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Database: UniProt
Entry: A0A1I4XAG1_9PROT
LinkDB: A0A1I4XAG1_9PROT
Original site: A0A1I4XAG1_9PROT 
ID   A0A1I4XAG1_9PROT        Unreviewed;        75 AA.
AC   A0A1I4XAG1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=SAMN05216386_0007 {ECO:0000313|EMBL:SFN22884.1};
OS   Nitrosospira briensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=35799 {ECO:0000313|EMBL:SFN22884.1, ECO:0000313|Proteomes:UP000183107};
RN   [1] {ECO:0000313|Proteomes:UP000183107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nsp8 {ECO:0000313|Proteomes:UP000183107};
RA   Varghese N.;
RL   Submitted (OCT-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; FOVJ01000001; SFN22884.1; -; Genomic_DNA.
DR   RefSeq; WP_074793402.1; NZ_FOVY01000003.1.
DR   AlphaFoldDB; A0A1I4XAG1; -.
DR   OrthoDB; 7066617at2; -.
DR   Proteomes; UP000183107; 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 inner membrane {ECO:0000256|ARBA:ARBA00022519};
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:UP000183107};
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          47..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   75 AA;  8223 MW;  8DA1F2BDCCCEA585 CRC64;
     MGSFSIWHWL IVLLIVVLVF GTKKLRNLGT DLGGAVKGFR EGVKSADDEE ITSGPRQTDA
     RIVEGEVKDK THVNS
//
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