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TATB_ARATH
ID   TATB_ARATH              Reviewed;         260 AA.
AC   Q9XH75;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 124.
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; OrderedLocusNames=At5g52440; ORFNames=K24M7.19;
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 [MRNA].
RX   PubMed=10402459; DOI=10.1083/jcb.146.1.45;
RA   Mori M., Summer E.J., Ma X., Cline K.;
RT   "Component specificity for the thylakoidal Sec and Delta pH-dependent
RT   protein transport pathways.";
RL   J. Cell Biol. 146:45-56(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
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   [6]
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 TatB family. {ECO:0000305}.
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DR   EMBL; AF139188; AAD32652.1; -; mRNA.
DR   EMBL; AB019226; BAB10541.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96214.1; -; Genomic_DNA.
DR   EMBL; AK118733; BAC43327.1; -; mRNA.
DR   EMBL; BT005414; AAO63834.1; -; mRNA.
DR   RefSeq; NP_200057.1; NM_124623.4.
DR   AlphaFoldDB; Q9XH75; -.
DR   BioGRID; 20565; 1.
DR   STRING; 3702.AT5G52440.1; -.
DR   TCDB; 2.A.64.2.1; the twin arginine targeting (tat) family.
DR   iPTMnet; Q9XH75; -.
DR   PaxDb; Q9XH75; -.
DR   PRIDE; Q9XH75; -.
DR   ProteomicsDB; 228044; -.
DR   EnsemblPlants; AT5G52440.1; AT5G52440.1; AT5G52440.
DR   GeneID; 835320; -.
DR   Gramene; AT5G52440.1; AT5G52440.1; AT5G52440.
DR   KEGG; ath:AT5G52440; -.
DR   Araport; AT5G52440; -.
DR   TAIR; locus:2156722; AT5G52440.
DR   eggNOG; ENOG502QSWH; Eukaryota.
DR   HOGENOM; CLU_072198_2_0_1; -.
DR   InParanoid; Q9XH75; -.
DR   OMA; NCAVSHT; -.
DR   OrthoDB; 1173036at2759; -.
DR   PhylomeDB; Q9XH75; -.
DR   PRO; PR:Q9XH75; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9XH75; baseline and differential.
DR   Genevisible; Q9XH75; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009534; C:chloroplast thylakoid; 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:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0033281; C:TAT protein transport complex; IDA:UniProtKB.
DR   GO; GO:0009579; C:thylakoid; IDA:TAIR.
DR   GO; GO:0009977; F:proton motive force dependent protein transmembrane transporter activity; IDA:TAIR.
DR   GO; GO:1902458; P:positive regulation of stomatal opening; IMP:TAIR.
DR   GO; GO:0045038; P:protein import into chloroplast thylakoid membrane; IDA:TAIR.
DR   GO; GO:0043953; P:protein transport by the Tat complex; IEA:InterPro.
DR   GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; IMP:TAIR.
DR   GO; GO:2000070; P:regulation of response to water deprivation; IMP:TAIR.
DR   GO; GO:0009409; P:response to cold; IMP:TAIR.
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; Reference proteome;
KW   Thylakoid; Transit peptide; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   TRANSIT         1..83
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           84..260
FT                   /note="Sec-independent protein translocase protein TATB,
FT                   chloroplastic"
FT                   /id="PRO_0000419914"
FT   TOPO_DOM        84..85
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107..260
FT                   /note="Stromal"
FT                   /evidence="ECO:0000255"
FT   REGION          146..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..179
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   260 AA;  28232 MW;  155591803ACC8CF7 CRC64;
     MAMALQIIAS SSSSPTITKS HLFSYPPLQS RYKASKPNLS SWFSLLGSSR FSPYIGLKHL
     GISISPKSSN PEKKRRCKSM MIRASLFGVG APEALVIGVV ALLVFGPKGL AEVARNLGKT
     LRTFQPTIRE LQDVSRDFKS TLEREIGLDD ISTPNVYNQN RTNPVQPPPP PPPPSVPSTE
     APVTANDPND SQSPKAYTSE DYLKFTEEQL KALSPAESQT EDQTQTQEPP QPTTVQTPTG
     ESQPNGTARE TTAASPPRQD
 
 
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