 {ECO:0000312|Araport:AT5G55280};
GN ORFNames=MCO15.23 {ECO:0000312|EMBL:BAB08597.1};
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].
RC STRAIN=cv. Columbia;
RX PubMed=7637778; DOI=10.1038/376473b0;
RA Osteryoung K.W., Vierling E.;
RT "Conserved cell and organelle division.";
RL Nature 376:473-474(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [3]
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 [4]
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 [5]
RP 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 [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-366.
RX PubMed=10213777; DOI=10.2307/3870883;
RA Pyke K.A.;
RT "Plastid division and development.";
RL Plant Cell 11:549-556(1999).
RN [7]
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 [8]
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 [9]
RP 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 [10]
RP INTERACTION WITH FTSZ2-1, AND SELF-INTERACTION.
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 FUNCTION, AND MUTAGENESIS OF GLY-267.
RX PubMed=16113226; DOI=10.1104/pp.105.061887;
RA DeBlasio S.L., Luesse D.L., Hangarter R.P.;
RT "A plant-specific protein essential for blue-light-induced chloroplast
RT movements.";
RL Plant Physiol. 139:101-114(2005).
RN [12]
RP INTERACTION WITH ARC3.
RX PubMed=17304239; DOI=10.1038/sj.embor.7400902;
RA Maple J., Vojta L., Soll J., Moeller S.G.;
RT "ARC3 is a stromal Z-ring accessory protein essential for plastid
RT division.";
RL EMBO Rep. 8:293-299(2007).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-159; GLY-267; ARG-298
RP AND GLY-366, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija-2;
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 [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=17725544; DOI=10.1042/bj20070543;
RA El-Kafafi E.-S., Karamoko M., Pignot-Paintrand I., Grunwald D.,
RA Mandaron P., Lerbs-Mache S., Falconet D.;
RT "Developmentally regulated association of plastid division protein FtsZ1
RT with thylakoid membranes in Arabidopsis thaliana.";
RL Biochem. J. 409:87-94(2008).
RN [15]
RP 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 [16]
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 [17]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18204083; DOI=10.1093/pcp/pcn012;
RA Fujiwara M.T., Hashimoto H., Kazama Y., Abe T., Yoshida S., Sato N.,
RA Itoh R.D.;
RT "The assembly of the FtsZ ring at the mid-chloroplast division site depends
RT on a balance between the activities of AtMinE1 and ARC11/AtMinD1.";
RL Plant Cell Physiol. 49:345-361(2008).
RN [18]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19403522; DOI=10.1093/pcp/pcp063;
RA Fujiwara M.T., Sekine K., Yamamoto Y.Y., Abe T., Sato N., Itoh R.D.;
RT "Live imaging of chloroplast FtsZ1 filaments, rings, spirals, and motile
RT dot structures in the AtMinE1 mutant and overexpressor of Arabidopsis
RT thaliana.";
RL Plant Cell Physiol. 50:1116-1126(2009).
RN [19]
RP FUNCTION, 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 [20]
RP FUNCTION AS GTPASE, SUBUNIT, AND MUTAGENESIS OF ASP-275.
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 [21]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND SUBUNIT.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=20195657; DOI=10.1007/s00709-010-0119-7;
RA Fujiwara M.T., Hashimoto H., Kazama Y., Hirano T., Yoshioka Y., Aoki S.,
RA Sato N., Itoh R.D., Abe T.;
RT "Dynamic morphologies of pollen plastids visualised by vegetative-specific
RT FtsZ1-GFP in Arabidopsis thaliana.";
RL Protoplasma 242:19-33(2010).
RN [22]
RP INTERACTION WITH ARC6; FTSZ2-1 AND FTSZ2-2.
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 [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-67, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER CYS-66, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [24]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=26500667; DOI=10.3389/fpls.2015.00823;
RA Fujiwara M.T., Kojo K.H., Kazama Y., Sasaki S., Abe T., Itoh R.D.;
RT "The Arabidopsis minE mutation causes new plastid and FtsZ1 localization
RT phenotypes in the leaf epidermis.";
RL Front. Plant Sci. 6:823-823(2015).
RN [25]
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 [26]
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 [27]
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 [28]
RP SUBCELLULAR LOCATION.
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 [29]
RP 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. Component of the plastid division
CC machinery that forms a contractile ring at the division site
CC (PubMed:25731613). Required for plastid division in a dose-dependent
CC manner. Involved in epidermal plastids division in a MINE1-dependent
CC manner (PubMed:26500667). Involved in blue light-induced chloroplast
CC movements. May regulate thylakoid development. In the vegetative shoot
CC apex, at the shoot apical meristem (SAM), where the proplastid-to-
CC chloroplast transition takes place, contributes equally with FTSZ2-1 in
CC the L2 layer to plastid division (PubMed:29920253).
CC {ECO:0000269|PubMed:10213777, ECO:0000269|PubMed:11115884,
CC ECO:0000269|PubMed:11743110, ECO:0000269|PubMed:16113226,
CC ECO:0000269|PubMed:17468127, ECO:0000269|PubMed:17725544,
CC ECO:0000269|PubMed:19925792, ECO:0000269|PubMed:20421292,
CC ECO:0000269|PubMed:25731613, ECO:0000269|PubMed:26500667,
CC ECO:0000269|PubMed:29920253, ECO:0000269|PubMed:9836740}.
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). This aggregation is regulated in
CC midchloroplast stroma by MIND1 (repressor) and MINE1 (promoter). Self-
CC interacts and binds to FTSZ2-1 in heteromers to form two
CC morphologically distinct types of filaments, termed type-I (smooth
CC filaments) and type-II (rough filaments), in a GTP-dependent manner
CC (PubMed:27322658). Interacts with ARC3. Part of a complex made of ARC3,
CC ARC6, FTSZ1 and FTSZ2 (PubMed:30824505, PubMed:22823492).
CC {ECO:0000269|PubMed:16146521, ECO:0000269|PubMed:17304239,
CC ECO:0000269|PubMed:18204083, ECO:0000269|PubMed:18284374,
CC ECO:0000269|PubMed:19403522, ECO:0000269|PubMed:19925792,
CC ECO:0000269|PubMed:20195657, ECO:0000269|PubMed:20421292,
CC ECO:0000269|PubMed:22823492, ECO:0000269|PubMed:27322658,
CC ECO:0000269|PubMed:30824505}.
CC -!- INTERACTION:
CC Q42545; Q9FIG9: ARC6; NbExp=2; IntAct=EBI-2131124, EBI-2000800;
CC Q42545; Q42545: FTSZ1; NbExp=3; IntAct=EBI-2131124, EBI-2131124;
CC Q42545; Q9LXJ0: FTSZ2-2; NbExp=6; IntAct=EBI-2131124, EBI-2430270;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:26500667,
CC ECO:0000269|PubMed:29967285}. 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
CC FTSZ2-1 rings (PubMed:29967285, PubMed:25731613, PubMed:26500667).
CC Exhibits a dynamic trunover in FtsZ ring facilitated by ARC3-mediated
CC destabilization (PubMed:25731613). {ECO:0000269|PubMed:25731613,
CC ECO:0000269|PubMed:26500667, ECO:0000269|PubMed:29967285}.
CC -!- TISSUE SPECIFICITY: In pollen grain, restricted to plastids of
CC vegetative cells. Also present in pollen tubes plastids.
CC {ECO:0000269|PubMed:20195657}.
CC -!- DISRUPTION PHENOTYPE: Highly heterogeneous chloroplast population with
CC giant chloroplasts and some smaller (PubMed:25731613). Impaired
CC chloroplast division, some green cells with one single big chloroplast
CC (PubMed:25731613). Abnormal thylakoids (PubMed:25731613). Increased
CC plastid volume in young leaf primordia and in the shoot apical meristem
CC (SAM), including the central zone as well as peripheral zone of L1, the
CC outermost layer, the peripheral zone of L2, and the peripheral zone of
CC L3 (PubMed:29920253). {ECO:0000269|PubMed:17468127,
CC ECO:0000269|PubMed:17725544, ECO:0000269|PubMed:25731613,
CC ECO:0000269|PubMed:29920253}.
CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000305}.
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DR EMBL; U39877; AAA82068.1; -; mRNA.
DR EMBL; AB010071; BAB08597.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96609.1; -; Genomic_DNA.
DR EMBL; AY034992; AAK59497.1; -; mRNA.
DR EMBL; AY113896; AAM44944.1; -; mRNA.
DR RefSeq; NP_200339.1; NM_124910.6.
DR AlphaFoldDB; Q42545; -.
DR SMR; Q42545; -.
DR BioGRID; 20865; 5.
DR IntAct; Q42545; 5.
DR MINT; Q42545; -.
DR STRING; 3702.AT5G55280.1; -.
DR iPTMnet; Q42545; -.
DR PaxDb; Q42545; -.
DR PRIDE; Q42545; -.
DR ProteomicsDB; 230552; -.
DR EnsemblPlants; AT5G55280.1; AT5G55280.1; AT5G55280.
DR GeneID; 835621; -.
DR Gramene; AT5G55280.1; AT5G55280.1; AT5G55280.
DR KEGG; ath:AT5G55280; -.
DR Araport; AT5G55280; -.
DR TAIR; locus:2161610; AT5G55280.
DR eggNOG; ENOG502QRFN; Eukaryota.
DR HOGENOM; CLU_024865_0_0_1; -.
DR InParanoid; Q42545; -.
DR OMA; GNPSIGQ; -.
DR OrthoDB; 1148979at2759; -.
DR PhylomeDB; Q42545; -.
DR PRO; PR:Q42545; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q42545; baseline and differential.
DR Genevisible; Q42545; AT.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
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:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0010020; P:chloroplast fission; IMP:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:UniProtKB.
DR GO; GO:0009902; P:chloroplast relocation; IMP:UniProtKB.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0048285; P:organelle fission; IBA:GO_Central.
DR GO; GO:0043572; P:plastid fission; IMP:TAIR.
DR GO; GO:0009637; P:response to blue light; IMP: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; IPR017975; Tubulin_CS.
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; PS01134; FTSZ_1; 1.
DR PROSITE; PS01135; FTSZ_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Chloroplast; GTP-binding; Membrane;
KW Nucleotide-binding; Plastid; Reference proteome; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 67..433
FT /note="Cell division protein FtsZ homolog 1, chloroplastic"
FT /id="PRO_0000010306"
FT REGION 399..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 170..172
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 201
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 249
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT MOD_RES 67
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 159
FT /note="D->N: Forms long filaments with impaired
FT midplastidial localization, heterogeneous chloroplast
FT population, one greatly enlarged with numerous smaller
FT chloroplasts per cell."
FT /evidence="ECO:0000269|PubMed:17468127"
FT MUTAGEN 267
FT /note="G->R: In pmi4; reduced accumulation with impaired
FT midplastidial localization in rings and filaments, giant
FT chloroplasts, and altered chloroplast movements in response
FT to blue light."
FT /evidence="ECO:0000269|PubMed:16113226,
FT ECO:0000269|PubMed:17468127"
FT MUTAGEN 275
FT /note="D->A: Impaired GTPase activity."
FT /evidence="ECO:0000269|PubMed:20421292"
FT MUTAGEN 298
FT /note="R->Q: Reduced accumulation, heterogeneous
FT chloroplast population."
FT /evidence="ECO:0000269|PubMed:17468127"
FT MUTAGEN 366
FT /note="G->A: In arc10; forms long filaments, heterogeneous
FT chloroplast population, one greatly enlarged with numerous
FT smaller chloroplasts per cell."
FT /evidence="ECO:0000269|PubMed:10213777,
FT ECO:0000269|PubMed:17468127"
FT CONFLICT 115
FT /note="S -> F (in Ref. 1; AAA82068)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 45565 MW; 82C942D597171EDB CRC64;
MAIIPLAQLN ELTISSSSSS FLTKSISSHS LHSSCICASS RISQFRGGFS KRRSDSTRSK
SMRLRCSFSP MESARIKVIG VGGGGNNAVN RMISSGLQSV DFYAINTDSQ ALLQSSAENP
LQIGELLTRG LGTGGNPLLG EQAAEESKDA IANALKGSDL VFITAGMGGG TGSGAAPVVA
QISKDAGYLT VGVVTYPFSF EGRKRSLQAL EAIEKLQKNV DTLIVIPNDR LLDIADEQTP
LQDAFLLADD VLRQGVQGIS DIITIPGLVN VDFADVKAVM KDSGTAMLGV GVSSSKNRAE
EAAEQATLAP LIGSSIQSAT GVVYNITGGK DITLQEVNRV SQVVTSLADP SANIIFGAVV
DDRYTGEIHV TIIATGFSQS FQKTLLTDPR AAKLLDKMGS SGQQENKGMS LPHQKQSPST
ISTKSSSPRR LFF
