TATA_ACIAC
ID TATA_ACIAC Reviewed; 87 AA.
AC A1TL12;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-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=Aave_1053;
OS Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=397945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAC00-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL Submitted (DEC-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. 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; CP000512; ABM31650.1; -; Genomic_DNA.
DR RefSeq; WP_011794208.1; NC_008752.1.
DR AlphaFoldDB; A1TL12; -.
DR SMR; A1TL12; -.
DR STRING; 397945.Aave_1053; -.
DR EnsemblBacteria; ABM31650; ABM31650; Aave_1053.
DR KEGG; aav:Aave_1053; -.
DR eggNOG; COG1826; Bacteria.
DR HOGENOM; CLU_086034_5_1_4; -.
DR OMA; MGLSIWH; -.
DR OrthoDB; 1907955at2; -.
DR Proteomes; UP000002596; 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..87
FT /note="Sec-independent protein translocase protein TatA"
FT /id="PRO_1000044346"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00236"
FT REGION 40..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 87 AA; 8988 MW; 87CA8CB022606683 CRC64;
MGSFSIWHWL IVLLIVVMVF GTKKLKNIGS DLGGAVKGFK DGMKDGSTPE GTPASTTAAT
PPAGQVTNQQ AHAADPGTID VEAKHKG
