ID   TATB_RUEST              Reviewed;         162 AA.
AC   Q1GFN7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=TM1040_1796;
OS   Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria; unclassified Ruegeria.
OX   NCBI_TaxID=292414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM1040;
RG   US DOE Joint Genome Institute;
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   Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Silicibacter sp. TM1040.";
RL   Submitted (MAY-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000377; ABF64529.1; -; Genomic_DNA.
DR   RefSeq; WP_011539124.1; NC_008044.1.
DR   AlphaFoldDB; Q1GFN7; -.
DR   STRING; 292414.TM1040_1796; -.
DR   EnsemblBacteria; ABF64529; ABF64529; TM1040_1796.
DR   KEGG; sit:TM1040_1796; -.
DR   eggNOG; COG1826; Bacteria.
DR   HOGENOM; CLU_086034_1_3_5; -.
DR   OMA; DLMQDYQ; -.
DR   OrthoDB; 2073616at2; -.
DR   Proteomes; UP000000636; 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   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..162
FT                   /note="Sec-independent protein translocase protein TatB"
FT                   /id="PRO_0000301242"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00237"
FT   REGION          69..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   162 AA;  17036 MW;  CF15A7F9AFD8E48C CRC64;
     MFDLGWTELL VIGVVALIVV GPKDLPKLFR NVGRFVGKAR GMAREFSRAM EDAADEAGVS
     DIQKTFKTAT NPMGSAMDSV KQATRDLTDS IDPTKFDPES ETGKLAADRA ENAKKIQAAT
     ARAAADRMAR EAAEAAAKAE EAEAALSATP ASTASSDSET KA