ID   TATA_METPP              Reviewed;          76 AA.
AC   A2SE14;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Mpe_A0841;
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX   NCBI_TaxID=420662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX   PubMed=17158667; DOI=10.1128/jb.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
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}.
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DR   EMBL; CP000555; ABM93803.1; -; Genomic_DNA.
DR   RefSeq; WP_011828441.1; NC_008825.1.
DR   AlphaFoldDB; A2SE14; -.
DR   SMR; A2SE14; -.
DR   STRING; 420662.Mpe_A0841; -.
DR   EnsemblBacteria; ABM93803; ABM93803; Mpe_A0841.
DR   KEGG; mpt:Mpe_A0841; -.
DR   eggNOG; COG1826; Bacteria.
DR   HOGENOM; CLU_086034_5_1_4; -.
DR   OMA; HWIVILV; -.
DR   OrthoDB; 1907955at2; -.
DR   Proteomes; UP000000366; 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   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..76
FT                   /note="Sec-independent protein translocase protein TatA"
FT                   /id="PRO_1000044397"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00236"
FT   REGION          44..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   76 AA;  7998 MW;  44D3D38A734EF286 CRC64;
     MGSFSIWHWL IVLLIVVLVF GTKKLKNIGS DLGGAVKGFK DGVRDGSTAP ADPAQQVTAN
     KSADANTVDV EAKQKS