ID C3MWS0_SULIM Unreviewed; 294 AA.
AC C3MWS0;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, 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 OrderedLocusNames=M1425_1622 {ECO:0000313|EMBL:ACP38370.1};
OS Sulfolobus islandicus (strain M.14.25 / Kamchatka #1).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=427317 {ECO:0000313|EMBL:ACP38370.1, ECO:0000313|Proteomes:UP000001350};
RN [1] {ECO:0000313|EMBL:ACP38370.1, ECO:0000313|Proteomes:UP000001350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.14.25 / Kamchatka #1 {ECO:0000313|Proteomes:UP000001350};
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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.
CC {ECO:0000256|HAMAP-Rule:MF_00902}.
CC -!- SUBUNIT: Forms a complex with TatA. {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; CP001400; ACP38370.1; -; Genomic_DNA.
DR RefSeq; WP_010922999.1; NC_012588.1.
DR AlphaFoldDB; C3MWS0; -.
DR GeneID; 84061977; -.
DR KEGG; sia:M1425_1622; -.
DR HOGENOM; CLU_031942_3_2_2; -.
DR Proteomes; UP000001350; 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|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 30..53
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 147..179
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 199..221
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 233..249
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
SQ SEQUENCE 294 AA; 33405 MW; 163A76543C4698BF CRC64;
MTERTREVEK LEERPLIEHL RELAYRLRRI LIALAITFMI YFMLGLELVR VYLPYPFFGL
KYVLAEVPVL YPSLFDSISV QLTQLFIYNE LPKGVKLIII NLFDPLFASF YISLYLAIFT
TIPIIVREIW AFVAPGLYEH EKKLFKSIIF PAFLLFALGS AFAYFLLIPL MLRIILLYAT
ALGSAVEPTL GLRSFVSTVM TLLIATGLSF ELPLIMGGLT GVGVVKSITW LKNWRWGVLV
SFIIAWIISP GTTGGIIETV IGITLSTLYF IGALISKFME KGRKKESQKT LERI
//