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Database: UniProt
Entry: Q3YAF1_PSEYM
LinkDB: Q3YAF1_PSEYM
Original site: Q3YAF1_PSEYM 
ID   Q3YAF1_PSEYM            Unreviewed;       266 AA.
AC   Q3YAF1;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Sec-independent protein translocase protein TatC {ECO:0000256|HAMAP-Rule:MF_00902};
GN   Name=tatC {ECO:0000256|HAMAP-Rule:MF_00902,
GN   ECO:0000313|EMBL:AAZ75670.1};
GN   ORFNames=AC507_1393 {ECO:0000313|EMBL:KPB69444.1};
OS   Pseudomonas syringae pv. maculicola.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=59511 {ECO:0000313|EMBL:AAZ75670.1};
RN   [1] {ECO:0000313|EMBL:AAZ75670.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ES4326 {ECO:0000313|EMBL:AAZ75670.1};
RA   Caldelari I., Mann S., Crooks C., Palmer T.;
RT   "Repertoire of virulence factors secreted by the tat pathway in Pseudomonas
RT   syringae.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KPB69444.1, ECO:0000313|Proteomes:UP000037920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YM7930 {ECO:0000313|EMBL:KPB69444.1,
RC   ECO:0000313|Proteomes:UP000037920};
RA   O'Brien H.E., Thakur S., Gong Y., Wang P.W., Guttman D.S.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KPB69444.1, ECO:0000313|Proteomes:UP000037920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YM7930 {ECO:0000313|EMBL:KPB69444.1,
RC   ECO:0000313|Proteomes:UP000037920};
RA   Mott G.A., Thakur S., Wang P.W., Desveaux D., Guttman D.S.;
RT   "Comparative genomics and high-throughput reverse genetic screens identify
RT   a new phytobacterial MAMP and an Arabidopsis receptor required for immune
RT   elicitation.";
RL   Submitted (OCT-2015) 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. Together with
CC       TatB, TatC is part of a receptor directly interacting with Tat signal
CC       peptides. {ECO:0000256|HAMAP-Rule:MF_00902}.
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_00902}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00902};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00902}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the TatC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00902}.
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DR   EMBL; DQ148412; AAZ75670.1; -; Genomic_DNA.
DR   EMBL; LGLD01000062; KPB69444.1; -; Genomic_DNA.
DR   RefSeq; WP_007252837.1; NZ_LGLD01000062.1.
DR   AlphaFoldDB; Q3YAF1; -.
DR   GeneID; 64468011; -.
DR   PATRIC; fig|59511.10.peg.1433; -.
DR   Proteomes; UP000037920; 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   HAMAP; MF_00902; TatC; 1.
DR   InterPro; IPR019820; Sec-indep_translocase_CS.
DR   InterPro; IPR002033; TatC.
DR   NCBIfam; TIGR00945; tatC; 1.
DR   PANTHER; PTHR30371; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATC; 1.
DR   PANTHER; PTHR30371:SF0; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATC, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00902; TatC; 1.
DR   PRINTS; PR01840; TATCFAMILY.
DR   PROSITE; PS01218; TATC; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00902};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00902};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_00902};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_00902};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00902};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00902}; Transport {ECO:0000256|HAMAP-Rule:MF_00902}.
FT   TRANSMEM        25..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        79..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        112..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        162..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        200..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        223..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   REGION          246..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   266 AA;  29842 MW;  82A6C7235867215F CRC64;
     MSADIPENDQ QMPLISHLTE LRTRLLRCVA AVFLIFAGLF YFTQKIYTLV SAPLRVYLPE
     GATMIATDVA SPFITPFKLT MMVALFLSMP VILHQIWGFI APGLYKHEKR VAIPLLVSSI
     ILFYAGMAFA YFLVFPIIFH FFASVTPEGV SMMTDIASYL DFVMTLFFAF GVAFEIPVAV
     VLLVWIGVVD VKYLKKIRPY VIIGCFVVGM ILTPPDIFSQ TLLAVPMWLL FELGILCSTM
     IKKRGEHPDD QVEDTDKPDQ PPATTP
//
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