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Database: UniProt
Entry: D2AC13_SHIF2
LinkDB: D2AC13_SHIF2
Original site: D2AC13_SHIF2 
ID   D2AC13_SHIF2            Unreviewed;       258 AA.
AC   D2AC13;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
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:ADA76217.1};
GN   OrderedLocusNames=SFxv_4269 {ECO:0000313|EMBL:ADA76217.1};
OS   Shigella flexneri serotype X (strain 2002017).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=591020 {ECO:0000313|EMBL:ADA76217.1, ECO:0000313|Proteomes:UP000001884};
RN   [1] {ECO:0000313|EMBL:ADA76217.1, ECO:0000313|Proteomes:UP000001884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2002017 {ECO:0000313|EMBL:ADA76217.1,
RC   ECO:0000313|Proteomes:UP000001884};
RX   PubMed=19955273; DOI=10.1128/JCM.00614-09;
RA   Ye C., Lan R., Xia S., Zhang J., Sun Q., Zhang S., Jing H., Wang L., Li Z.,
RA   Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., Luo X.,
RA   Bai X., Wang Y., Wang P., Xu Q., Xu J.;
RT   "Emergence of a new multidrug-resistant serotype X variant in an epidemic
RT   clone of Shigella flexneri.";
RL   J. Clin. Microbiol. 48:419-426(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 inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00902}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00902}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the TatC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00902}.
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DR   EMBL; CP001383; ADA76217.1; -; Genomic_DNA.
DR   RefSeq; WP_000109947.1; NC_017328.1.
DR   AlphaFoldDB; D2AC13; -.
DR   KEGG; sfe:SFxv_4269; -.
DR   PATRIC; fig|591020.3.peg.4574; -.
DR   HOGENOM; CLU_031942_1_1_6; -.
DR   Proteomes; UP000001884; 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; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_00902};
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        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        74..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        116..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        157..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        195..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        218..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
SQ   SEQUENCE   258 AA;  28866 MW;  D1F4F08663ADA81C CRC64;
     MSVEDTQPLI THLIELRKRL LNCIIAVIVI FLCLVYFAND IYHLVSAPLI KQLPQGSTMI
     ATDVASPFFT PIKLTFMVSL ILSAPVILYQ VWAFIAPALY KHERRLVVPL LVSSSLLFYI
     GMAFAYFVVF PLAFGFLANT APEGVQVSTD IASYLSFVMA LFMAFGVSFE VPVAIVLLCW
     MGITSSEDLR KKRPYVLVGA FVVGMLLTPP DVFSQTLLAI PMYCLFEIGV FFSRFYVGKG
     RNREEENDAE AESEKTEE
//
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