TATC_PEA
ID TATC_PEA Reviewed; 353 AA.
AC Q94G17;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Sec-independent protein translocase protein TATC, chloroplastic;
DE AltName: Full=Protein TWIN-ARGININE TRANSLOCATION C;
DE Short=cpTatC;
DE Flags: Precursor;
GN Name=TATC;
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, SUBCELLULAR LOCATION, AND TOPOLOGY.
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, AND SUBCELLULAR LOCATION.
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 FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=19207210; DOI=10.1111/j.1365-313x.2009.03816.x;
RA Martin J.R., Harwood J.H., McCaffery M., Fernandez D.E., Cline K.;
RT "Localization and integration of thylakoid protein translocase subunit
RT cpTatC.";
RL Plant J. 58:831-842(2009).
RN [6]
RP 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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, 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:11457457,
CC ECO:0000269|PubMed:11502764, ECO:0000269|PubMed:19207210,
CC ECO:0000269|PubMed:22564412}.
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:19207210,
CC ECO:0000269|PubMed:22564412}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000305|PubMed:11457457, ECO:0000305|PubMed:14653819,
CC ECO:0000305|PubMed:19207210, ECO:0000305|PubMed:22564412}; Multi-pass
CC membrane protein {ECO:0000305|PubMed:11457457,
CC ECO:0000305|PubMed:14653819, ECO:0000305|PubMed:19207210,
CC ECO:0000305|PubMed:22564412}. Note=The N-terminus is located in the
CC stroma.
CC -!- MISCELLANEOUS: TATC targets to thylakoids via a stromal intermediate,
CC and then probably integrated through a thylakoid translocation pathway.
CC {ECO:0000305|PubMed:22564412}.
CC -!- SIMILARITY: Belongs to the TatC family. {ECO:0000305}.
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DR EMBL; AF284759; AAK93948.1; -; mRNA.
DR AlphaFoldDB; Q94G17; -.
DR SMR; Q94G17; -.
DR PRIDE; Q94G17; -.
DR EnsemblPlants; Psat6g222720.2; Psat6g222720.2.cds; Psat6g222720.
DR Gramene; Psat6g222720.2; Psat6g222720.2.cds; Psat6g222720.
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: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_00902; TatC; 1.
DR InterPro; IPR019820; Sec-indep_translocase_CS.
DR InterPro; IPR002033; TatC.
DR PANTHER; PTHR30371; PTHR30371; 1.
DR Pfam; PF00902; TatC; 1.
DR PRINTS; PR01840; TATCFAMILY.
DR TIGRFAMs; TIGR00945; tatC; 1.
DR PROSITE; PS01218; TATC; 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..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 51..?
FT /note="Thylakoid"
FT /evidence="ECO:0000255"
FT CHAIN ?..353
FT /note="Sec-independent protein translocase protein TATC,
FT chloroplastic"
FT /id="PRO_0000419911"
FT TOPO_DOM 51..136
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..192
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..223
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..270
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..302
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..330
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..353
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT REGION 63..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 353 AA; 38912 MW; C08ED36571E6E2FB CRC64;
MGLGTTTVPT NILPQFGLHR THLNPIRVNN STGFSYPLSL RKNKSFDRLV CFAVDDEIRE
KQQQQLSTSS TRLGSAVEER PENKDMIDGI SEEALENFKE DGERSAIYDF LYPSKELLPD
DKEMSIFDHL EELRERIFIS VLGVGGSILG CFAFSKDLVK ILEAPVKSEG VRFLQLAPGE
FFFTTLKVSG YCGLLLGSPI ILYEIIAFII PGLTKEERKF LGPIVLGSSV LFYAGITFSY
LVLVPAALNF FVNYAEGAVE SLWSIDQYFE FVLVLMFSTG LSFQVPIIQL LLGQLGLVSG
DKMLSVWRYV VVGAVVAAAV VTPSTDPLTQ VLLAAPLLGL YLGGAWMVKL AGR
