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Database: UniProt
Entry: D7GEA7_PROFC
LinkDB: D7GEA7_PROFC
Original site: D7GEA7_PROFC 
ID   D7GEA7_PROFC            Unreviewed;       290 AA.
AC   D7GEA7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
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:CBL56868.1};
GN   OrderedLocusNames=PFREUD_13510 {ECO:0000313|EMBL:CBL56868.1};
OS   Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM
OS   4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=754252 {ECO:0000313|EMBL:CBL56868.1, ECO:0000313|Proteomes:UP000000936};
RN   [1] {ECO:0000313|EMBL:CBL56868.1, ECO:0000313|Proteomes:UP000000936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1
RC   {ECO:0000313|Proteomes:UP000000936};
RX   PubMed=20668525; DOI=10.1371/journal.pone.0011748;
RA   Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S.,
RA   Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P.,
RA   Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., Gaillardin C.,
RA   Lortal S.;
RT   "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy
RT   actinobacterium with food and probiotic applications.";
RL   PLoS ONE 5:E11748-E11748(2010).
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; FN806773; CBL56868.1; -; Genomic_DNA.
DR   RefSeq; WP_013161236.1; NC_014215.1.
DR   AlphaFoldDB; D7GEA7; -.
DR   STRING; 754252.PFREUD_13510; -.
DR   GeneID; 61221996; -.
DR   KEGG; pfr:PFREUD_13510; -.
DR   eggNOG; COG0805; Bacteria.
DR   HOGENOM; CLU_031942_6_0_11; -.
DR   Proteomes; UP000000936; 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   HAMAP; MF_00902; TatC; 1.
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.
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|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW   Rule:MF_00902}; Reference proteome {ECO:0000313|Proteomes:UP000000936};
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        52..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        120..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        151..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        197..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        233..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        256..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   290 AA;  32036 MW;  637B0BAECB27FD3B CRC64;
     MAITVDEKAG DGSQEAAPGK KRRRLHLLPK SWRPPEPAAD GSMELVDHLR ELRYRVIVSI
     LAVLAVALCC FIFYNQLTAV AFHPIQQAIE VYRAKNPGAE VEITTTNVTG GFTLFMKVPF
     IAGFILSCPV WLYQLWAFIA PGLLSNERRA AIRFLGTSIP LFLTGVLLGY WISPKGFAVL
     LQFNPPGVLN LNDANEFLTF ELTLLLVFGV SFLLPVVLVT LNRFGIISGA GLGKFRSMAI
     FLCFLFSAVA TPSTDPISMC VLAVPMSFLY VIAEVLCKRH DKRQVAEQQQ
//
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