ID C6WSZ1_METML Unreviewed; 249 AA.
AC C6WSZ1;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=Mmol_0323 {ECO:0000313|EMBL:ACT47233.1};
OS Methylotenera mobilis (strain JLW8 / ATCC BAA-1282 / DSM 17540).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylotenera.
OX NCBI_TaxID=583345 {ECO:0000313|EMBL:ACT47233.1, ECO:0000313|Proteomes:UP000002742};
RN [1] {ECO:0000313|Proteomes:UP000002742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540
RC {ECO:0000313|Proteomes:UP000002742};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M., Chistoserdova L.;
RT "Complete sequence of Methylotenera mobilis JLW8.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACT47233.1, ECO:0000313|Proteomes:UP000002742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540
RC {ECO:0000313|Proteomes:UP000002742};
RX PubMed=21622745; DOI=10.1128/JB.00404-11;
RA Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT "Genomes of three methylotrophs from a single niche uncover genetic and
RT metabolic divergence of Methylophilaceae.";
RL J. Bacteriol. 193:3757-3764(2011).
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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00902}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00902}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the TatC family. {ECO:0000256|HAMAP-
CC Rule:MF_00902}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00902}.
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DR EMBL; CP001672; ACT47233.1; -; Genomic_DNA.
DR RefSeq; WP_015831275.1; NC_012968.1.
DR AlphaFoldDB; C6WSZ1; -.
DR STRING; 583345.Mmol_0323; -.
DR KEGG; mmb:Mmol_0323; -.
DR eggNOG; COG0805; Bacteria.
DR HOGENOM; CLU_031942_1_1_4; -.
DR OrthoDB; 9777044at2; -.
DR Proteomes; UP000002742; Chromosome.
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; IPR019820; Sec-indep_translocase_CS.
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.
DR PROSITE; PS01218; TATC; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00902};
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:UP000002742};
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 21..46
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 66..87
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 108..135
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 155..181
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 193..216
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
SQ SEQUENCE 249 AA; 27142 MW; 043829CC56D039DC CRC64;
MTPTENFISH LIELRNRLLR IVAGFILVFI ALFPFANEIY ALLAAPLLSK LPAGGQMIAT
AVTTPFFVPM KVAMMAAFLL SLPHTLYQIW SFVAPGLYAH EKKFMIPIIL ASSFLFLSGM
AFAYFLVFPV IFGFIVGTAP AGVAVMTDIG NYLDFIITLF CAFGLAFEVP IAVVMAARFG
WVSISALKEA RGYVVVGAFV IAAVVTPPDV ISQFMLAMPM WLLYELGIVV ARFTAAKEDE
SEPTILPPA
//
