ID A0A0A0DFY1_9STRE Unreviewed; 235 AA.
AC A0A0A0DFY1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ORFNames=SSIN_1281 {ECO:0000313|EMBL:KGM36980.1};
OS Streptococcus sinensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=176090 {ECO:0000313|EMBL:KGM36980.1, ECO:0000313|Proteomes:UP000030019};
RN [1] {ECO:0000313|EMBL:KGM36980.1, ECO:0000313|Proteomes:UP000030019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKU4 {ECO:0000313|EMBL:KGM36980.1,
RC ECO:0000313|Proteomes:UP000030019};
RA Teng J.L., Huang Y., Tse H., Lau S.K., Woo P.C.;
RL Submitted (JUN-2014) 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.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGM36980.1}.
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DR EMBL; JPEN01000070; KGM36980.1; -; Genomic_DNA.
DR RefSeq; WP_037616980.1; NZ_JPEN01000070.1.
DR AlphaFoldDB; A0A0A0DFY1; -.
DR STRING; 176090.SSIN_1281; -.
DR PATRIC; fig|176090.4.peg.1242; -.
DR eggNOG; COG0805; Bacteria.
DR Proteomes; UP000030019; 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:SF4; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATCD; 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 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 61..88
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 100..127
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 147..176
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 188..206
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 212..229
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
SQ SEQUENCE 235 AA; 26896 MW; 011B2B73EB2AF45B CRC64;
MSSKEQTVVE HLTEFRWRFI AVLIWFGLIF LVSLLFAANI YKWLTASFEQ KLIVLGPDDI
LWIYISLASL VAFSLTLPFM VYQIWEFIRP ALRNSEAKAI FAYIPATFFS FVLGLAFGFY
FVSPAILQVL LSLGDGLFAV QMTAQNYLSF LFHTTIPIAC LFELPVIVAF LTSIGLLKPQ
FLIKYRRYAY FVLLVLAVIL TPADFISDLS MTVPLILLYE VSILLSKMIE KRRIS
//
