ID   TATB_SHESA              Reviewed;         147 AA.
AC   A0L1M8;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Sec-independent protein translocase protein TatB {ECO:0000255|HAMAP-Rule:MF_00237};
GN   Name=tatB {ECO:0000255|HAMAP-Rule:MF_00237};
GN   OrderedLocusNames=Shewana3_3729;
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANA-3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA   Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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. Together with
CC       TatC, TatB is part of a receptor directly interacting with Tat signal
CC       peptides. TatB may form an oligomeric binding site that transiently
CC       accommodates folded Tat precursor proteins before their translocation.
CC       {ECO:0000255|HAMAP-Rule:MF_00237}.
CC   -!- SUBUNIT: The Tat system comprises two distinct complexes: a TatABC
CC       complex, containing multiple copies of TatA, TatB and TatC subunits,
CC       and a separate TatA complex, containing only TatA subunits. Substrates
CC       initially bind to the TatABC complex, which probably triggers
CC       association of the separate TatA complex to form the active translocon.
CC       {ECO:0000255|HAMAP-Rule:MF_00237}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00237}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00237}.
CC   -!- SIMILARITY: Belongs to the TatB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00237}.
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DR   EMBL; CP000469; ABK49947.1; -; Genomic_DNA.
DR   RefSeq; WP_011718486.1; NC_008577.1.
DR   AlphaFoldDB; A0L1M8; -.
DR   SMR; A0L1M8; -.
DR   STRING; 94122.Shewana3_3729; -.
DR   EnsemblBacteria; ABK49947; ABK49947; Shewana3_3729.
DR   KEGG; shn:Shewana3_3729; -.
DR   eggNOG; COG1826; Bacteria.
DR   HOGENOM; CLU_086034_1_0_6; -.
DR   OMA; GQFQEAM; -.
DR   OrthoDB; 2073616at2; -.
DR   Proteomes; UP000002589; Chromosome.
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_00237; TatB; 1.
DR   InterPro; IPR003369; TatA/B/E.
DR   InterPro; IPR018448; TatB.
DR   Pfam; PF02416; TatA_B_E; 1.
DR   TIGRFAMs; TIGR01410; tatB; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..147
FT                   /note="Sec-independent protein translocase protein TatB"
FT                   /id="PRO_0000301236"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00237"
FT   REGION          85..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   147 AA;  15919 MW;  5EA04C43BAF1F27B CRC64;
     MFDGIGFMEL LLIGVLGLVV LGPERLPVAV RSVTSWIRAM KRMANSVKEE LEQELKIEQL
     HADLKKAESK GLSNLSPELQ ESIDQLKQAA QSVNRPYQVQ DVPAPENQIH NPASQSVSTE
     ASPSASSAPT SESNQGEDTR SNPKANG