ID   TATB_PECAS              Reviewed;         197 AA.
AC   Q6DAQ3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Sec-independent protein translocase protein TatB {ECO:0000255|HAMAP-Rule:MF_00237};
GN   Name=tatB {ECO:0000255|HAMAP-Rule:MF_00237}; OrderedLocusNames=ECA0200;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG73119.1; -; Genomic_DNA.
DR   RefSeq; WP_011091839.1; NC_004547.2.
DR   AlphaFoldDB; Q6DAQ3; -.
DR   SMR; Q6DAQ3; -.
DR   STRING; 218491.ECA0200; -.
DR   DNASU; 2884322; -.
DR   EnsemblBacteria; CAG73119; CAG73119; ECA0200.
DR   KEGG; eca:ECA0200; -.
DR   PATRIC; fig|218491.5.peg.199; -.
DR   eggNOG; COG1826; Bacteria.
DR   HOGENOM; CLU_086034_1_0_6; -.
DR   OMA; MFEVGWT; -.
DR   OrthoDB; 2073616at2; -.
DR   Proteomes; UP000007966; 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; IPR018448; TatB.
DR   TIGRFAMs; TIGR01410; tatB; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..197
FT                   /note="Sec-independent protein translocase protein TatB"
FT                   /id="PRO_0000301166"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00237"
FT   REGION          93..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   197 AA;  21343 MW;  43BE176C091EA609 CRC64;
     MFDIGFGELL LVMVLGLIVL GPERLPVAVR TVASWIRTLR SLASTVQNEL SQELKLQEFQ
     ESLKKVEKAS LQNLSPELKA SMDELKDAAE AMKRGYTETP SPQKSDDPKK SGDHSATVEP
     QSNIPLNDPE AAYDGVIEAE TAVRPADSQQ KPENAAVAEN HNDGRHATSD EAVGNNNVKP
     EQSQPSAASA RQPSDSR