TOC33_ARATH
ID TOC33_ARATH Reviewed; 297 AA.
AC O23680; Q94B42; Q9GDD3;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Translocase of chloroplast 33, chloroplastic;
DE Short=AtToc33;
DE EC=3.6.5.-;
DE AltName: Full=33 kDa chloroplast outer envelope protein;
DE AltName: Full=Plastid protein import 1;
GN Name=TOC33; Synonyms=PPI1; OrderedLocusNames=At1g02280; ORFNames=T7I23.11;
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], CHARACTERIZATION, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INTERACTION WITH TOC75.
RC STRAIN=cv. Columbia; TISSUE=Etiolated seedling;
RX PubMed=10998188; DOI=10.1046/j.1365-313x.2000.00849.x;
RA Gutensohn M., Schulz B.I., Nicolay P., Fluegge U.-I.;
RT "Functional analysis of the two Arabidopsis homologues of Toc34, a
RT component of the chloroplast protein import apparatus.";
RL Plant J. 23:771-783(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION.
RX PubMed=11549763; DOI=10.2307/3871427;
RA Sun C.-W., Chen L.-J., Lin L.-C., Li H.-M.;
RT "Leaf-specific upregulation of chloroplast translocon genes by a CCT motif-
RT containing protein, CIA2.";
RL Plant Cell 13:2053-2061(2001).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11553737; DOI=10.1104/pp.127.1.90;
RA Yu T.-S., Li H.-M.;
RT "Chloroplast protein translocon components atToc159 and atToc33 are not
RT essential for chloroplast biogenesis in guard cells and root cells.";
RL Plant Physiol. 127:90-96(2001).
RN [8]
RP INTERACTION WITH TOC159.
RX PubMed=12473690; DOI=10.1083/jcb.200208017;
RA Smith M.D., Hiltbrunner A., Kessler F., Schnell D.J.;
RT "The targeting of the atToc159 preprotein receptor to the chloroplast outer
RT membrane is mediated by its GTPase domain and is regulated by GTP.";
RL J. Cell Biol. 159:833-843(2002).
RN [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION AT SER-181,
RP DIMERIZATION WITH TOC34, AND MUTAGENESIS OF SER-170; SER-175; SER-181;
RP SER-190 AND SER-200.
RX PubMed=12741849; DOI=10.1021/bi034001q;
RA Jelic M., Soll J., Schleiff E.;
RT "Two Toc34 homologues with different properties.";
RL Biochemistry 42:5906-5916(2003).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF GLU-208; ASP-217; ASP-219 AND GLU-220.
RX PubMed=12782294; DOI=10.1016/s0014-5793(03)00478-2;
RA Aronsson H., Combe J., Jarvis P.;
RT "Unusual nucleotide-binding properties of the chloroplast protein import
RT receptor, atToc33.";
RL FEBS Lett. 544:79-85(2003).
RN [11]
RP FUNCTION, DIMERIZATION WITH TOC159, AND MUTAGENESIS OF ARG-130.
RX PubMed=12869544; DOI=10.1074/jbc.m305946200;
RA Weibel P., Hiltbrunner A., Brand L., Kessler F.;
RT "Dimerization of Toc-GTPases at the chloroplast protein import machinery.";
RL J. Biol. Chem. 278:37321-37329(2003).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 45-GLY--SER-50, AND
RP INTERACTION WITH TOC159.
RX PubMed=12951325; DOI=10.1074/jbc.m307873200;
RA Wallas T.R., Smith M.D., Sanchez-Nieto S., Schnell D.J.;
RT "The roles of Toc34 and Toc75 in targeting the Toc159 preprotein receptor
RT to chloroplasts.";
RL J. Biol. Chem. 278:44289-44297(2003).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY LIGHT, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12897258; DOI=10.1105/tpc.012955;
RA Kubis S., Baldwin A., Patel R., Razzaq A., Dupree P., Lilley K., Kurth J.,
RA Leister D., Jarvis P.;
RT "The Arabidopsis ppi1 mutant is specifically defective in the expression,
RT chloroplast import, and accumulation of photosynthetic proteins.";
RL Plant Cell 15:1859-1871(2003).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
RN [15]
RP FUNCTION.
RX PubMed=15053763; DOI=10.1111/j.1365-313x.2004.02024.x;
RA Constan D., Patel R., Keegstra K., Jarvis P.;
RT "An outer envelope membrane component of the plastid protein import
RT apparatus plays an essential role in Arabidopsis.";
RL Plant J. 38:93-106(2004).
RN [16]
RP INTERACTION WITH PPORA AND OP161.
RX PubMed=15773849; DOI=10.1111/j.1365-313x.2005.02353.x;
RA Reinbothe S., Pollmann S., Springer A., James R.J., Tichtinsky G.,
RA Reinbothe C.;
RT "A role of Toc33 in the protochlorophyllide-dependent plastid import
RT pathway of NADPH:protochlorophyllide oxidoreductase (POR) A.";
RL Plant J. 42:1-12(2005).
RN [17]
RP FUNCTION, PHOSPHORYLATION AT SER-181, AND MUTAGENESIS OF SER-181.
RX PubMed=16412428; DOI=10.1016/j.febslet.2005.12.055;
RA Aronsson H., Combe J., Patel R., Jarvis P.;
RT "In vivo assessment of the significance of phosphorylation of the
RT Arabidopsis chloroplast protein import receptor, atToc33.";
RL FEBS Lett. 580:649-655(2006).
RN [18]
RP FUNCTION.
RX PubMed=16435266; DOI=10.1055/s-2005-873044;
RA Hust B., Gutensohn M.;
RT "Deletion of core components of the plastid protein import machinery causes
RT differential arrest of embryo development in Arabidopsis thaliana.";
RL Plant Biol. 8:18-30(2006).
RN [19]
RP FUNCTION, AND PHOSPHORYLATION AT SER-181.
RX PubMed=18054337; DOI=10.1016/j.febslet.2007.11.071;
RA Oreb M., Zoryan M., Vojta A., Maier U.G., Eichacker L.A., Schleiff E.;
RT "Phospho-mimicry mutant of atToc33 affects early development of Arabidopsis
RT thaliana.";
RL FEBS Lett. 581:5945-5951(2007).
RN [20]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17261588; DOI=10.1074/jbc.m609491200;
RA Reddick L.E., Vaughn M.D., Wright S.J., Campbell I.M., Bruce B.D.;
RT "In vitro comparative kinetic analysis of the chloroplast Toc GTPases.";
RL J. Biol. Chem. 282:11410-11426(2007).
RN [21]
RP INTERACTION WITH SP1.
RX PubMed=23118188; DOI=10.1126/science.1225053;
RA Ling Q., Huang W., Baldwin A., Jarvis P.;
RT "Chloroplast biogenesis is regulated by direct action of the ubiquitin-
RT proteasome system.";
RL Science 338:655-659(2012).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 2-250 IN COMPLEX WITH GDP AND
RP MAGNESIUM, DIMERIZATION, AND MUTAGENESIS OF ARG-130.
RX PubMed=17337454; DOI=10.1074/jbc.m608385200;
RA Yeh Y.-H., Kesavulu M.M., Li H.-M., Wu S.-Z., Sun Y.-J., Konozy E.H.E.,
RA Hsiao C.-D.;
RT "Dimerization is important for the GTPase activity of chloroplast
RT translocon components atToc33 and psToc159.";
RL J. Biol. Chem. 282:13845-13853(2007).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 1-251 IN COMPLEX WITH GDP AND
RP MAGNESIUM, DIMERIZATION, AND MUTAGENESIS OF ARG-130.
RX PubMed=18541539; DOI=10.1074/jbc.m710576200;
RA Koenig P., Oreb M., Rippe K., Muhle-Goll C., Sinning I., Schleiff E.,
RA Tews I.;
RT "On the significance of Toc-GTPase homodimers.";
RL J. Biol. Chem. 283:23104-23112(2008).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-251 IN COMPLEX WITH GDP; GNP
RP AND MAGNESIUM, AND DIMERIZATION.
RX PubMed=18400179; DOI=10.1016/j.str.2008.01.008;
RA Koenig P., Oreb M., Hoefle A., Kaltofen S., Rippe K., Sinning I.,
RA Schleiff E., Tews I.;
RT "The GTPase cycle of the chloroplast import receptors Toc33/Toc34:
RT implications from monomeric and dimeric structures.";
RL Structure 16:585-596(2008).
CC -!- FUNCTION: GTPase involved in protein precursor import into
CC chloroplasts. Seems to recognize chloroplast-destined precursor
CC proteins and regulate their presentation to the translocation channel
CC through GTP hydrolysis. Binds GTP, GDP, XTP, but not ATP. Probably
CC specialized in the import of nuclear encoded photosynthetic preproteins
CC from the cytoplasm to the chloroplast, especially during early
CC development stages. {ECO:0000269|PubMed:11553737,
CC ECO:0000269|PubMed:12741849, ECO:0000269|PubMed:12782294,
CC ECO:0000269|PubMed:12869544, ECO:0000269|PubMed:12897258,
CC ECO:0000269|PubMed:12951325, ECO:0000269|PubMed:15053763,
CC ECO:0000269|PubMed:16412428, ECO:0000269|PubMed:16435266,
CC ECO:0000269|PubMed:18054337}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17337454, ECO:0000269|PubMed:18400179,
CC ECO:0000269|PubMed:18541539};
CC Note=Binds 1 Mg(2+) ion by subunit. {ECO:0000269|PubMed:17337454,
CC ECO:0000269|PubMed:18400179, ECO:0000269|PubMed:18541539};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=290 nM for GDP (at pH 7.4) {ECO:0000269|PubMed:12741849,
CC ECO:0000269|PubMed:17261588};
CC KM=5.7 uM for GTP (at pH 7.6 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:12741849, ECO:0000269|PubMed:17261588};
CC Vmax=1040 nmol/min/ug enzyme with GTP as substrate (at pH 7.4)
CC {ECO:0000269|PubMed:12741849, ECO:0000269|PubMed:17261588};
CC -!- SUBUNIT: Homodimer, heterodimer with TOC34 and TOC159, and monomer. The
CC homodimerization and the dimerization with TOC159 require the binding
CC of GTP on Arg-130, and a hypothetical coGAP factor. The dimeric form
CC has a higher GTPase activity than the monomeric form. Part of the TOC
CC core complex that includes 1 protein for the specific recognition of
CC transit peptides surrounded by a ring composed of four proteins forming
CC translocation channels, and four to five GTP-binding proteins providing
CC energy. This core complex can interact with components of the TIC
CC complex to form a larger import complex. Chloroplastic protein
CC precursor such as prSS (precursor of the RuBisCO small subunit)
CC interacts with these complexes. The TOC complex contains a specific
CC subset of polar lipids such as digalactosyldiacylglyceride (DGDG),
CC phosphatidylcholine (PC) and phosphatidylglycerol (PG). Interacts at
CC least with TOC75-3. Forms large complexes including TOC33, pPORA and
CC OEP161 during pPORA import into plastids at the plastid envelope
CC membrane (PubMed:10998188, PubMed:12473690, PubMed:12951325,
CC PubMed:15773849, PubMed:17337454, PubMed:18400179, PubMed:18541539).
CC Interacts with SP1 (PubMed:23118188). {ECO:0000269|PubMed:10998188,
CC ECO:0000269|PubMed:12473690, ECO:0000269|PubMed:12951325,
CC ECO:0000269|PubMed:15773849, ECO:0000269|PubMed:17337454,
CC ECO:0000269|PubMed:18400179, ECO:0000269|PubMed:18541539,
CC ECO:0000269|PubMed:23118188}.
CC -!- INTERACTION:
CC O23680; Q39016: CPK11; NbExp=4; IntAct=EBI-639377, EBI-979321;
CC O23680; Q38869: CPK4; NbExp=5; IntAct=EBI-639377, EBI-979475;
CC O23680; Q8L7N4: SP1; NbExp=2; IntAct=EBI-639377, EBI-6559199;
CC O23680; O23680: TOC33; NbExp=4; IntAct=EBI-639377, EBI-639377;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:10998188, ECO:0000269|PubMed:12766230,
CC ECO:0000269|PubMed:12951325}; Single-pass membrane protein
CC {ECO:0000269|PubMed:10998188, ECO:0000269|PubMed:12766230,
CC ECO:0000269|PubMed:12951325}. Note=May contain beta barrel
CC transmembrane regions.
CC -!- TISSUE SPECIFICITY: Mostly expressed in seedlings and flowers, and, to
CC a lower extent, in roots, stems, and leaves.
CC {ECO:0000269|PubMed:10998188, ECO:0000269|PubMed:12897258}.
CC -!- DEVELOPMENTAL STAGE: Mostly expressed in photosynthetic tissues
CC undergoing rapid growth. Observed in cotyledons and vascular tissues of
CC hypocotyls of young seedling. In roots, restricted to apical and
CC lateral meristems, and vascular bundles. In stems, mostly detected in
CC the upper part. Expressed in young and middle-aged leaves. In flowers,
CC confined to sepals. {ECO:0000269|PubMed:10998188,
CC ECO:0000269|PubMed:12897258}.
CC -!- INDUCTION: Up-regulated by CIA2 in leaves. Induced in light but
CC repressed in darkness. {ECO:0000269|PubMed:11549763,
CC ECO:0000269|PubMed:12897258}.
CC -!- PTM: Phosphorylated by a kinase present in the outer envelope of
CC chloroplast. When Ser-181 is phosphorylated, the binding to preprotein,
CC GTP and GDP is inhibited, and thus, GTPase activity is repressed.
CC {ECO:0000269|PubMed:12741849, ECO:0000269|PubMed:16412428,
CC ECO:0000269|PubMed:18054337}.
CC -!- DISRUPTION PHENOTYPE: Plants exhibits a pale yellowish phenotype.
CC {ECO:0000269|PubMed:10998188, ECO:0000269|PubMed:11553737,
CC ECO:0000269|PubMed:12897258}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family.
CC TOC34 subfamily. {ECO:0000305}.
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DR EMBL; AJ010724; CAC17698.1; -; mRNA.
DR EMBL; U89959; AAC24375.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27409.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27410.1; -; Genomic_DNA.
DR EMBL; AY042869; AAK68809.1; -; mRNA.
DR EMBL; AY056448; AAL08304.1; -; mRNA.
DR EMBL; BT025654; ABF74715.1; -; mRNA.
DR RefSeq; NP_001117215.1; NM_001123743.2.
DR RefSeq; NP_171730.1; NM_100108.5.
DR PDB; 2J3E; X-ray; 3.20 A; A=2-250.
DR PDB; 3BB3; X-ray; 2.94 A; A=1-251.
DR PDB; 3BB4; X-ray; 2.85 A; A=1-251.
DR PDB; 3DEF; X-ray; 1.96 A; A=1-251.
DR PDBsum; 2J3E; -.
DR PDBsum; 3BB3; -.
DR PDBsum; 3BB4; -.
DR PDBsum; 3DEF; -.
DR AlphaFoldDB; O23680; -.
DR SMR; O23680; -.
DR BioGRID; 24483; 8.
DR IntAct; O23680; 8.
DR STRING; 3702.AT1G02280.1; -.
DR iPTMnet; O23680; -.
DR PaxDb; O23680; -.
DR PRIDE; O23680; -.
DR ProteomicsDB; 234323; -.
DR DNASU; 839248; -.
DR EnsemblPlants; AT1G02280.1; AT1G02280.1; AT1G02280.
DR EnsemblPlants; AT1G02280.2; AT1G02280.2; AT1G02280.
DR GeneID; 839248; -.
DR Gramene; AT1G02280.1; AT1G02280.1; AT1G02280.
DR Gramene; AT1G02280.2; AT1G02280.2; AT1G02280.
DR KEGG; ath:AT1G02280; -.
DR Araport; AT1G02280; -.
DR TAIR; locus:2204923; AT1G02280.
DR eggNOG; ENOG502QSV2; Eukaryota.
DR HOGENOM; CLU_051932_0_0_1; -.
DR InParanoid; O23680; -.
DR OMA; HEIQDHA; -.
DR OrthoDB; 1108753at2759; -.
DR PhylomeDB; O23680; -.
DR BioCyc; ARA:AT1G02280-MON; -.
DR BRENDA; 3.6.5.2; 399.
DR EvolutionaryTrace; O23680; -.
DR PRO; PR:O23680; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O23680; baseline and differential.
DR Genevisible; O23680; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IDA:TAIR.
DR GO; GO:0003924; F:GTPase activity; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:TAIR.
DR GO; GO:0015450; F:protein-transporting ATPase activity; IEA:InterPro.
DR GO; GO:0045036; P:protein targeting to chloroplast; TAS:TAIR.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006703; G_AIG1.
DR InterPro; IPR045058; GIMA/IAN/Toc.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005688; Toc34.
DR PANTHER; PTHR10903; PTHR10903; 1.
DR Pfam; PF04548; AIG1; 1.
DR PIRSF; PIRSF038134; Toc34; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00991; 3a0901s02IAP34; 1.
DR PROSITE; PS51720; G_AIG1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; GTP-binding; Hydrolase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Plastid;
KW Plastid outer membrane; Protein transport; Receptor; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..297
FT /note="Translocase of chloroplast 33, chloroplastic"
FT /id="PRO_0000352655"
FT TRANSMEM 37..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 34..258
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 65..68
FT /note="Homodimerization"
FT /evidence="ECO:0000305|PubMed:18400179"
FT REGION 125..130
FT /note="Homodimerization"
FT /evidence="ECO:0000305|PubMed:18400179"
FT BINDING 46..51
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:18400179,
FT ECO:0007744|PDB:3BB4"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17337454,
FT ECO:0000269|PubMed:18400179, ECO:0000269|PubMed:18541539"
FT BINDING 65..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:18400179"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17337454,
FT ECO:0000269|PubMed:18400179, ECO:0000269|PubMed:18541539"
FT BINDING 160
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:18400179,
FT ECO:0007744|PDB:3BB4"
FT BINDING 208..209
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:18400179,
FT ECO:0007744|PDB:3BB4"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12741849,
FT ECO:0000269|PubMed:16412428, ECO:0000269|PubMed:18054337"
FT MUTAGEN 45..50
FT /note="GGVGKS->RGVGNR: Reduced GTPase activity and impaired
FT interaction with TOC159."
FT /evidence="ECO:0000269|PubMed:12951325"
FT MUTAGEN 130
FT /note="R->A: Loss of homidimerization and
FT heterodimerization with TOC159, reduction of GTPase
FT activity."
FT /evidence="ECO:0000269|PubMed:12869544,
FT ECO:0000269|PubMed:17337454, ECO:0000269|PubMed:18541539"
FT MUTAGEN 170
FT /note="S->A: Normal phosphorylation."
FT /evidence="ECO:0000269|PubMed:12741849"
FT MUTAGEN 175
FT /note="S->A: Normal phosphorylation."
FT /evidence="ECO:0000269|PubMed:12741849"
FT MUTAGEN 181
FT /note="S->A: Loss of phosphorylation, normal activity."
FT /evidence="ECO:0000269|PubMed:12741849,
FT ECO:0000269|PubMed:16412428"
FT MUTAGEN 181
FT /note="S->D,E: According to PubMed:16412428, supposed to
FT mimic the effects of phosphoserine, but normal activity."
FT /evidence="ECO:0000269|PubMed:12741849,
FT ECO:0000269|PubMed:16412428"
FT MUTAGEN 181
FT /note="S->T: Phosphothreonine instead of phosphoserine."
FT /evidence="ECO:0000269|PubMed:12741849,
FT ECO:0000269|PubMed:16412428"
FT MUTAGEN 190
FT /note="S->A: Normal phosphorylation."
FT /evidence="ECO:0000269|PubMed:12741849"
FT MUTAGEN 200
FT /note="S->A: Normal phosphorylation."
FT /evidence="ECO:0000269|PubMed:12741849"
FT MUTAGEN 208
FT /note="E->Q: Normal GTPase activity, but weaker nucleotide
FT binding."
FT /evidence="ECO:0000269|PubMed:12782294"
FT MUTAGEN 217
FT /note="D->N: Normal GTPase activity."
FT /evidence="ECO:0000269|PubMed:12782294"
FT MUTAGEN 219
FT /note="D->N: Normal GTPase activity."
FT /evidence="ECO:0000269|PubMed:12782294"
FT MUTAGEN 220
FT /note="E->Q: Normal GTPase activity."
FT /evidence="ECO:0000269|PubMed:12782294"
FT CONFLICT 147
FT /note="G -> A (in Ref. 4; AAK68809)"
FT /evidence="ECO:0000305"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:3DEF"
FT HELIX 16..31
FT /evidence="ECO:0007829|PDB:3DEF"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:3DEF"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:3DEF"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2J3E"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:3DEF"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:3DEF"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3DEF"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:2J3E"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:3DEF"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3DEF"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:3DEF"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:3DEF"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:3DEF"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:3DEF"
FT HELIX 171..190
FT /evidence="ECO:0007829|PDB:3DEF"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:2J3E"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:3DEF"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:3DEF"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:2J3E"
FT HELIX 229..241
FT /evidence="ECO:0007829|PDB:3DEF"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:3BB4"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:3BB3"
SQ SEQUENCE 297 AA; 32925 MW; E48892E123BA412D CRC64;
MGSLVREWVG FQQFPAATQE KLIEFFGKLK QKDMNSMTVL VLGKGGVGKS STVNSLIGEQ
VVRVSPFQAE GLRPVMVSRT MGGFTINIID TPGLVEAGYV NHQALELIKG FLVNRTIDVL
LYVDRLDVYR VDELDKQVVI AITQTFGKEI WCKTLLVLTH AQFSPPDELS YETFSSKRSD
SLLKTIRAGS KMRKQEFEDS AIAVVYAENS GRCSKNDKDE KALPNGEAWI PNLVKAITDV
ATNQRKAIHV DKKMVDGSYS DDKGKKLIPL IIGAQYLIVK MIQGAIRNDI KTSGKPL
