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Database: UniProt
Entry: I3TKT7_TISMK
LinkDB: I3TKT7_TISMK
Original site: I3TKT7_TISMK 
ID   I3TKT7_TISMK            Unreviewed;        82 AA.
AC   I3TKT7;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
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:AFK53375.1};
GN   OrderedLocusNames=TMO_1536 {ECO:0000313|EMBL:AFK53375.1};
OS   Tistrella mobilis (strain KA081020-065).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK53375.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK53375.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK53375.1,
RC   ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(2012).
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 inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00236}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00236}.
CC   -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000256|HAMAP-
CC       Rule:MF_00236}.
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DR   EMBL; CP003236; AFK53375.1; -; Genomic_DNA.
DR   RefSeq; WP_014745053.1; NC_017956.1.
DR   AlphaFoldDB; I3TKT7; -.
DR   STRING; 1110502.TMO_1536; -.
DR   KEGG; tmo:TMO_1536; -.
DR   PATRIC; fig|1110502.3.peg.1583; -.
DR   eggNOG; COG1826; Bacteria.
DR   HOGENOM; CLU_086034_5_0_5; -.
DR   Proteomes; UP000005258; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_00236};
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:UP000005258};
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          40..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   82 AA;  8925 MW;  EB98E13FCF734979 CRC64;
     MSIGIWQIVL ILVLVLILFG AGKLPRVMGD VAKGIKSFKA GMKDEETENN SSSSQDPKVL
     NKPQDARMAD EVRRDEVSGP KA
//
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