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Database: UniProt
Entry: H5X3R8_9PSEU
LinkDB: H5X3R8_9PSEU
Original site: H5X3R8_9PSEU 
ID   H5X3R8_9PSEU            Unreviewed;       322 AA.
AC   H5X3R8;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=SacmaDRAFT_2842 {ECO:0000313|EMBL:EHR51081.1};
OS   Saccharomonospora marina XMU15.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR51081.1, ECO:0000313|Proteomes:UP000004926};
RN   [1] {ECO:0000313|EMBL:EHR51081.1, ECO:0000313|Proteomes:UP000004926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XMU15 {ECO:0000313|EMBL:EHR51081.1,
RC   ECO:0000313|Proteomes:UP000004926};
RX   PubMed=22768369; DOI=10.4056/sigs.2655905;
RA   Klenk H.P., Lu M., Lucas S., Lapidus A., Copeland A., Pitluck S.,
RA   Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., Land M.,
RA   Ivanova N., Rohde M., Goker M., Detter J.C., Li W.J., Kyrpides N.C.,
RA   Woyke T.;
RT   "Genome sequence of the ocean sediment bacterium Saccharomonospora marina
RT   type strain (XMU15(T)).";
RL   Stand. Genomic Sci. 6:265-275(2012).
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00902}.
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DR   EMBL; CM001439; EHR51081.1; -; Genomic_DNA.
DR   RefSeq; WP_009154466.1; NZ_CM001439.1.
DR   AlphaFoldDB; H5X3R8; -.
DR   STRING; 882083.SacmaDRAFT_2842; -.
DR   eggNOG; COG0805; Bacteria.
DR   HOGENOM; CLU_031942_6_0_11; -.
DR   OrthoDB; 9777044at2; -.
DR   Proteomes; UP000004926; 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 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:UP000004926};
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        41..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        109..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        142..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        188..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        225..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   322 AA;  36130 MW;  8BF70066C7C40813 CRC64;
     MADSPDKRER RGSKRRARSR RHNPDGTMTL IEHIYEFRRR LGFALLALVA GGIVGFLWFS
     NRVGPIPSLG DLVTGPYCAI PPEQRFPKEP PCRLLQTVPF EAFMIQLKVG LTAGAVLFAP
     AWLYQLWAFI APGLYSKERK YALTFVGFAS VLFACGVVLA YFMVPHALEL LTNFGGGAFD
     TWFTGDKYVS FVISLLLIFG VSFELPLLVV MLNRVGVVRY EQLKKWRRGI IFILFVFAAF
     VTPADPFSMI ALAGALTLLF EFALQLTRLH DRKRDRHRAE EGWDRLADDE AAPFDYTPTS
     VDDEPRAKQS GNASNAAPDD VT
//
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