TATAY_BACSU
ID TATAY_BACSU Reviewed; 57 AA.
AC O05522; Q797D3;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Sec-independent protein translocase protein TatAy {ECO:0000255|HAMAP-Rule:MF_00236};
GN Name=tatAy {ECO:0000255|HAMAP-Rule:MF_00236}; Synonyms=ydiI;
GN OrderedLocusNames=BSU05980;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9202461; DOI=10.1099/00221287-143-6-1861;
RA Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA Ogasawara N.;
RT "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT Bacillus subtilis chromosome.";
RL Microbiology 143:1861-1866(1997).
RN [2]
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 [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 EXPORT OF THE YWBN PROTEIN, AND CHARACTERIZATION OF THE TWO TAT TRANSLOCASE
RP 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 [5]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19049517; DOI=10.1111/j.1742-4658.2008.06776.x;
RA Barnett J.P., van der Ploeg R., Eijlander R.T., Nenninger A., Mendel S.,
RA Rozeboom R., Kuipers O.P., van Dijl J.M., Robinson C.;
RT "The twin-arginine translocation (Tat) systems from Bacillus subtilis
RT display a conserved mode of complex organization and similar substrate
RT recognition requirements.";
RL FEBS J. 276:232-243(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 membranes. TatA could
CC form the protein-conducting channel of the Tat system. Required for
CC YwbN secretion. {ECO:0000255|HAMAP-Rule:MF_00236,
CC ECO:0000269|PubMed:19049517}.
CC -!- SUBUNIT: Forms a complex with TatCy. Two types of complexes exist: one
CC composed of TatAy and TatCy, and another composed only of TatAy.
CC Cytosolic TatA forms large complexes or aggregates. {ECO:0000255|HAMAP-
CC Rule:MF_00236, ECO:0000269|PubMed:19049517}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00236,
CC ECO:0000269|PubMed:19049517}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00236, ECO:0000269|PubMed:19049517}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:19049517}.
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 -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000255|HAMAP-
CC Rule:MF_00236}.
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DR EMBL; D88802; BAA19722.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12417.1; -; Genomic_DNA.
DR PIR; B69787; B69787.
DR RefSeq; NP_388479.1; NC_000964.3.
DR RefSeq; WP_003234072.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O05522; -.
DR SMR; O05522; -.
DR IntAct; O05522; 16.
DR STRING; 224308.BSU05980; -.
DR TCDB; 2.A.64.3.2; the twin arginine targeting (tat) family.
DR PaxDb; O05522; -.
DR PRIDE; O05522; -.
DR EnsemblBacteria; CAB12417; CAB12417; BSU_05980.
DR GeneID; 939878; -.
DR KEGG; bsu:BSU05980; -.
DR PATRIC; fig|224308.179.peg.643; -.
DR eggNOG; COG1826; Bacteria.
DR InParanoid; O05522; -.
DR OMA; FREFKNG; -.
DR PhylomeDB; O05522; -.
DR BioCyc; BSUB:BSU05980-MON; -.
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 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 Cell membrane; Cytoplasm; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..57
FT /note="Sec-independent protein translocase protein TatAy"
FT /id="PRO_0000097980"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00236"
SQ SEQUENCE 57 AA; 6065 MW; 91E4CB4138D8E751 CRC64;
MPIGPGSLAV IAIVALIIFG PKKLPELGKA AGDTLREFKN ATKGLTSDEE EKKKEDQ