GenomeNet

Database: UniProt
Entry: A0A399G6S2_9ACTN
LinkDB: A0A399G6S2_9ACTN
Original site: A0A399G6S2_9ACTN 
ID   A0A399G6S2_9ACTN        Unreviewed;       270 AA.
AC   A0A399G6S2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
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   ECO:0000313|EMBL:UOE21991.1};
GN   ORFNames=NI17_010925 {ECO:0000313|EMBL:UOE21991.1}, NI17_01115
GN   {ECO:0000313|EMBL:RII04278.1};
OS   Thermobifida halotolerans.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=483545 {ECO:0000313|EMBL:RII04278.1};
RN   [1] {ECO:0000313|EMBL:RII04278.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44931 {ECO:0000313|EMBL:RII04278.1};
RA   Toth A., Tancsics T.A., Farkas T., Papp P., Olasz F., Balint B.,
RA   Herczeg R., Nagy I., Baka E., Kukolya J.;
RT   "De novo genome project of the cellulose decomposer Thermobifida
RT   halotolerans type strain.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:UOE21991.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 44931 {ECO:0000313|EMBL:UOE21991.1};
RA   Nagy I., Horvath B., Kukolya J., Nagy I., Orsini M.;
RT   "De novo genome project of the cellulose decomposer Thermobifida
RT   halotolerans type strain.";
RL   Submitted (OCT-2020) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JRUV01000069; RII04278.1; -; Genomic_DNA.
DR   EMBL; CP063196; UOE21991.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A399G6S2; -.
DR   STRING; 483545.GCA_001660385_04598; -.
DR   OrthoDB; 9777044at2; -.
DR   Proteomes; UP000265719; 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:UP000265719};
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        14..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        67..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        105..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        152..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        190..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   REGION          242..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   270 AA;  30034 MW;  0F398B5259304318 CRC64;
     MPLMDHLREL RNRVIKALVF VALGMGVGFT VFEPVWDFLQ RPYCSLPAEV RNDDGCGLNY
     TGIFDGFFLY FQVSLIVGLL VSSPFWLYQL WAFIAPALRG KEKRYTYLFV GFAVPLFLLG
     ATVAYFVTAK GMEIMFSFAP EGATALITLP NYLGYIIMML AVFGAAFVLP LIVVLLNFLG
     VLPHRMIAKW RRVIIFLAFV FAAIATPGGD PFTMLALGIP VVALFEIAEL IAFVNDRRRG
     RDRDPLAELD DDELSPLDDA DSAAGTTPNR
//
DBGET integrated database retrieval system