TATA_ARATH
ID TATA_ARATH Reviewed; 147 AA.
AC Q9LKU2;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 119.
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; OrderedLocusNames=At5g28750; ORFNames=T32B20.e;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP SUBUNIT.
RX PubMed=18930082; DOI=10.1016/j.bbamcr.2008.09.006;
RA Jakob M., Kaiser S., Gutensohn M., Hanner P., Kloesgen R.B.;
RT "Tat subunit stoichiometry in Arabidopsis thaliana challenges the proposed
RT function of TatA as the translocation pore.";
RL Biochim. Biophys. Acta 1793:388-394(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. {ECO:0000269|PubMed:18930082}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=The C-
CC terminus is located in the stroma. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000305}.
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DR EMBL; AF262041; AAF67362.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93831.1; -; Genomic_DNA.
DR EMBL; AF325006; AAG40358.1; -; mRNA.
DR EMBL; AY056276; AAL07125.1; -; mRNA.
DR EMBL; AY091429; AAM14368.1; -; mRNA.
DR RefSeq; NP_198227.1; NM_122758.4.
DR PDB; 7B7O; NMR; -; A=62-114.
DR PDBsum; 7B7O; -.
DR AlphaFoldDB; Q9LKU2; -.
DR SMR; Q9LKU2; -.
DR STRING; 3702.AT5G28750.1; -.
DR TCDB; 2.A.64.2.1; the twin arginine targeting (tat) family.
DR iPTMnet; Q9LKU2; -.
DR PaxDb; Q9LKU2; -.
DR PRIDE; Q9LKU2; -.
DR ProteomicsDB; 234233; -.
DR EnsemblPlants; AT5G28750.1; AT5G28750.1; AT5G28750.
DR GeneID; 832987; -.
DR Gramene; AT5G28750.1; AT5G28750.1; AT5G28750.
DR KEGG; ath:AT5G28750; -.
DR Araport; AT5G28750; -.
DR TAIR; locus:2184241; AT5G28750.
DR eggNOG; ENOG502S7UG; Eukaryota.
DR HOGENOM; CLU_135887_0_0_1; -.
DR InParanoid; Q9LKU2; -.
DR OMA; SMTEQPK; -.
DR OrthoDB; 1641169at2759; -.
DR PhylomeDB; Q9LKU2; -.
DR PRO; PR:Q9LKU2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LKU2; baseline and differential.
DR Genevisible; Q9LKU2; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0033281; C:TAT protein transport complex; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:TAIR.
DR GO; GO:0043953; P:protein transport by the Tat complex; IEA:InterPro.
DR GO; GO:0032594; P:protein transport within lipid bilayer; IDA:TAIR.
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 3D-structure; Chloroplast; Membrane; Plastid; Protein transport;
KW Reference proteome; Thylakoid; Transit peptide; Translocation;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..59
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 60..147
FT /note="Sec-independent protein translocase protein TATA,
FT chloroplastic"
FT /id="PRO_0000419918"
FT TOPO_DOM 60..61
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..147
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT REGION 109..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:7B7O"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:7B7O"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:7B7O"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:7B7O"
SQ SEQUENCE 147 AA; 15713 MW; AC8FA76F4F8BBF95 CRC64;
MATSVATLSS PPPVSLPLLS SSRSSFFSNC FTVTTRPNTR SLVAIGRRIR QEPTRKPLTC
NALFGLGVPE LAVIAGVAAL LFGPKKLPEI GKSIGKTVKS FQQAAKEFES ELKTEPEESV
AESSQVATSN KEEEKKTEVS SSSKENV
