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Database: UniProt
Entry: V3PT31_9ENTR
LinkDB: V3PT31_9ENTR
Original site: V3PT31_9ENTR 
ID   V3PT31_9ENTR            Unreviewed;       256 AA.
AC   V3PT31;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=L370_01129 {ECO:0000313|EMBL:ESN15100.1};
OS   Enterobacter sp. MGH 24.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=1329828 {ECO:0000313|EMBL:ESN15100.1, ECO:0000313|Proteomes:UP000017624};
RN   [1] {ECO:0000313|EMBL:ESN15100.1, ECO:0000313|Proteomes:UP000017624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGH 24 {ECO:0000313|EMBL:ESN15100.1,
RC   ECO:0000313|Proteomes:UP000017624};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Murphy C., Cosimi L., Cerqueira G., Feldgarden M., Hung D., Onderdonk A.B.,
RA   Ferraro M.J., Hooper D., Dekker J., O'Brien T., Huang S., Quan V.,
RA   Ernst C., Delaney M., DuBois A., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Enterobacter cloacae complex MGH 24.";
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. 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:ESN15100.1}.
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DR   EMBL; AYJG01000003; ESN15100.1; -; Genomic_DNA.
DR   RefSeq; WP_023309607.1; NZ_KI535657.1.
DR   AlphaFoldDB; V3PT31; -.
DR   GeneID; 75135806; -.
DR   PATRIC; fig|1329828.3.peg.1108; -.
DR   HOGENOM; CLU_031942_1_1_6; -.
DR   Proteomes; UP000017624; 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; 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 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        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        74..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        116..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        157..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        195..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        218..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
SQ   SEQUENCE   256 AA;  28518 MW;  4E4DD8B9A462FF3A CRC64;
     MAVDDTQPLI THLIELRKRL LNCIIAVLLI FLCLVYFAND IYQVVSAPLI KQMPLGATMI
     ATDVASPFFT PIKLTFWVSL IASAPVILYQ VWAFVAPALY KHERKLVIPL LVSSSLLFYI
     GMAFAYFVVF PLAFGFLTHT APEGVQVSTD IASYLSFVMA LFMAFGVAFE VPVAIVLLCW
     VGVTTPDDLR KKRPYILVGA FVVGMLLTPP DVFSQTLLAI PMYCLFEVGV FFSRFYVGKG
     RRADDEDDTS DKTTEE
//
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