ID A0A0A2MM38_9FLAO Unreviewed; 265 AA.
AC A0A0A2MM38;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=Q766_08810 {ECO:0000313|EMBL:KGO93389.1};
OS Flavobacterium subsaxonicum WB 4.1-42 = DSM 21790.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1121898 {ECO:0000313|EMBL:KGO93389.1, ECO:0000313|Proteomes:UP000030111};
RN [1] {ECO:0000313|EMBL:KGO93389.1, ECO:0000313|Proteomes:UP000030111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB 4.1-42 {ECO:0000313|EMBL:KGO93389.1,
RC ECO:0000313|Proteomes:UP000030111};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) 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:KGO93389.1}.
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DR EMBL; JRLY01000005; KGO93389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2MM38; -.
DR STRING; 1121898.GCA_000422725_02115; -.
DR eggNOG; COG0805; Bacteria.
DR OrthoDB; 9777044at2; -.
DR Proteomes; UP000030111; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000030111};
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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 89..112
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 124..146
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 179..201
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 213..228
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 234..252
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
SQ SEQUENCE 265 AA; 30151 MW; FF491222ACFA25A4 CRC64;
MSFLDHLEEL RWLLVRSTIA ILIGACVAFA FSEYIFNNII FAPKRADFIT YRFFCDLANK
YDLDKSFCVT ELPFSIQSRT MDGQFSTDIW TSITAGLILA FPFILFQVWK FIRPALYDTE
RKHAVGFIVS TSILFFLGVL FGYYLIMPLS LNFLGNYKIS DVVENNIDLD SYLSLIKTTV
ISCGLVFEMP IIIFFLAKLG LVTAGFLRKY RKYAFVIILI IAAIVTPPDV VSQMIVTIPL
VILYEVSILI AGRMNKTPKI EETNG
//