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Database: UniProt
Entry: A0A1H0NTU4_9MICO
LinkDB: A0A1H0NTU4_9MICO
Original site: A0A1H0NTU4_9MICO 
ID   A0A1H0NTU4_9MICO        Unreviewed;        95 AA.
AC   A0A1H0NTU4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN04489867_1033 {ECO:0000313|EMBL:SDO95895.1};
OS   Pedococcus dokdonensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Pedococcus.
OX   NCBI_TaxID=443156 {ECO:0000313|EMBL:SDO95895.1, ECO:0000313|Proteomes:UP000199077};
RN   [1] {ECO:0000313|Proteomes:UP000199077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22329 {ECO:0000313|Proteomes:UP000199077};
RA   Varghese N., Submissions S.;
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; LT629711; SDO95895.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0NTU4; -.
DR   STRING; 443156.SAMN04489867_1033; -.
DR   OrthoDB; 5245163at2; -.
DR   Proteomes; UP000199077; Chromosome i.
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};
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   REGION          44..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   95 AA;  10251 MW;  12AD2F956E835E4E CRC64;
     MRGLFEGWHL IILLVLLVVL FGFKRLPDAA RSIGRSMRIF KSEVEEMKQD GKSAASSDTV
     KGETVKDAGA SPGTEGTNPI REDNTPRTDN SSGAS
//
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