ID A0A1R4B810_9VIBR Unreviewed; 83 AA.
AC A0A1R4B810;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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 ECO:0000313|EMBL:SJL85060.1};
GN ORFNames=VPAL9027_03081 {ECO:0000313|EMBL:SJL85060.1};
OS Vibrio palustris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1918946 {ECO:0000313|EMBL:SJL85060.1, ECO:0000313|Proteomes:UP000189475};
RN [1] {ECO:0000313|EMBL:SJL85060.1, ECO:0000313|Proteomes:UP000189475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 9027 {ECO:0000313|EMBL:SJL85060.1,
RC ECO:0000313|Proteomes:UP000189475};
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; FUFT01000009; SJL85060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4B810; -.
DR STRING; 1918946.VPAL9027_03081; -.
DR OrthoDB; 7066617at2; -.
DR Proteomes; UP000189475; 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:UP000189475};
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..22
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00236"
FT REGION 41..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 83 AA; 9051 MW; D74C84CE5B045AEF CRC64;
MGGISIWQLL IVALIVVVLF GTKKLRNVGS DVGGAVKGFK KAMEEDDSTA KKESDSDFEN
QNISHKESAQ SDSTEKKHDK EQA
//