ID   TCYJ_ECOL6              Reviewed;         266 AA.
AC   P0AEN0; P39174;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=L-cystine-binding protein TcyJ {ECO:0000250|UniProtKB:P0AEM9};
DE            Short=CBP {ECO:0000250|UniProtKB:P0AEM9};
DE   AltName: Full=Protein FliY {ECO:0000250|UniProtKB:P0AEM9};
DE   Flags: Precursor;
GN   Name=tcyJ {ECO:0000250|UniProtKB:P0AEM9}; Synonyms=fliY;
GN   OrderedLocusNames=c2335;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Part of the ABC transporter complex TcyJLN involved in L-
CC       cystine import. Binds cystine. {ECO:0000250|UniProtKB:P0AEM9}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (TcyN),
CC       two transmembrane proteins (TcyL) and a solute-binding protein (TcyJ).
CC       {ECO:0000250|UniProtKB:P0AEM9}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P0AEM9}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN80794.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AE014075; AAN80794.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001296168.1; NC_004431.1.
DR   AlphaFoldDB; P0AEN0; -.
DR   SMR; P0AEN0; -.
DR   STRING; 199310.c2335; -.
DR   PRIDE; P0AEN0; -.
DR   DNASU; 1036969; -.
DR   EnsemblBacteria; AAN80794; AAN80794; c2335.
DR   KEGG; ecc:c2335; -.
DR   eggNOG; COG0834; Bacteria.
DR   HOGENOM; CLU_019602_18_5_6; -.
DR   OMA; QPTKWDG; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProt.
DR   GO; GO:0015276; F:ligand-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001320; Iontro_rcpt.
DR   InterPro; IPR018313; SBP_3_CS.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   SMART; SM00062; PBPb; 1.
DR   SMART; SM00079; PBPe; 1.
DR   PROSITE; PS01039; SBP_BACTERIAL_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Periplasm; Signal; Transport.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000250|UniProtKB:P0AEM9"
FT   CHAIN           30..266
FT                   /note="L-cystine-binding protein TcyJ"
FT                   /id="PRO_0000044624"
SQ   SEQUENCE   266 AA;  29039 MW;  1B088DF3F34E5D47 CRC64;
     MKLAHLGRQA LMGVMAVALV AGMSVKSFAD EGLLNKVKER GTLLVGLEGT YPPFSFQGDD
     GKLTGFEVEF AQQLAKHLGV EASLKPTKWD GMLASLDSKR IDVVINQVTI SDERKKKYDF
     STPYTISGIQ ALVKKGNEGT IKTADDLKGK KVGVGLGTNY EEWLRQNVQG VDVRTYDDDP
     TKYQDLRVGR IDAILVDRLA ALDLVKKTND TLAVTGEAFS RQESGVALRK GNEDLLKAVN
     DAIAEMQKDG TLQALSEKWF GADVTK