ID   TATA_LEPIN              Reviewed;          85 AA.
AC   Q8F4W2;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   25-MAY-2022, entry version 84.
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=LA_1926;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
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: Forms a complex with TatC. {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}.
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DR   EMBL; AE010300; AAN49125.2; -; Genomic_DNA.
DR   RefSeq; NP_712107.2; NC_004342.2.
DR   RefSeq; WP_000457916.1; NC_004342.2.
DR   AlphaFoldDB; Q8F4W2; -.
DR   SMR; Q8F4W2; -.
DR   STRING; 189518.LA_1926; -.
DR   EnsemblBacteria; AAN49125; AAN49125; LA_1926.
DR   GeneID; 61141872; -.
DR   KEGG; lil:LA_1926; -.
DR   PATRIC; fig|189518.3.peg.1913; -.
DR   HOGENOM; CLU_086034_5_4_12; -.
DR   Proteomes; UP000001408; Chromosome I.
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   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..85
FT                   /note="Sec-independent protein translocase protein TatA"
FT                   /id="PRO_0000097943"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00236"
FT   REGION          50..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   85 AA;  9302 MW;  28AF1CCF9B5D5F30 CRC64;
     MFAPLAVFGS LGWTEILLIL FIALLLFGGK RLPSLAKDLG DGIRSFRKSL TGESDDSSQQ
     ISQEQERSVP KEETKTSKSK KSKSA