ID A0A073K7U9_9BACI Unreviewed; 247 AA.
AC A0A073K7U9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, 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=BAMA_05975 {ECO:0000313|EMBL:KEK18328.1};
OS Bacillus manliponensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=574376 {ECO:0000313|EMBL:KEK18328.1, ECO:0000313|Proteomes:UP000027822};
RN [1] {ECO:0000313|EMBL:KEK18328.1, ECO:0000313|Proteomes:UP000027822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15802 {ECO:0000313|EMBL:KEK18328.1,
RC ECO:0000313|Proteomes:UP000027822};
RA Lai Q., Liu Y., Shao Z.;
RT "Draft genome sequence of Bacillus manliponensis JCM 15802 (MCCC
RT 1A00708).";
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:KEK18328.1}.
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DR EMBL; JOTN01000015; KEK18328.1; -; Genomic_DNA.
DR RefSeq; WP_034641225.1; NZ_JOTN01000015.1.
DR AlphaFoldDB; A0A073K7U9; -.
DR STRING; 574376.BAMA_05975; -.
DR eggNOG; COG0805; Bacteria.
DR OrthoDB; 9777044at2; -.
DR Proteomes; UP000027822; 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 Reference proteome {ECO:0000313|Proteomes:UP000027822};
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..205
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 211..230
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
SQ SEQUENCE 247 AA; 28057 MW; D1841A5A7DA1B924 CRC64;
MNDQEMSVVE HLGELRKRLI ITALSFLVFL IVGFSYTKEI YQFIVKDLDM KLTVLGPSDI
LWIYFVIAAV FSIVCTIPIA ALQLWLFVKP ALLPHEQRAT ILYIPALFLL FIGGLCFGYF
IILPFVLQFL IGLGSDMFQT MFTTEKYFSF VMNMTVPFAV IFELPVIAMF LTSIGILNPV
LLQQVRRYAY FVLIVIAVCI TPPDFVSDFA VAIPLLVIYE LSITVSKFVY NRKLKKELQS
SSQSASV
//