ID A0A0S8AUJ4_9BACT Unreviewed; 260 AA.
AC A0A0S8AUJ4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 16.
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=AMK71_00215 {ECO:0000313|EMBL:KPK03015.1};
OS Nitrospira bacterium SG8_35_4.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704025 {ECO:0000313|EMBL:KPK03015.1, ECO:0000313|Proteomes:UP000050997};
RN [1] {ECO:0000313|EMBL:KPK03015.1, ECO:0000313|Proteomes:UP000050997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_35_4 {ECO:0000313|EMBL:KPK03015.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK03015.1}.
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DR EMBL; LJTM01000002; KPK03015.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8AUJ4; -.
DR PATRIC; fig|1704025.3.peg.78; -.
DR Proteomes; UP000050997; 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 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 17..35
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 80..101
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 122..146
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 166..195
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 207..223
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
SQ SEQUENCE 260 AA; 29363 MW; 961243D81FCD7D1C CRC64;
MDKAPLTEHL GELRNRILIS LIAVAVSFAG SFYYSETLFS ILISPLHNTL SFSLDNPYIS
IVPGKNPDLE LVFLAPAEAI WMHIKMAFIC AFIISSPIIF FEIWRFVAPG LMEQEKKYAL
PFVFTTTFLF LIGALFCFVI ILPFAMNFLL TYKTENLKPM LSVGKYVDFC LKFILAFGAI
FELPVVTVFA TRMGIVTPDF LAKNRKYAVL IAFVLAALLT PTPDAFNQSL MAVPMIILYE
VGIWASKFLD RKKKKKGIQK
//
