TATA_PEA
ID TATA_PEA Reviewed; 137 AA.
AC Q9XH46;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Sec-independent protein translocase protein TATA, chloroplastic;
DE AltName: Full=Protein THYLAKOID ASSEMBLY 4;
DE AltName: Full=Protein TWIN-ARGININE TRANSLOCATION A;
DE Flags: Precursor;
GN Name=TATA; Synonyms=THA4;
OS Pisum sativum (Garden pea).
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10402459; DOI=10.1083/jcb.146.1.45;
RA Mori M., Summer E.J., Ma X., Cline K.;
RT "Component specificity for the thylakoidal Sec and Delta pH-dependent
RT protein transport pathways.";
RL J. Cell Biol. 146:45-56(1999).
RN [2]
RP SUBUNIT.
RX PubMed=11956224; DOI=10.1083/jcb.200202048;
RA Mori H., Cline K.;
RT "A twin arginine signal peptide and the pH gradient trigger reversible
RT assembly of the thylakoid [Delta]pH/Tat translocase.";
RL J. Cell Biol. 157:205-210(2002).
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-65.
RX PubMed=14653819; DOI=10.1046/j.1432-1033.2003.03894.x;
RA Fincher V., Dabney-Smith C., Cline K.;
RT "Functional assembly of thylakoid deltapH-dependent/Tat protein transport
RT pathway components in vitro.";
RL Eur. J. Biochem. 270:4930-4941(2003).
RN [4]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-65 AND LEU-75.
RX PubMed=12941940; DOI=10.1074/jbc.m307923200;
RA Dabney-Smith C., Mori H., Cline K.;
RT "Requirement of a Tha4-conserved transmembrane glutamate in thylakoid Tat
RT translocase assembly revealed by biochemical complementation.";
RL J. Biol. Chem. 278:43027-43033(2003).
RN [5]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-65.
RX PubMed=16407186; DOI=10.1074/jbc.m512453200;
RA Dabney-Smith C., Mori H., Cline K.;
RT "Oligomers of Tha4 organize at the thylakoid Tat translocase during protein
RT transport.";
RL J. Biol. Chem. 281:5476-5483(2006).
RN [6]
RP FUNCTION.
RX PubMed=18842584; DOI=10.1074/jbc.m806334200;
RA Frielingsdorf S., Jakob M., Kloesgen R.B.;
RT "A stromal pool of TatA promotes Tat-dependent protein transport across the
RT thylakoid membrane.";
RL J. Biol. Chem. 283:33838-33845(2008).
RN [7]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLY-60; GLY-62 AND PRO-64.
RX PubMed=19193764; DOI=10.1091/mbc.e08-12-1189;
RA Dabney-Smith C., Cline K.;
RT "Clustering of C-terminal stromal domains of Tha4 homo-oligomers during
RT translocation by the Tat protein transport system.";
RL Mol. Biol. Cell 20:2060-2069(2009).
RN [8]
RP FUNCTION, AND TOPOLOGY.
RX PubMed=22896708; DOI=10.1074/jbc.m112.385666;
RA Aldridge C., Storm A., Cline K., Dabney-Smith C.;
RT "The chloroplast twin arginine transport (Tat) component, Tha4, undergoes
RT conformational changes leading to Tat protein transport.";
RL J. Biol. Chem. 287:34752-34763(2012).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=22564412; DOI=10.1083/jcb.201201096;
RA Celedon J.M., Cline K.;
RT "Stoichiometry for binding and transport by the twin arginine translocation
RT system.";
RL J. Cell Biol. 197:523-534(2012).
CC -!- FUNCTION: Part of the twin-arginine translocation (Tat) system that
CC transports large folded proteins containing a characteristic twin-
CC arginine motif in their signal peptide across the thylakoid membrane.
CC Involved in delta pH-dependent protein transport required for
CC chloroplast development, especially thylakoid membrane formation. TATC
CC and TATB mediate precursor recognition, whereas TATA facilitates
CC translocation. {ECO:0000269|PubMed:10402459,
CC ECO:0000269|PubMed:12941940, ECO:0000269|PubMed:14653819,
CC ECO:0000269|PubMed:16407186, ECO:0000269|PubMed:18842584,
CC ECO:0000269|PubMed:19193764, ECO:0000269|PubMed:22564412,
CC ECO:0000269|PubMed:22896708}.
CC -!- SUBUNIT: In thylakoid membranes, TATC and TATB form a large receptor
CC complex, containing about eight TATC-TATB pairs, which binds the
CC precursor protein. Twin arginine signal peptide promotes pH-triggered
CC docking of TATA oligomers to TATC-TATB receptor complex, inducing a
CC conformational switch of TATA that results in activation of the
CC translocase. TATA dissociates from TATC-TATB upon completion of
CC translocation. According to PubMed:22564412, it is estimated that the
CC translocase fully saturated with precursor proteins and TATA is an 2.2-
CC megadalton complex that can individually transport eight precursor
CC proteins or cooperatively transport multimeric precursors.
CC {ECO:0000269|PubMed:11956224, ECO:0000269|PubMed:12941940,
CC ECO:0000269|PubMed:14653819, ECO:0000269|PubMed:16407186,
CC ECO:0000269|PubMed:19193764, ECO:0000269|PubMed:22564412}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000305|PubMed:10402459, ECO:0000305|PubMed:14653819}; Single-pass
CC membrane protein {ECO:0000305|PubMed:10402459,
CC ECO:0000305|PubMed:14653819}. Note=The C-terminus is located in the
CC stroma.
CC -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000305}.
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DR EMBL; AF144708; AAD33943.1; -; mRNA.
DR AlphaFoldDB; Q9XH46; -.
DR SMR; Q9XH46; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0031361; C:integral component of thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0033281; C:TAT protein transport complex; IDA:UniProtKB.
DR GO; GO:0009977; F:proton motive force dependent protein transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0045038; P:protein import into chloroplast thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0043953; P:protein transport by the Tat complex; IDA:UniProtKB.
DR HAMAP; MF_00236; TatA_E; 1.
DR InterPro; IPR003369; TatA/B/E.
DR InterPro; IPR006312; TatA/E.
DR Pfam; PF02416; TatA_B_E; 1.
DR TIGRFAMs; TIGR01411; tatAE; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Plastid; Protein transport; Thylakoid;
KW Transit peptide; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 55..137
FT /note="Sec-independent protein translocase protein TATA,
FT chloroplastic"
FT /id="PRO_0000419919"
FT TOPO_DOM 55..56
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..137
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT REGION 104..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 60
FT /note="G->C: Loss of protein translocation; when associated
FT with C-64."
FT /evidence="ECO:0000269|PubMed:19193764"
FT MUTAGEN 62
FT /note="G->C: Loss of protein translocation; when associated
FT with C-64."
FT /evidence="ECO:0000269|PubMed:19193764"
FT MUTAGEN 64
FT /note="P->C: Loss of protein translocation; when associated
FT with C-60 or C-62."
FT /evidence="ECO:0000269|PubMed:19193764"
FT MUTAGEN 65
FT /note="E->A,D,Q: Loss of protein translocation."
FT /evidence="ECO:0000269|PubMed:12941940,
FT ECO:0000269|PubMed:14653819, ECO:0000269|PubMed:16407186"
FT MUTAGEN 75
FT /note="L->I: No effect on protein translocation."
FT /evidence="ECO:0000269|PubMed:12941940"
SQ SEQUENCE 137 AA; 14799 MW; 9184B27508DB7066 CRC64;
MEITLSISSS SVIPTRLPNS SCYSNLSFLS SNSNTSSLLL KKARIKTRTT KGFTCNAFFG
LGVPELVVIA GVAALVFGPK KLPEVGRSIG QTVKSFQQAA KEFETELKKE PNPTEEISVA
SEQEKQEIKV SSTKDNV
