ID   TATB_RHIL3              Reviewed;         203 AA.
AC   Q1MHM4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, 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=RL2047;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
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; AM236080; CAK07539.1; -; Genomic_DNA.
DR   RefSeq; WP_011651656.1; NC_008380.1.
DR   AlphaFoldDB; Q1MHM4; -.
DR   SMR; Q1MHM4; -.
DR   STRING; 216596.RL2047; -.
DR   EnsemblBacteria; CAK07539; CAK07539; RL2047.
DR   KEGG; rle:RL2047; -.
DR   eggNOG; COG1826; Bacteria.
DR   HOGENOM; CLU_086034_1_3_5; -.
DR   OMA; GQFQEAM; -.
DR   OrthoDB; 2073616at2; -.
DR   Proteomes; UP000006575; 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..203
FT                   /note="Sec-independent protein translocase protein TatB"
FT                   /id="PRO_0000301220"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00237"
FT   REGION          179..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   203 AA;  21753 MW;  2949574A88EBDE0D CRC64;
     MFDIGWTELL VIAVVLIVVV GPKDLPPMLR AFGKMTQRAR KVAGDFRAQF DEALREAELD
     DVRQTISDAQ KLNPVNSLRE AMNPLRQMGN EIKADLQKAT TVTENKTEVP PDAVAAPTPS
     MSLPETPPLV ATPAPSEPVA AAVVQADTVA AKPKAVRKPR GKIADKVDAA AAVAVPVEKP
     KRTTAVRKPA TLKKPAQTKK DEA