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Sec-independent protein translocase protein TATA, chloroplastic (Protein THYLAKOID ASSEMBLY 4) (Protein TWIN-ARGININE TRANSLOCATION A)

 TATA_PEA                Reviewed;         137 AA.
Q9XH46;
31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
15-MAR-2017, entry version 51.
RecName: Full=Sec-independent protein translocase protein TATA, chloroplastic;
AltName: Full=Protein THYLAKOID ASSEMBLY 4;
AltName: Full=Protein TWIN-ARGININE TRANSLOCATION A;
Flags: Precursor;
Name=TATA; Synonyms=THA4;
Pisum sativum (Garden pea).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Fabeae; Pisum.
NCBI_TaxID=3888;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10402459; DOI=10.1083/jcb.146.1.45;
Mori M., Summer E.J., Ma X., Cline K.;
"Component specificity for the thylakoidal Sec and Delta pH-dependent
protein transport pathways.";
J. Cell Biol. 146:45-56(1999).
[2]
SUBUNIT.
PubMed=11956224; DOI=10.1083/jcb.200202048;
Mori H., Cline K.;
"A twin arginine signal peptide and the pH gradient trigger reversible
assembly of the thylakoid [Delta]pH/Tat translocase.";
J. Cell Biol. 157:205-210(2002).
[3]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-65.
PubMed=14653819; DOI=10.1046/j.1432-1033.2003.03894.x;
Fincher V., Dabney-Smith C., Cline K.;
"Functional assembly of thylakoid deltapH-dependent/Tat protein
transport pathway components in vitro.";
Eur. J. Biochem. 270:4930-4941(2003).
[4]
FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-65 AND LEU-75.
PubMed=12941940; DOI=10.1074/jbc.M307923200;
Dabney-Smith C., Mori H., Cline K.;
"Requirement of a Tha4-conserved transmembrane glutamate in thylakoid
Tat translocase assembly revealed by biochemical complementation.";
J. Biol. Chem. 278:43027-43033(2003).
[5]
FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-65.
PubMed=16407186; DOI=10.1074/jbc.M512453200;
Dabney-Smith C., Mori H., Cline K.;
"Oligomers of Tha4 organize at the thylakoid Tat translocase during
protein transport.";
J. Biol. Chem. 281:5476-5483(2006).
[6]
FUNCTION.
PubMed=18842584; DOI=10.1074/jbc.M806334200;
Frielingsdorf S., Jakob M., Kloesgen R.B.;
"A stromal pool of TatA promotes Tat-dependent protein transport
across the thylakoid membrane.";
J. Biol. Chem. 283:33838-33845(2008).
[7]
FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLY-60; GLY-62 AND PRO-64.
PubMed=19193764; DOI=10.1091/mbc.E08-12-1189;
Dabney-Smith C., Cline K.;
"Clustering of C-terminal stromal domains of Tha4 homo-oligomers
during translocation by the Tat protein transport system.";
Mol. Biol. Cell 20:2060-2069(2009).
[8]
FUNCTION, AND TOPOLOGY.
PubMed=22896708; DOI=10.1074/jbc.M112.385666;
Aldridge C., Storm A., Cline K., Dabney-Smith C.;
"The chloroplast twin arginine transport (Tat) component, Tha4,
undergoes conformational changes leading to Tat protein transport.";
J. Biol. Chem. 287:34752-34763(2012).
[9]
FUNCTION, AND SUBUNIT.
PubMed=22564412; DOI=10.1083/jcb.201201096;
Celedon J.M., Cline K.;
"Stoichiometry for binding and transport by the twin arginine
translocation system.";
J. Cell Biol. 197:523-534(2012).
-!- FUNCTION: Part of the twin-arginine translocation (Tat) system
that transports large folded proteins containing a characteristic
twin-arginine motif in their signal peptide across the thylakoid
membrane. Involved in delta pH-dependent protein transport
required for chloroplast development, especially thylakoid
membrane formation. TATC and TATB mediate precursor recognition,
whereas TATA facilitates translocation.
{ECO:0000269|PubMed:10402459, ECO:0000269|PubMed:12941940,
ECO:0000269|PubMed:14653819, ECO:0000269|PubMed:16407186,
ECO:0000269|PubMed:18842584, ECO:0000269|PubMed:19193764,
ECO:0000269|PubMed:22564412, ECO:0000269|PubMed:22896708}.
-!- SUBUNIT: In thylakoid membranes, TATC and TATB form a large
receptor complex, containing about eight TATC-TATB pairs, which
binds the precursor protein. Twin arginine signal peptide promotes
pH-triggered docking of TATA oligomers to TATC-TATB receptor
complex, inducing a conformational switch of TATA that results in
activation of the translocase. TATA dissociates from TATC-TATB
upon completion of translocation. According to PubMed:22564412, it
is estimated that the translocase fully saturated with precursor
proteins and TATA is an 2.2-megadalton complex that can
individually transport eight precursor proteins or cooperatively
transport multimeric precursors. {ECO:0000269|PubMed:11956224,
ECO:0000269|PubMed:12941940, ECO:0000269|PubMed:14653819,
ECO:0000269|PubMed:16407186, ECO:0000269|PubMed:19193764,
ECO:0000269|PubMed:22564412}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
{ECO:0000305|PubMed:10402459, ECO:0000305|PubMed:14653819};
Single-pass membrane protein {ECO:0000305|PubMed:10402459,
ECO:0000305|PubMed:14653819}. Note=The C-terminus is located in
the stroma.
-!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF144708; AAD33943.1; -; mRNA.
SMR; Q9XH46; -.
GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
GO; GO:0031361; C:integral component of thylakoid membrane; IDA:UniProtKB.
GO; GO:0033281; C:TAT protein transport complex; IDA:UniProtKB.
GO; GO:0009977; F:proton motive force dependent protein transmembrane transporter activity; IMP:UniProtKB.
GO; GO:0045038; P:protein import into chloroplast thylakoid membrane; IDA:UniProtKB.
GO; GO:0009306; P:protein secretion; IEA:InterPro.
GO; GO:0043953; P:protein transport by the Tat complex; IDA:UniProtKB.
HAMAP; MF_00236; TatA_E; 1.
InterPro; IPR003369; TatA/B/E.
InterPro; IPR006312; TatA/E.
InterPro; IPR003998; TatB-like.
Pfam; PF02416; MttA_Hcf106; 1.
PRINTS; PR01506; TATBPROTEIN.
TIGRFAMs; TIGR01411; tatAE; 1.
1: Evidence at protein level;
Chloroplast; Membrane; Plastid; Protein transport; Thylakoid;
Transit peptide; Translocation; Transmembrane; Transmembrane helix;
Transport.
TRANSIT 1 54 Chloroplast. {ECO:0000255}.
CHAIN 55 137 Sec-independent protein translocase
protein TATA, chloroplastic.
/FTId=PRO_0000419919.
TOPO_DOM 55 56 Lumenal. {ECO:0000255}.
TRANSMEM 57 77 Helical. {ECO:0000255}.
TOPO_DOM 78 137 Stromal. {ECO:0000255}.
MUTAGEN 60 60 G->C: Loss of protein translocation; when
associated with C-64.
{ECO:0000269|PubMed:19193764}.
MUTAGEN 62 62 G->C: Loss of protein translocation; when
associated with C-64.
{ECO:0000269|PubMed:19193764}.
MUTAGEN 64 64 P->C: Loss of protein translocation; when
associated with C-60 or C-62.
{ECO:0000269|PubMed:19193764}.
MUTAGEN 65 65 E->A,D,Q: Loss of protein translocation.
{ECO:0000269|PubMed:12941940,
ECO:0000269|PubMed:14653819,
ECO:0000269|PubMed:16407186}.
MUTAGEN 75 75 L->I: No effect on protein translocation.
{ECO:0000269|PubMed:12941940}.
SEQUENCE 137 AA; 14799 MW; 9184B27508DB7066 CRC64;
MEITLSISSS SVIPTRLPNS SCYSNLSFLS SNSNTSSLLL KKARIKTRTT KGFTCNAFFG
LGVPELVVIA GVAALVFGPK KLPEVGRSIG QTVKSFQQAA KEFETELKKE PNPTEEISVA
SEQEKQEIKV SSTKDNV


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