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Database: UniProt
Entry: A0A410UKE7_9GAMM
LinkDB: A0A410UKE7_9GAMM
Original site: A0A410UKE7_9GAMM 
ID   A0A410UKE7_9GAMM        Unreviewed;        81 AA.
AC   A0A410UKE7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
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:QAU24723.1};
GN   ORFNames=EO087_12600 {ECO:0000313|EMBL:QAU24723.1};
OS   Dyella sp. M7H15-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=2501295 {ECO:0000313|EMBL:QAU24723.1, ECO:0000313|Proteomes:UP000288967};
RN   [1] {ECO:0000313|EMBL:QAU24723.1, ECO:0000313|Proteomes:UP000288967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M7H15-1 {ECO:0000313|EMBL:QAU24723.1,
RC   ECO:0000313|Proteomes:UP000288967};
RA   Gao Z.-H., Qiu L.-H., Yang Z.;
RT   "Dyella phosphatilytica sp. nov. strain M7H15-1T., a phosphate solubilizing
RT   bacterium isolated from forest soil and analysis of the complete genome
RT   sequence.";
RL   Submitted (JAN-2019) 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; CP035300; QAU24723.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A410UKE7; -.
DR   KEGG; dye:EO087_12600; -.
DR   OrthoDB; 7066617at2; -.
DR   Proteomes; UP000288967; Chromosome.
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:UP000288967};
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..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00236"
FT   REGION          41..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   81 AA;  8980 MW;  C67C771BBDA063DD CRC64;
     MGLDSIWHWA ILLIIILLVF GTGKLTRVGS DLGNAVKGFK KAMQGDEDEE KRKAQEKLQA
     DPPPSENTQA NQNQRDSSES K
//
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