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Database: UniProt
Entry: A0A0P1FG35_THAGE
LinkDB: A0A0P1FG35_THAGE
Original site: A0A0P1FG35_THAGE 
ID   A0A0P1FG35_THAGE        Unreviewed;       306 AA.
AC   A0A0P1FG35;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
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:CUH66888.1};
GN   ORFNames=TG4357_02699 {ECO:0000313|EMBL:CUH66888.1};
OS   Thalassovita gelatinovora (Thalassobius gelatinovorus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Thalassovita.
OX   NCBI_TaxID=53501 {ECO:0000313|EMBL:CUH66888.1, ECO:0000313|Proteomes:UP000051587};
RN   [1] {ECO:0000313|EMBL:CUH66888.1, ECO:0000313|Proteomes:UP000051587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 4357 {ECO:0000313|EMBL:CUH66888.1,
RC   ECO:0000313|Proteomes:UP000051587};
RG   Swine Surveillance;
RL   Submitted (SEP-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; CYSA01000025; CUH66888.1; -; Genomic_DNA.
DR   RefSeq; WP_058263407.1; NZ_FOFW01000005.1.
DR   AlphaFoldDB; A0A0P1FG35; -.
DR   STRING; 53501.SAMN04488043_105236; -.
DR   OrthoDB; 9777044at2; -.
DR   Proteomes; UP000051587; 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; 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|HAMAP-Rule:MF_00902};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051587};
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        28..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        116..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        191..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        225..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   REGION          275..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..306
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   306 AA;  33554 MW;  37E80253B23FB0DA CRC64;
     MTNTDDLDDS SAPLIEHLAE LRTRLIRALI AFIIGMVICF SFGGAILDFL LIPIEKTMRD
     LGNPNPVMQY TAPQEYFFTL IRISMVGGLA LAFPVIAHQL WRFVAPGLYR KEKSAFLPFL
     IASPALFLLG ASFAHFVVIP LAMAFFLGFS DFPSFVSALL SGEDVAQTVD SGIDIVFNGK
     VNETLDITLK MIVAFGLCFQ LPVLLTLMGK AGLATAAGLR STRKYAVVGI LVVAALVTPP
     DVTTQVILFV VVYGLYEISI FLVARVETKR EDTLRAEGYY DDEDEEDDPL MAEFDADDEA
     DSEDKA
//
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