ID   TATB_MARMM              Reviewed;         169 AA.
AC   Q0AND7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Mmar10_1908;
OS   Maricaulis maris (strain MCS10).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC   Maricaulis.
OX   NCBI_TaxID=394221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS10;
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   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA   Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
RL   Submitted (AUG-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; CP000449; ABI66200.1; -; Genomic_DNA.
DR   RefSeq; WP_011643845.1; NC_008347.1.
DR   AlphaFoldDB; Q0AND7; -.
DR   SMR; Q0AND7; -.
DR   STRING; 394221.Mmar10_1908; -.
DR   EnsemblBacteria; ABI66200; ABI66200; Mmar10_1908.
DR   KEGG; mmr:Mmar10_1908; -.
DR   eggNOG; COG1826; Bacteria.
DR   HOGENOM; CLU_086034_1_3_5; -.
DR   OMA; WIRAMRS; -.
DR   OrthoDB; 2073616at2; -.
DR   Proteomes; UP000001964; 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..169
FT                   /note="Sec-independent protein translocase protein TatB"
FT                   /id="PRO_0000301181"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00237"
FT   REGION          106..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   169 AA;  18178 MW;  DF13C5262B7DA537 CRC64;
     MSPGIGMPEL LVVLVLALVV VGPQQLPVMM RKVGQMMAQA RAMAKDFQNS FEEIGRETEL
     SELRREIDAL KQANPINQIH GELDKAARGT QDDDIRALKL KHVEQNQAET DADKAAKAAK
     LAALDSEGPQ STTPEADARA DAAASADETE RAAPVETTPA KPVDEIKGR