ID   TOC64_PEA               Reviewed;         593 AA.
AC   Q9MUK5;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Translocon at the outer membrane of chloroplasts 64;
GN   Name=TOC64;
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], PROTEIN SEQUENCE OF 1-30; 118-140; 273-282;
RP   327-332; 345-354; 451-456; 474-481; 564-567 AND 580-590, FUNCTION,
RP   INTERACTION WITH TOC COMPLEX, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=10725334; DOI=10.1083/jcb.148.6.1213;
RA   Sohrt K., Soll J.;
RT   "Toc64, a new component of the protein translocon of chloroplasts.";
RL   J. Cell Biol. 148:1213-1221(2000).
RN   [2]
RP   INTERACTION WITH TOC12.
RX   PubMed=15317846; DOI=10.1091/mbc.e04-05-0405;
RA   Becker T., Hritz J., Vogel M., Caliebe A., Bukau B., Soll J., Schleiff E.;
RT   "Toc12, a novel subunit of the intermembrane space preprotein translocon of
RT   chloroplasts.";
RL   Mol. Biol. Cell 15:5130-5144(2004).
RN   [3]
RP   FUNCTION, MUTAGENESIS OF ASN-516 AND ARG-550, AND INTERACTION WITH HSP90;
RP   HSP70 AND TOC34.
RX   PubMed=16619024; DOI=10.1038/sj.emboj.7601091;
RA   Qbadou S., Becker T., Mirus O., Tews I., Soll J., Schleiff E.;
RT   "The molecular chaperone Hsp90 delivers precursor proteins to the
RT   chloroplast import receptor Toc64.";
RL   EMBO J. 25:1836-1847(2006).
RN   [4]
RP   FUNCTION, TOPOLOGY, AND INTERACTION WITH TIC22.
RX   PubMed=17306301; DOI=10.1016/j.jmb.2007.01.047;
RA   Qbadou S., Becker T., Bionda T., Reger K., Ruprecht M., Soll J.,
RA   Schleiff E.;
RT   "Toc64--a preprotein-receptor at the outer membrane with bipartide
RT   function.";
RL   J. Mol. Biol. 367:1330-1346(2007).
RN   [5]
RP   3D-STRUCTURE MODELING.
RX   PubMed=19198901; DOI=10.1007/s00894-008-0449-y;
RA   Mirus O., Bionda T., von Haeseler A., Schleiff E.;
RT   "Evolutionarily evolved discriminators in the 3-TPR domain of the Toc64
RT   family involved in protein translocation at the outer membrane of
RT   chloroplasts and mitochondria.";
RL   J. Mol. Model. 15:971-982(2009).
CC   -!- FUNCTION: Chaperone receptor mediating Hsp90-dependent protein
CC       targeting to chloroplasts. Bi-functional preprotein receptor acting on
CC       both sides of the membrane. {ECO:0000269|PubMed:10725334,
CC       ECO:0000269|PubMed:16619024, ECO:0000269|PubMed:17306301}.
CC   -!- SUBUNIT: Part of the Toc complex and of the intermembrane space
CC       complex. Interacts with TOC12, TIC22 and with the cytosolic domain of
CC       TOC34 in a GTP dependent manner. Interacts (via TPR region) with HSP90
CC       and with HSP70 with low efficiency. {ECO:0000269|PubMed:10725334,
CC       ECO:0000269|PubMed:15317846, ECO:0000269|PubMed:16619024,
CC       ECO:0000269|PubMed:17306301}.
CC   -!- INTERACTION:
CC       Q9MUK5; Q41009: TOC34; NbExp=6; IntAct=EBI-638487, EBI-638506;
CC       Q9MUK5; Q43715: TOC75; NbExp=2; IntAct=EBI-638487, EBI-638469;
CC       Q9MUK5; Q9LKR1; NbExp=4; IntAct=EBI-638487, EBI-638531;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- DOMAIN: The TPR region (477-578) is not required for assembly into the
CC       Toc complex, but interacts with TOC34 only while transferring the
CC       preprotein from HSP90 to the Toc core translocon.
CC   -!- DOMAIN: The amidase region (166-200) is required for the efficient
CC       transfer of the preprotein.
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DR   EMBL; AF179282; AAF62870.1; -; mRNA.
DR   AlphaFoldDB; Q9MUK5; -.
DR   SMR; Q9MUK5; -.
DR   IntAct; Q9MUK5; 14.
DR   MINT; Q9MUK5; -.
DR   TCDB; 3.A.9.1.1; the chloroplast envelope protein translocase (cept or tic-toc) family.
DR   EnsemblPlants; Psat4g001480.1; Psat4g001480.1.cds; Psat4g001480.
DR   Gramene; Psat4g001480.1; Psat4g001480.1.cds; Psat4g001480.
DR   GO; GO:0031359; C:integral component of chloroplast outer membrane; IEA:EnsemblPlants.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR013105; TPR_2.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF01425; Amidase; 2.
DR   Pfam; PF07719; TPR_2; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Membrane; Plastid;
KW   Plastid outer membrane; Protein transport; Repeat; TPR repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..593
FT                   /note="Translocon at the outer membrane of chloroplasts 64"
FT                   /id="PRO_0000414023"
FT   TOPO_DOM        1..4
FT                   /note="Chloroplast intermembrane"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..144
FT                   /note="Cytoplasmic"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        166..403
FT                   /note="Chloroplast intermembrane"
FT   TRANSMEM        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        425..593
FT                   /note="Cytoplasmic"
FT   REPEAT          477..510
FT                   /note="TPR 1"
FT   REPEAT          511..544
FT                   /note="TPR 2"
FT   REPEAT          545..578
FT                   /note="TPR 3"
FT   MUTAGEN         516
FT                   /note="N->A: Loss of HSP90 binding, but no effect on HSP70
FT                   binding."
FT                   /evidence="ECO:0000269|PubMed:16619024"
FT   MUTAGEN         550
FT                   /note="R->A: 80% decrease of HSP70 and HSP90 binding."
FT                   /evidence="ECO:0000269|PubMed:16619024"
SQ   SEQUENCE   593 AA;  64498 MW;  084E16C7E54E663B CRC64;
     MKSMASPSSQ IWVILGLGLA GIYVLTRKLT QAVKEDFGAF LLKLKLLPPP PPAPPKAPHP
     LSSLNFAISD IFDIEGHVST FGHPEWARTH EPASSTASAV SALVESGATC IGTTVVDELA
     YGISGENKHF GTPTNPAVPN RVPGGSSSGA AVAVAANFVD FSLGVDTSGG VRVPAGFCGI
     LGFRPSHGAV SHVGIIPVST SLDTVGWFAK DPDVLRRVGH ILLQAPFVMQ RNPRQIIIAD
     DCFQHLNVPL DRTSQVVIKA TEKLFGKQVL KHINFEDYIS SKVSSLKACS IQKSNGVLKS
     SSLKLLANVM QSLQRHEFEH THSEWMSIVK PDLHPAVSAQ LHEKFEVSEL EIENSKSVRS
     ELRVAVNSLL KDEGVLVIPT VADPPPKLGG KEFLSHDYQS RALSLLSIAS ISGCCQVTVP
     LGFFDKNPVS VSLIARHGGD RFLLDTLKTM YTVLQEQADI AAPSKSSKSV VSKEQSAEIS
     KEKGNQAYKD KQWQKAIGFY TEAIKLCGNN ATYYSNRAQA YLELGSYLQA EEDCTTAISF
     DKKNVKAYFR RGTAREMLGY YKEAIDDFKY ALVLEPTNKR AASSAERLRK LFQ