ID   TATA_STRM5              Reviewed;          75 AA.
AC   B4SNR8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Sec-independent protein translocase protein TatA {ECO:0000255|HAMAP-Rule:MF_00236};
GN   Name=tatA {ECO:0000255|HAMAP-Rule:MF_00236}; OrderedLocusNames=Smal_3989;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA   Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) 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. TatA could
CC       form the protein-conducting channel of the Tat system.
CC       {ECO:0000255|HAMAP-Rule:MF_00236}.
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_00236}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00236}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00236}.
CC   -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000255|HAMAP-
CC       Rule:MF_00236}.
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; CP001111; ACF53688.1; -; Genomic_DNA.
DR   RefSeq; WP_012512521.1; NC_011071.1.
DR   AlphaFoldDB; B4SNR8; -.
DR   SMR; B4SNR8; -.
DR   STRING; 391008.Smal_3989; -.
DR   EnsemblBacteria; ACF53688; ACF53688; Smal_3989.
DR   KEGG; smt:Smal_3989; -.
DR   eggNOG; COG1826; Bacteria.
DR   HOGENOM; CLU_086034_5_3_6; -.
DR   OMA; KDGMREG; -.
DR   OrthoDB; 1907955at2; -.
DR   BioCyc; SMAL391008:SMAL_RS20250-MON; -.
DR   Proteomes; UP000001867; 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_00236; TatA_E; 1.
DR   InterPro; IPR003369; TatA/B/E.
DR   InterPro; IPR006312; TatA/E.
DR   Pfam; PF02416; TatA_B_E; 1.
DR   TIGRFAMs; TIGR01411; tatAE; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..75
FT                   /note="Sec-independent protein translocase protein TatA"
FT                   /id="PRO_1000197909"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00236"
FT   REGION          40..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   75 AA;  8386 MW;  E9348E26CAA95928 CRC64;
     MGSFSIWHWL VVLAIVLLVF GTKRLTSGAK DLGSAVKEFK KGMRDEDKPN AQLGDESRSQ
     DASRTAQDEH DRTPR