TATC_MAIZE
ID TATC_MAIZE Reviewed; 356 AA.
AC C4IZX0;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Sec-independent protein translocase protein TATC, chloroplastic;
DE AltName: Full=Protein TWIN-ARGININE TRANSLOCATION C;
DE Flags: Precursor;
GN Name=TATC;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=The N-
CC terminus is located in the stroma. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TatC family. {ECO:0000305}.
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DR EMBL; BT084117; ACR34470.1; -; mRNA.
DR RefSeq; XP_008652912.1; XM_008654690.1.
DR AlphaFoldDB; C4IZX0; -.
DR SMR; C4IZX0; -.
DR STRING; 4577.GRMZM2G025123_P01; -.
DR PaxDb; C4IZX0; -.
DR EnsemblPlants; Zm00001eb009240_T002; Zm00001eb009240_P002; Zm00001eb009240.
DR EnsemblPlants; Zm00001eb009240_T003; Zm00001eb009240_P003; Zm00001eb009240.
DR Gramene; Zm00001eb009240_T002; Zm00001eb009240_P002; Zm00001eb009240.
DR Gramene; Zm00001eb009240_T003; Zm00001eb009240_P003; Zm00001eb009240.
DR eggNOG; ENOG502QVCB; Eukaryota.
DR HOGENOM; CLU_031942_2_0_1; -.
DR OMA; RMLNYSA; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; C4IZX0; baseline and differential.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033281; C:TAT protein transport complex; IBA:GO_Central.
DR GO; GO:0009977; F:proton motive force dependent protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IBA:GO_Central.
DR GO; GO:0043953; P:protein transport by the Tat complex; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Chloroplast; Membrane; Plastid; Protein transport; Reference proteome;
KW Thylakoid; Transit peptide; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 56..?
FT /note="Thylakoid"
FT /evidence="ECO:0000255"
FT CHAIN ?..356
FT /note="Sec-independent protein translocase protein TATC,
FT chloroplastic"
FT /id="PRO_0000419912"
FT TOPO_DOM 56..143
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..195
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..222
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..273
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..305
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..330
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..356
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT REGION 64..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 38684 MW; E0D61F70E124903A CRC64;
MGSAGALLWH TPQQLHGRGI LFRQSRPLLR QRNLPLISLA APALEPERRR RQCLRCAAVD
GDGALRESGP LPQKESPSSG IGAALEDPPP GPPVENGSFG GPSQEEQSAL YTFLYPSKDL
LPDDKEMSIF DHLEELRDRI FISVLAVGAA ILGCFAFSKD LVIFLEAPVT AQGVRFLQLS
PGEFFFTTLK VSGYCGLLLG SPIILYEIIA FVIPGLTRDE RKFLGPIVLG SSVLFYLGIF
FSYTVLSPAA LNFFVNYADG AVESLWSIDQ YFEFILVLMF STGLSFQVPV IQLLLGQLGL
VSSDQMLSIW RYVVVGAVVA AAVLTPSTDP LTQMLLAGPL LGLYLGGAWM VKITGR
