ID A0A1M6ZUN6_9RHOB Unreviewed; 74 AA.
AC A0A1M6ZUN6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05444414_11160 {ECO:0000313|EMBL:SHL34192.1};
OS Roseovarius marisflavi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1054996 {ECO:0000313|EMBL:SHL34192.1, ECO:0000313|Proteomes:UP000184191};
RN [1] {ECO:0000313|EMBL:SHL34192.1, ECO:0000313|Proteomes:UP000184191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29327 {ECO:0000313|EMBL:SHL34192.1,
RC ECO:0000313|Proteomes:UP000184191};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FRBN01000011; SHL34192.1; -; Genomic_DNA.
DR RefSeq; WP_073198173.1; NZ_FRBN01000011.1.
DR AlphaFoldDB; A0A1M6ZUN6; -.
DR STRING; 1054996.SAMN05444414_11160; -.
DR OrthoDB; 7161179at2; -.
DR Proteomes; UP000184191; 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 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};
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 42..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 74 AA; 7875 MW; 26941E472A9B0742 CRC64;
MLNNIGLPGL LLIAVVVLVL FGRGKISSLM GEVGKGITSF KKGVSEGTKE LEDESKESVE
TARDVTPTDE KDKV
//
