ID A0A2W7NFN7_9RHOB Unreviewed; 298 AA.
AC A0A2W7NFN7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, 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=LX81_00942 {ECO:0000313|EMBL:PZX18313.1};
OS Palleronia aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Palleronia.
OX NCBI_TaxID=568105 {ECO:0000313|EMBL:PZX18313.1, ECO:0000313|Proteomes:UP000248916};
RN [1] {ECO:0000313|EMBL:PZX18313.1, ECO:0000313|Proteomes:UP000248916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22009 {ECO:0000313|EMBL:PZX18313.1,
RC ECO:0000313|Proteomes:UP000248916};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JUN-2018) 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. 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 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:PZX18313.1}.
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DR EMBL; QKZL01000003; PZX18313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W7NFN7; -.
DR OrthoDB; 9777044at2; -.
DR Proteomes; UP000248916; 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:UP000248916};
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 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 76..103
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 115..137
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 180..201
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 213..230
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT REGION 275..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..291
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 298 AA; 32789 MW; B71844D9A783F08B CRC64;
MSAEDDIDDS SAPLIEHLAE LRTRLIRSVA AFIVGMVISF TVATPIFNFL TAPLCEALAQ
RGQDCDLIFI SPQEGFFVAI KVSLLGGLFL AFPIIATQLW RFVAPGLYRS ERGAFLPFLL
ASPFMFVMGA AFAFYVVTPL AYDFFLGFQQ FGAQGEALTP EASAPLSVVF QGSAQEYLNL
TIKFIVSFGL CFQLPVLLTL MGKAGLVSSR GLADVRKYAV VGILVLAALV TPPDVITQVI
LFIVVYGLYE ISIFLVRRVE KKRTEELRAE GVLGPDEELY DYDDDLDDAE PEDETKRP
//
