ID A0A1T4WF82_9GAMM Unreviewed; 83 AA.
AC A0A1T4WF82;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Sec-independent protein translocase protein TatA {ECO:0000256|HAMAP-Rule:MF_00236};
GN Name=tatA {ECO:0000256|HAMAP-Rule:MF_00236};
GN ORFNames=SAMN02745130_01606 {ECO:0000313|EMBL:SKA75974.1};
OS Thiothrix eikelboomii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thiothrix.
OX NCBI_TaxID=92487 {ECO:0000313|EMBL:SKA75974.1, ECO:0000313|Proteomes:UP000190460};
RN [1] {ECO:0000313|EMBL:SKA75974.1, ECO:0000313|Proteomes:UP000190460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49788 {ECO:0000313|EMBL:SKA75974.1,
RC ECO:0000313|Proteomes:UP000190460};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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:0000256|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:0000256|HAMAP-Rule:MF_00236}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00236};
CC Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00236}.
CC -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000256|HAMAP-
CC Rule:MF_00236}.
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DR EMBL; FUYB01000005; SKA75974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4WF82; -.
DR STRING; 92487.SAMN02745130_01606; -.
DR OrthoDB; 7066617at2; -.
DR Proteomes; UP000190460; Unassembled WGS sequence.
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 Gene3D; 1.20.5.3310; -; 1.
DR HAMAP; MF_00236; TatA_E; 1.
DR InterPro; IPR003369; TatA/B/E.
DR InterPro; IPR006312; TatA/E.
DR NCBIfam; TIGR01411; tatAE; 1.
DR PANTHER; PTHR42982; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATA; 1.
DR PANTHER; PTHR42982:SF1; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATA; 1.
DR Pfam; PF02416; TatA_B_E; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00236};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00236};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_00236}; Reference proteome {ECO:0000313|Proteomes:UP000190460};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_00236};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00236};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00236};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00236}.
FT TRANSMEM 6..21
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00236"
FT REGION 45..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 83 AA; 9030 MW; CC33CEEA101B9B99 CRC64;
MHFSPLQLVL ILVIVILLFG TKKLRSMGGD LGEAFKNFRK AVKDGDEATA PEAEKTAQQI
PPANSNPIQG NVIDVQAKEK DKV
//
