TOC34_PEA
ID TOC34_PEA Reviewed; 310 AA.
AC Q41009; Q41029;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Translocase of chloroplast 34;
DE EC=3.6.5.-;
DE AltName: Full=34 kDa chloroplast outer envelope protein;
DE AltName: Full=GTP-binding protein IAP34;
DE AltName: Full=GTP-binding protein OEP34;
GN Name=TOC34; Synonyms=IAP34, OEP34;
OS Pisum sativum (Garden pea).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Miranda; TISSUE=Leaf;
RX PubMed=7757113; DOI=10.1046/j.1365-313x.1995.7030401.x;
RA Seedorf M., Waegemann K., Soll J.;
RT "A constituent of the chloroplast import complex represents a new type of
RT GTP-binding protein.";
RL Plant J. 7:401-411(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 119-139 AND 157-180.
RX PubMed=7973656; DOI=10.1126/science.7973656;
RA Kessler F., Blobel G., Patel H.V., Schnell D.J.;
RT "Identification of two GTP-binding proteins in the chloroplast protein
RT import machinery.";
RL Science 266:1035-1039(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-258 IN COMPLEX WITH GTP,
RP HOMODIMERIZATION, AND MUTAGENESIS OF ARG-128.
RX PubMed=11753431; DOI=10.1038/nsb744;
RA Sun Y.-J., Forouhar F., Li Hm H.-M., Tu S.-L., Yeh Y.-H., Kao S.,
RA Shr H.-L., Chou C.-C., Chen C., Hsiao C.-D.;
RT "Crystal structure of pea Toc34, a novel GTPase of the chloroplast protein
RT translocon.";
RL Nat. Struct. Biol. 9:95-100(2002).
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.
CC -!- SUBUNIT: Homodimer and monomer. Part of the TOC core complex that
CC includes a protein for the specific recognition of transit peptides
CC surrounded by a ring composed of four proteins forming translocation
CC channels, and four to five GTP-binding proteins providing energy. This
CC core complex can interact with components of the TIC complex to form a
CC larger import complex. Chloroplastic protein precursor such as prSS
CC (precursor of the RuBisCO small subunit) interacts with these
CC complexes. The TOC complex contains a specific subset of polar lipids
CC such as digalactosyldiacylglyceride (DGDG), phosphatidylcholine (PC)
CC and phosphatidylglycerol (PG). TOC34 interacts at least with TOC75.
CC {ECO:0000269|PubMed:11753431}.
CC -!- INTERACTION:
CC Q41009; Q41009: TOC34; NbExp=5; IntAct=EBI-638506, EBI-638506;
CC Q41009; Q9MUK5: TOC64; NbExp=6; IntAct=EBI-638506, EBI-638487;
CC Q41009; P48347: GRF10; Xeno; NbExp=2; IntAct=EBI-638506, EBI-1803304;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane.
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; Z28341; CAA82196.1; -; mRNA.
DR EMBL; L36856; AAC25785.1; -; mRNA.
DR PIR; B55171; B55171.
DR PDB; 1H65; X-ray; 2.00 A; A/B/C=1-258.
DR PDB; 3BB1; X-ray; 2.80 A; A/B/C/D/E/F/G/H=1-266.
DR PDBsum; 1H65; -.
DR PDBsum; 3BB1; -.
DR AlphaFoldDB; Q41009; -.
DR SMR; Q41009; -.
DR DIP; DIP-332N; -.
DR IntAct; Q41009; 9.
DR MINT; Q41009; -.
DR TCDB; 3.A.9.1.1; the chloroplast envelope protein translocase (cept or tic-toc) family.
DR EnsemblPlants; Psat3g083600.1; Psat3g083600.1.cds; Psat3g083600.
DR Gramene; Psat3g083600.1; Psat3g083600.1.cds; Psat3g083600.
DR BRENDA; 3.6.5.2; 4872.
DR EvolutionaryTrace; Q41009; -.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015450; F:protein-transporting ATPase activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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; Direct protein sequencing; GTP-binding;
KW Hydrolase; Membrane; Nucleotide-binding; Plastid; Plastid outer membrane;
KW Protein transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..310
FT /note="Translocase of chloroplast 34"
FT /id="PRO_0000144793"
FT TOPO_DOM 1..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..310
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 37..260
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 46..53
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 68..71
FT /note="Homodimerization"
FT REGION 72..76
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 93..96
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 128..133
FT /note="Homodimerization"
FT REGION 162..165
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 210..212
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT BINDING 49..54
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11753431"
FT BINDING 73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11753431"
FT BINDING 210..211
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11753431"
FT MUTAGEN 128
FT /note="R->A: No dimerization and reduced GTPase activity."
FT /evidence="ECO:0000269|PubMed:11753431"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:1H65"
FT HELIX 19..34
FT /evidence="ECO:0007829|PDB:1H65"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:1H65"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:1H65"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1H65"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:1H65"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:1H65"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1H65"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:1H65"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1H65"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:1H65"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:1H65"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:1H65"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:1H65"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1H65"
FT HELIX 174..192
FT /evidence="ECO:0007829|PDB:1H65"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:1H65"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1H65"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:1H65"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1H65"
FT HELIX 254..258
FT /evidence="ECO:0007829|PDB:1H65"
SQ SEQUENCE 310 AA; 34157 MW; 00D5E79735BF041F CRC64;
MASQQQTVRE WSGINTFAPA TQTKLLELLG NLKQEDVNSL TILVMGKGGV GKSSTVNSII
GERVVSISPF QSEGPRPVMV SRSRAGFTLN IIDTPGLIEG GYINDMALNI IKSFLLDKTI
DVLLYVDRLD AYRVDNLDKL VAKAITDSFG KGIWNKAIVA LTHAQFSPPD GLPYDEFFSK
RSEALLQVVR SGASLKKDAQ ASDIPVVLIE NSGRCNKNDS DEKVLPNGIA WIPHLVQTIT
EVALNKSESI FVDKNLIDGP NPNQRGKLWI PLIFALQYLF LAKPIEALIR RDIATETKPA
WETRDVGDRK
