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TATC_MYCLE
ID   TATC_MYCLE              Reviewed;         310 AA.
AC   P54078; Q9CC36; Q9S373;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Sec-independent protein translocase protein TatC {ECO:0000255|HAMAP-Rule:MF_00902};
GN   Name=tatC {ECO:0000255|HAMAP-Rule:MF_00902}; Synonyms=mttB;
GN   OrderedLocusNames=ML1332; ORFNames=B2126_C1_183, MLCB2533.28, u2126a;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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:0000255|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:0000255|HAMAP-Rule:MF_00902}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00902};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00902}.
CC   -!- SIMILARITY: Belongs to the TatC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00902}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17191.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAC31713.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U00017; AAA17191.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL035310; CAA22942.1; -; Genomic_DNA.
DR   EMBL; AL583921; CAC31713.1; ALT_INIT; Genomic_DNA.
DR   PIR; F87075; F87075.
DR   PIR; S72851; S72851.
DR   AlphaFoldDB; P54078; -.
DR   SMR; P54078; -.
DR   STRING; 272631.ML1332; -.
DR   EnsemblBacteria; CAC31713; CAC31713; CAC31713.
DR   KEGG; mle:ML1332; -.
DR   Leproma; ML1332; -.
DR   eggNOG; COG0805; Bacteria.
DR   HOGENOM; CLU_031942_6_0_11; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR30371; PTHR30371; 1.
DR   Pfam; PF00902; TatC; 1.
DR   PRINTS; PR01840; TATCFAMILY.
DR   TIGRFAMs; TIGR00945; tatC; 1.
DR   PROSITE; PS01218; TATC; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Protein transport; Reference proteome;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..310
FT                   /note="Sec-independent protein translocase protein TatC"
FT                   /id="PRO_0000098089"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT   REGION          291..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   310 AA;  34536 MW;  74362D5AD9C3E96F CRC64;
     MRACDLLKRI KQHYRRSRTN PDATMSLIDH LTELRTRLLI SLAAIVVTTI FGFIWYSHSI
     FGLESLGEWL RRPYCSLPQS ARADISPDGQ CRLLATAPFD QFMLRIKVGM AAGIVLASPV
     WFYQLWAFIT PGLYTKERRF TVAFVVPAAV LFAGGTVLAY LVLSKALGFL LIVGSGVQVT
     ALSGDRYFGF LLNLLVVFGV SFEFPLLIVM LNIAGLLTYQ RLKSWRRGLI FAMFVFAAVF
     TPGSDPFSMT ALGAALTVLL ELAIQLVRLH DKRRVKHEAL IADDEASVIE PPSSIPERSY
     TATRSHDDVT
 
 
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