TATB_PEA
ID TATB_PEA Reviewed; 261 AA.
AC Q94G16;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Sec-independent protein translocase protein TATB, chloroplastic;
DE AltName: Full=Protein HIGH CHLOROPHYLL FLUORESCENCE 106;
DE AltName: Full=Protein TWIN-ARGININE TRANSLOCATION B;
DE Flags: Precursor;
GN Name=TATB; Synonyms=HCF106;
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].
RX PubMed=11457457; DOI=10.1016/s0014-5793(01)02626-6;
RA Mori H., Summer E.J., Cline K.;
RT "Chloroplast TatC plays a direct role in thylakoid (Delta)pH-dependent
RT protein transport.";
RL FEBS Lett. 501:65-68(2001).
RN [2]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11502764; DOI=10.1083/jcb.200105149;
RA Cline K., Mori H.;
RT "Thylakoid DeltapH-dependent precursor proteins bind to a cpTatC-Hcf106
RT complex before Tha4-dependent transport.";
RL J. Cell Biol. 154:719-729(2001).
RN [3]
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 [4]
RP SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-96.
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=19854178; DOI=10.1016/j.febslet.2009.10.057;
RA Vladimirou E., Li M., Aldridge C.P., Frigerio L., Kirkilionis M.,
RA Robinson C.;
RT "Diffusion of a membrane protein, Tat subunit Hcf106, is highly restricted
RT within the chloroplast thylakoid network.";
RL FEBS Lett. 583:3690-3696(2009).
RN [6]
RP 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:11502764}.
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:11502764, ECO:0000269|PubMed:11956224,
CC ECO:0000269|PubMed:14653819, ECO:0000269|PubMed:22564412}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000305|PubMed:14653819, ECO:0000305|PubMed:19854178}; Single-pass
CC membrane protein {ECO:0000305|PubMed:14653819,
CC ECO:0000305|PubMed:19854178}. Note=The C-terminus is located in the
CC stroma. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TatB family. {ECO:0000305}.
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DR EMBL; AF284760; AAK93949.1; -; mRNA.
DR AlphaFoldDB; Q94G16; -.
DR EnsemblPlants; Psat6g193680.1; Psat6g193680.1.cds; Psat6g193680.
DR Gramene; Psat6g193680.1; Psat6g193680.1.cds; Psat6g193680.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:1902458; P:positive regulation of stomatal opening; IEA:EnsemblPlants.
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 GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:2000070; P:regulation of response to water deprivation; IEA:EnsemblPlants.
DR GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
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..86
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 87..261
FT /note="Sec-independent protein translocase protein TATB,
FT chloroplastic"
FT /id="PRO_0000419915"
FT TOPO_DOM 87..88
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..261
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT REGION 160..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 96
FT /note="E->Q: Loss of protein translocation."
FT /evidence="ECO:0000269|PubMed:14653819"
SQ SEQUENCE 261 AA; 28435 MW; C75558751F5747CA CRC64;
MTPSLAIASS TSTMLLCPKL GTCSMSLSTC TPTSHSKIHH FHLYSLGKRL FTPWNGFKQL
GFSTKPKKPL FHFIGKKGRC KGKVVYASLF GVGAPEALVI GVVALLVFGP KGLAEVARNL
GKTLREFQPT IREIQDVSRE FKSTLEREIG IDDITNPLQS TYSSNVRNTT PTPSATEITN
NSQTAVDPNG KVDESKAYSS EEYLKITEEQ LKAVAAQQQE QTSSPKEDEI EQQIQPPANE
TAATVPPPQK PESESSLPSD L
