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Database: UniProt
Entry: F2RDX1_STRVP
LinkDB: F2RDX1_STRVP
Original site: F2RDX1_STRVP 
ID   F2RDX1_STRVP            Unreviewed;       315 AA.
AC   F2RDX1;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
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=SVEN_1224 {ECO:0000313|EMBL:CCA54511.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA54511.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA54511.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC   PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(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 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}.
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DR   EMBL; FR845719; CCA54511.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2RDX1; -.
DR   STRING; 953739.SVEN_1224; -.
DR   KEGG; sve:SVEN_1224; -.
DR   PATRIC; fig|953739.5.peg.3288; -.
DR   eggNOG; COG0805; Bacteria.
DR   HOGENOM; CLU_031942_6_0_11; -.
DR   OrthoDB; 9777044at2; -.
DR   Proteomes; UP000006854; 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; 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|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW   Rule:MF_00902}; Reference proteome {ECO:0000313|Proteomes:UP000006854};
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..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        88..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        123..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        172..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        207..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   REGION          258..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   315 AA;  33660 MW;  B83831CF355B594E CRC64;
     MPKSARKQEK DPEGRMPLVE HLRELRNRLA KGLLAVAAVT IVALVYSEEL MQFLTKSVPT
     CAPGVSSNGG NCAIVSFNTL MAPFSTTIQL SLTAGLVVAS PVWLYQLWAF VAPGLHKSEK
     KYTYAFVGAA VPLFSAGAYL AYLILPISVK VLISLTPEGS ANILSLGDVL DFTLRMVLVF
     GLAFELPLVL VMLNLTGVLT GRRMAGWWRG VIMGVFVFGA VITPTTDPVG MIALAGPITV
     LYFGAVAFSL LNDRRRKRNN PDAELDDDEA SSLDLTPETV GAVEPVGASR ALPEQATGEH
     GGTGAHRVNG YDDIT
//
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