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Database: UniProt
Entry: A0A0F3M5U4_ORITS
LinkDB: A0A0F3M5U4_ORITS
Original site: A0A0F3M5U4_ORITS 
ID   A0A0F3M5U4_ORITS        Unreviewed;       255 AA.
AC   A0A0F3M5U4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
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:KJV51098.1};
GN   ORFNames=GILLIAM_01735 {ECO:0000313|EMBL:SPR08630.1}, OTSGILL_2530
GN   {ECO:0000313|EMBL:KJV51098.1};
OS   Orientia tsutsugamushi str. Gilliam.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Orientia.
OX   NCBI_TaxID=1359184 {ECO:0000313|EMBL:KJV51098.1, ECO:0000313|Proteomes:UP000033769};
RN   [1] {ECO:0000313|EMBL:KJV51098.1, ECO:0000313|Proteomes:UP000033769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gilliam {ECO:0000313|EMBL:KJV51098.1,
RC   ECO:0000313|Proteomes:UP000033769};
RA   Daugherty S.C., Su Q., Abolude K., Beier-Sexton M., Carlyon J.A.,
RA   Carter R., Day N.P., Dumler S.J., Dyachenko V., Godinez A., Kurtti T.J.,
RA   Lichay M., Mullins K.E., Ott S., Pappas-Brown V., Paris D.H., Patel P.,
RA   Richards A.L., Sadzewicz L., Sears K., Seidman D., Sengamalay N.,
RA   Stenos J., Tallon L.J., Vincent G., Fraser C.M., Munderloh U.,
RA   Dunning-Hotopp J.C.;
RT   "Genome Sequencing of Rickettsiales.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SPR08630.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gilliam {ECO:0000313|EMBL:SPR08630.1};
RA   Keele B.F.;
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000244959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gilliam {ECO:0000313|Proteomes:UP000244959};
RA   Batty M. E., Batty M E.;
RL   Submitted (MAR-2018) 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; LANO01000055; KJV51098.1; -; Genomic_DNA.
DR   EMBL; LS398551; SPR08630.1; -; Genomic_DNA.
DR   RefSeq; WP_011944753.1; NZ_LS398551.1.
DR   GeneID; 66652597; -.
DR   PATRIC; fig|1359184.3.peg.2448; -.
DR   Proteomes; UP000033769; Unassembled WGS sequence.
DR   Proteomes; UP000244959; 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   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   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        21..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        77..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        119..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        163..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        201..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
SQ   SEQUENCE   255 AA;  29295 MW;  3B1C90F4ACF02872 CRC64;
     MQTMNSKTYT LGEHLAELKV RILKVLICFF LACGISYYYS KNIYHFLTIP LKNILPDQNH
     RIIYTGLAEG FFTYLQLSFY TGFLIIIPIL SAQIYLFIAP GLYKSEKIYF KILMFMSPIL
     FYIGNLFVFY FVIPNACHFF LGFESLKENE LPIVLEARMS EYLTLLIQFS LAFGISFELP
     LILITLNVLN IISISTLIQK RRIAIVLNFI IAAILTPPDI LSQFALATPL ILLYEASIII
     CKILKLRTNA GHKMD
//
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