TATB_MAIZE
ID TATB_MAIZE Reviewed; 243 AA.
AC O48950; A0A1D6ECA8;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Sec-independent protein translocase protein TATB, chloroplastic {ECO:0000305};
DE AltName: Full=Protein HIGH CHLOROPHYLL FLUORESCENCE 106 {ECO:0000303|PubMed:9367960};
DE AltName: Full=Protein TWIN-ARGININE TRANSLOCATION B {ECO:0000305};
DE Flags: Precursor;
GN Name=TATB {ECO:0000305|PubMed:10402459};
GN Synonyms=HCF106 {ECO:0000303|PubMed:9367960};
GN ORFNames=ZEAMMB73_Zm00001d003913 {ECO:0000312|EMBL:ONM17954.1};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. B73; TISSUE=Seedling leaf;
RX PubMed=9367960; DOI=10.1126/science.278.5342.1467;
RA Settles A.M., Yonetani A., Baron A., Bush D.R., Cline K., Martienssen R.;
RT "Sec-independent protein translocation by the maize Hcf106 protein.";
RL Science 278:1467-1470(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3]
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).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=7664731; DOI=10.1002/j.1460-2075.1995.tb00062.x;
RA Voelker R., Barkan A.;
RT "Two nuclear mutations disrupt distinct pathways for targeting proteins to
RT the chloroplast thylakoid.";
RL EMBO J. 14:3905-3914(1995).
RN [5]
RP FUNCTION.
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 [6]
RP FUNCTION.
RX PubMed=10816594; DOI=10.1074/jbc.m004137200;
RA Summer E.J., Mori H., Settles A.M., Cline K.;
RT "The thylakoid delta pH-dependent pathway machinery facilitates RR-
RT independent N-tail protein integration.";
RL J. Biol. Chem. 275:23483-23490(2000).
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:10402459,
CC ECO:0000269|PubMed:10816594, ECO:0000269|PubMed:9367960}.
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:0000305|PubMed:9367960}; Single-pass membrane protein
CC {ECO:0000305|PubMed:9367960}. Note=The C-terminus is located in the
CC stroma.
CC -!- DISRUPTION PHENOTYPE: Seedling lethality. Non-photosynthetic mutants
CC possess near normal pigment levels but lack one or more elements of the
CC electron transport activity in chloroplasts. Defects in protein
CC targeting across chloroplast thylakoid membrane (PubMed:7664731).
CC {ECO:0000269|PubMed:7664731, ECO:0000269|PubMed:9367960}.
CC -!- SIMILARITY: Belongs to the TatB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ONM17954.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF027808; AAC01571.1; -; mRNA.
DR EMBL; CM007648; ONM17954.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BT068439; ACN35336.1; -; mRNA.
DR PIR; T01297; T01297.
DR RefSeq; NP_001105878.1; NM_001112408.1.
DR AlphaFoldDB; O48950; -.
DR STRING; 4577.GRMZM5G898735_P02; -.
DR PaxDb; O48950; -.
DR PRIDE; O48950; -.
DR EnsemblPlants; Zm00001eb085050_T002; Zm00001eb085050_P002; Zm00001eb085050.
DR GeneID; 732790; -.
DR Gramene; Zm00001eb085050_T002; Zm00001eb085050_P002; Zm00001eb085050.
DR KEGG; zma:732790; -.
DR MaizeGDB; 47580; -.
DR eggNOG; ENOG502QSWH; Eukaryota.
DR HOGENOM; CLU_072198_0_0_1; -.
DR OrthoDB; 1446751at2759; -.
DR Proteomes; UP000007305; Chromosome 2.
DR ExpressionAtlas; O48950; baseline and differential.
DR Genevisible; O48950; ZM.
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:0009977; F:proton motive force dependent protein transmembrane transporter activity; 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 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..67
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 68..243
FT /note="Sec-independent protein translocase protein TATB,
FT chloroplastic"
FT /id="PRO_0000419916"
FT TOPO_DOM 68..69
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..243
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT REGION 129..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 243 AA; 26326 MW; 98A1EE715BABA385 CRC64;
MTPTANLLLP APPFVPISDV RRLQLPPRVR HQPRPCWKGV EWGSIQTRMV SSFVAVGSRT
RRRNVICASL FGVGAPEALV IGVVALLVFG PKGLAEVARN LGKTLRAFQP TIRELQDVSR
EFRSTLEREI GIDEVSQSTN YRPTTMNNNQ QPAADPNVKP EPAPYTSEEL MKVTEEQIAA
SAAAAWNPQQ PATSQQQEEA PTTPRSEDAP TSGGSDGPAA PARAVSDSDP NQVNKSQKAE
GER
