(data stored in ACNUC7421 zone)

SWISSPROT: TATAD_BACSU

ID   TATAD_BACSU             Reviewed;          70 AA.
AC   O31467;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 2.
DT   11-DEC-2019, entry version 107.
DE   RecName: Full=Sec-independent protein translocase protein TatAd {ECO:0000255|HAMAP-Rule:MF_00236};
GN   Name=tatAd {ECO:0000255|HAMAP-Rule:MF_00236}; Synonyms=yczB;
GN   OrderedLocusNames=BSU02630;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   SEQUENCE REVISION TO 18 AND 34.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [3]
RP   IDENTIFICATION OF THE TAT GENES.
RX   PubMed=11007775; DOI=10.1074/jbc.m004887200;
RA   Jongbloed J.D.H., Martin U., Antelmann H., Hecker M., Tjalsma H.,
RA   Venema G., Bron S., van Dijl J.M., Mueller J.;
RT   "TatC is a specificity determinant for protein secretion via the twin-
RT   arginine translocation pathway.";
RL   J. Biol. Chem. 275:41350-41357(2000).
RN   [4]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH PHOD PRECURSOR.
RX   PubMed=12867413; DOI=10.1074/jbc.m306516200;
RA   Pop O.I., Westermann M., Volkmer-Engert R., Schulz D., Lemke C.,
RA   Schreiber S., Gerlach R., Wetzker R., Mueller J.P.;
RT   "Sequence-specific binding of prePhoD to soluble TatAd indicates protein-
RT   mediated targeting of the Tat export in Bacillus subtilis.";
RL   J. Biol. Chem. 278:38428-38436(2003).
RN   [5]
RP   CHARACTERIZATION OF THE TWO TAT TRANSLOCASE SYSTEMS.
RX   PubMed=15554971; DOI=10.1111/j.1365-2958.2004.04341.x;
RA   Jongbloed J.D.H., Grieger U., Antelmann H., Hecker M., Nijland R., Bron S.,
RA   van Dijl J.M.;
RT   "Two minimal Tat translocases in Bacillus.";
RL   Mol. Microbiol. 54:1319-1325(2004).
RN   [6]
RP   SUBUNIT.
RX   PubMed=16678787; DOI=10.1016/j.bbamem.2006.03.018;
RA   Westermann M., Pop O.I., Gerlach R., Appel T.R., Schloermann W.,
RA   Schreiber S., Mueller J.P.;
RT   "The TatAd component of the Bacillus subtilis twin-arginine protein
RT   transport system forms homo-multimeric complexes in its cytosolic and
RT   membrane embedded localisation.";
RL   Biochim. Biophys. Acta 1758:443-451(2006).
RN   [7]
RP   INTERACTION WITH TATCD.
RX   PubMed=16698798; DOI=10.1074/jbc.m513900200;
RA   Schreiber S., Stengel R., Westermann M., Volkmer-Engert R., Pop O.I.,
RA   Mueller J.P.;
RT   "Affinity of TatCd for TatAd elucidates its receptor function in the
RT   Bacillus subtilis twin arginine translocation (Tat) translocase system.";
RL   J. Biol. Chem. 281:19977-19984(2006).
RN   [8]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   PubMed=18029357; DOI=10.1074/jbc.m708134200;
RA   Barnett J.P., Eijlander R.T., Kuipers O.P., Robinson C.;
RT   "A minimal Tat system from a gram-positive organism: a bifunctional TatA
RT   subunit participates in discrete TatAC and TatA complexes.";
RL   J. Biol. Chem. 283:2534-2542(2008).
RN   [9]
RP   STRUCTURE BY NMR.
RX   PubMed=20726548; DOI=10.1021/ja1053785;
RA   Hu Y., Zhao E., Li H., Xia B., Jin C.;
RT   "Solution NMR structure of the TatA component of the twin-arginine protein
RT   transport system from gram-positive bacterium Bacillus subtilis.";
RL   J. Am. Chem. Soc. 132:15942-15944(2010).
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 membranes. TatA could
CC       form the protein-conducting channel of the Tat system. Required for
CC       PhoD secretion. The cytosolic fraction of TatAd binds the precursor of
CC       PhoD. {ECO:0000255|HAMAP-Rule:MF_00236, ECO:0000269|PubMed:18029357}.
CC   -!- SUBUNIT: Forms a complex with TatCd. Two types of complexes exist: one
CC       composed of TatAd and TatCd, and another composed only of TatAd.
CC       Soluble TatAd forms homomultimers bigger than 100 kDa. Soluble TatAd
CC       associates in homomultimeric micelle-like particles with a size of
CC       about 12 or 25 nm in diameter as well as in elongated particles of 12
CC       nm in diameter. {ECO:0000255|HAMAP-Rule:MF_00236,
CC       ECO:0000269|PubMed:16678787, ECO:0000269|PubMed:18029357}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC       Cytoplasm, cytosol. Note=At the onset of phosphate starvation,
CC       substantial amounts of TatAd are present in the cytosol. Upon ongoing
CC       starvation, the amount of TatAd in the cytosol decreases.
CC   -!- INDUCTION: Expressed under conditions of phosphate starvation.
CC   -!- MISCELLANEOUS: B.subtilis possesses two minimal, substrate-specific,
CC       Tat translocases: TatAd-TatCd and TatAy-TatCy, each one composed of a
CC       TatA and a TatC protein. TatA is bifunctional and performs the function
CC       of both the TatA and TatB proteins of Gram-negative organisms.
CC   -!- MISCELLANEOUS: Membrane-localization and maintenance of TatAd is
CC       assisted by TatCd.
CC   -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000255|HAMAP-
CC       Rule:MF_00236}.
DR   EMBL; AL009126; CAB12057.2; -; Genomic_DNA.
DR   PIR; A69767; A69767.
DR   RefSeq; NP_388145.2; NC_000964.3.
DR   RefSeq; WP_003223835.1; NZ_JNCM01000030.1.
DR   PDB; 2L16; NMR; -; A=1-70.
DR   PDBsum; 2L16; -.
DR   SMR; O31467; -.
DR   IntAct; O31467; 20.
DR   STRING; 224308.BSU02630; -.
DR   TCDB; 2.A.64.3.1; the twin arginine targeting (tat) family.
DR   PaxDb; O31467; -.
DR   PRIDE; O31467; -.
DR   EnsemblBacteria; CAB12057; CAB12057; BSU02630.
DR   GeneID; 938398; -.
DR   KEGG; bsu:BSU02630; -.
DR   PATRIC; fig|224308.179.peg.273; -.
DR   eggNOG; ENOG41067S4; Bacteria.
DR   eggNOG; ENOG410XUF0; LUCA.
DR   HOGENOM; HOG000245365; -.
DR   InParanoid; O31467; -.
DR   KO; K03116; -.
DR   OMA; SEWIIIA; -.
DR   PhylomeDB; O31467; -.
DR   BioCyc; BSUB:BSU02630-MONOMER; -.
DR   PRO; PR:O31467; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0033281; C:TAT protein transport complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0008320; F:protein transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043953; P:protein transport by the Tat complex; IEA:UniProtKB-UniRule.
DR   DisProt; DP00827; -.
DR   HAMAP; MF_00236; TatA_E; 1.
DR   InterPro; IPR003369; TatA/B/E.
DR   InterPro; IPR006312; TatA/E.
DR   Pfam; PF02416; MttA_Hcf106; 1.
DR   TIGRFAMs; TIGR01411; tatAE; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O31467.
DR   SWISS-2DPAGE; O31467.
KW   3D-structure; Cell membrane; Cytoplasm; Membrane; Protein transport;
KW   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..70
FT                   /note="Sec-independent protein translocase protein TatAd"
FT                   /id="PRO_0000097981"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00236"
FT   STRAND          3..5
FT                   /evidence="ECO:0000244|PDB:2L16"
FT   HELIX           7..20
FT                   /evidence="ECO:0000244|PDB:2L16"
FT   TURN            23..25
FT                   /evidence="ECO:0000244|PDB:2L16"
FT   HELIX           26..49
FT                   /evidence="ECO:0000244|PDB:2L16"
SQ   SEQUENCE   70 AA;  7431 MW;  3D6B356BC425D111 CRC64;
     MFSNIGIPGL ILIFVIALII FGPSKLPEIG RAAGRTLLEF KSATKSLVSG DEKEEKSAEL
     TAVKQDKNAG
//

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