ID   TATC_ECOL6              Reviewed;         258 AA.
AC   Q8FBI6;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Sec-independent protein translocase protein TatC {ECO:0000255|HAMAP-Rule:MF_00902};
GN   Name=tatC {ECO:0000255|HAMAP-Rule:MF_00902}; Synonyms=mttB;
GN   OrderedLocusNames=c4787;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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:0000255|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:0000255|HAMAP-Rule:MF_00902}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00902}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00902}.
CC   -!- SIMILARITY: Belongs to the TatC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00902}.
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DR   EMBL; AE014075; AAN83220.1; -; Genomic_DNA.
DR   RefSeq; WP_000109949.1; NC_004431.1.
DR   AlphaFoldDB; Q8FBI6; -.
DR   SMR; Q8FBI6; -.
DR   STRING; 199310.c4787; -.
DR   EnsemblBacteria; AAN83220; AAN83220; c4787.
DR   KEGG; ecc:c4787; -.
DR   eggNOG; COG0805; Bacteria.
DR   HOGENOM; CLU_031942_1_1_6; -.
DR   OMA; EMSFLDH; -.
DR   BioCyc; ECOL199310:C4787-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR30371; PTHR30371; 1.
DR   Pfam; PF00902; TatC; 1.
DR   PRINTS; PR01840; TATCFAMILY.
DR   TIGRFAMs; TIGR00945; tatC; 1.
DR   PROSITE; PS01218; TATC; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..258
FT                   /note="Sec-independent protein translocase protein TatC"
FT                   /id="PRO_0000098084"
FT   TOPO_DOM        2..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT   TOPO_DOM        45..75
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT   TOPO_DOM        97..115
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT   TOPO_DOM        137..156
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT   TOPO_DOM        178..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT   TOPO_DOM        211
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT   TOPO_DOM        233..258
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   258 AA;  28892 MW;  E799459206463A55 CRC64;
     MSVEDTQPLI THLIELRKRL LNCIISVIVI FLCLVYFAND IYHLVSAPLI KQLPQGSTMI
     ATDVASPFFT PIKLTFMVSL ILSAPVILYQ VWAFIAPALY KHERRLVVPL LVSSSLLFYI
     GMAFAYFVVF PLAFGFLANT APEGVQVSTD IASYLSFVMA LFMAFGVSFE VPVAIVLLCW
     MGITSPEDLR KKRPYVLVGA FVVGMLLTPP DVFSQTLLAI PMYCLFEIGV FFSRFYVGKG
     RNREEENDAE AESEKTEE