TCYJ_ECOLI
ID TCYJ_ECOLI Reviewed; 266 AA.
AC P0AEM9; P39174;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=L-cystine-binding protein TcyJ {ECO:0000305};
DE Short=CBP;
DE AltName: Full=Protein FliY;
DE AltName: Full=Sulfate starvation-induced protein 7;
DE Short=SSI7;
DE Flags: Precursor;
GN Name=tcyJ {ECO:0000303|PubMed:26350134};
GN Synonyms=fliY {ECO:0000303|PubMed:8550423}, yzzR;
GN OrderedLocusNames=b1920, JW1905;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / RP437;
RX PubMed=8550423; DOI=10.1128/jb.178.1.24-34.1996;
RA Mytelka D.S., Chamberlin M.J.;
RT "Escherichia coli fliAZY operon.";
RL J. Bacteriol. 178:24-34(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 30-59, AND FUNCTION.
RX PubMed=8450713; DOI=10.1016/0024-3205(93)90103-a;
RA Butler J.D., Levin S.W., Facchiano A., Miele L., Mukherjee A.B.;
RT "Amino acid composition and N-terminal sequence of purified cystine binding
RT protein of Escherichia coli.";
RL Life Sci. 52:1209-1215(1993).
RN [6]
RP PROTEIN SEQUENCE OF 30-41.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP PROTEIN SEQUENCE OF 30-39; 143-148; 183-187 AND 249-266.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8774726; DOI=10.1111/j.1432-1033.1996.0773u.x;
RA Quadroni M., Staudenmann W., Kertesz M.A., James P.;
RT "Analysis of global responses by protein and peptide fingerprinting of
RT proteins isolated by two-dimensional gel electrophoresis. Application to
RT the sulfate-starvation response of Escherichia coli.";
RL Eur. J. Biochem. 239:773-781(1996).
RN [8]
RP FUNCTION.
RC STRAIN=W;
RX PubMed=4564569; DOI=10.1016/s0021-9258(19)44579-1;
RA Berger E.A., Heppel L.A.;
RT "A binding protein involved in the transport of cystine and diaminopimelic
RT acid in Escherichia coli.";
RL J. Biol. Chem. 247:7684-7694(1972).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20351115; DOI=10.1074/jbc.m109.081356;
RA Ohtsu I., Wiriyathanawudhiwong N., Morigasaki S., Nakatani T., Kadokura H.,
RA Takagi H.;
RT "The L-cysteine/L-cystine shuttle system provides reducing equivalents to
RT the periplasm in Escherichia coli.";
RL J. Biol. Chem. 285:17479-17487(2010).
RN [10]
RP FUNCTION, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=25139244; DOI=10.1111/jam.12623;
RA Deutch C.E., Spahija I., Wagner C.E.;
RT "Susceptibility of Escherichia coli to the toxic L-proline analogue L-
RT selenaproline is dependent on two L-cystine transport systems.";
RL J. Appl. Microbiol. 117:1487-1499(2014).
RN [11]
RP FUNCTION, SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25837721; DOI=10.1371/journal.pone.0120619;
RA Ohtsu I., Kawano Y., Suzuki M., Morigasaki S., Saiki K., Yamazaki S.,
RA Nonaka G., Takagi H.;
RT "Uptake of L-cystine via an ABC transporter contributes defense of
RT oxidative stress in the L-cystine export-dependent manner in Escherichia
RT coli.";
RL PLoS ONE 10:E0120619-E0120619(2015).
RN [12]
RP FUNCTION, SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26350134; DOI=10.1128/jb.00277-15;
RA Chonoles Imlay K.R., Korshunov S., Imlay J.A.;
RT "Physiological roles and adverse effects of the two cystine importers of
RT Escherichia coli.";
RL J. Bacteriol. 197:3629-3644(2015).
CC -!- FUNCTION: Part of the ABC transporter complex TcyJLN involved in L-
CC cystine import (PubMed:25139244, PubMed:20351115, PubMed:25837721,
CC PubMed:26350134). This high affinity cystine transporter is involved in
CC resistance to oxidative stress by forming a L-cysteine/L-cystine
CC shuttle system with the EamA transporter, which exports L-cysteine as
CC reducing equivalents to the periplasm to prevent the cells from
CC oxidative stress. Exported L-cysteine can reduce the periplasmic
CC hydrogen peroxide to water, and then generated L-cystine is imported
CC back into the cytoplasm via the TcyJLN complex (PubMed:20351115,
CC PubMed:25837721). Functions at low cystine concentrations
CC (PubMed:26350134). The system can also transport L-cysteine,
CC diaminopimelic acid (DAP), djenkolate, lanthionine, D-cystine,
CC homocystine, and it mediates accumulation of the toxic compounds L-
CC selenaproline (SCA) and L-selenocystine (SeCys) (PubMed:25139244,
CC PubMed:26350134). Binds cystine and DAP (PubMed:4564569,
CC PubMed:8450713). {ECO:0000269|PubMed:20351115,
CC ECO:0000269|PubMed:25139244, ECO:0000269|PubMed:25837721,
CC ECO:0000269|PubMed:26350134, ECO:0000269|PubMed:4564569,
CC ECO:0000269|PubMed:8450713}.
CC -!- ACTIVITY REGULATION: The TcyJLN system is inhibited by L-cystine, L-
CC cysteine, DL-2,6-diaminopimelic acid and L-cystathionine, and is
CC stimulated by D-cysteine. {ECO:0000269|PubMed:25139244}.
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:0000305|PubMed:25837721, ECO:0000305|PubMed:26350134}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:20351115}.
CC -!- INDUCTION: Transcription is controlled by CysB (PubMed:26350134).
CC Expression is highly induced by H(2)O(2) (PubMed:25837721,
CC PubMed:20351115). Induced by sulfate (PubMed:26350134). Also slightly
CC induced by exogenous L-cysteine (PubMed:20351115).
CC {ECO:0000269|PubMed:20351115, ECO:0000269|PubMed:25837721,
CC ECO:0000269|PubMed:26350134}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene significantly impairs
CC intracellular uptake of L-cystine (PubMed:25837721, PubMed:20351115).
CC Mutants show a higher sensitivity to H(2)O(2) than wild-type cells
CC (PubMed:20351115). The tcyJ-tcyP double mutant is unable to import
CC cystine and is completely resistant to both L-selenaproline and L-
CC selenocystine (PubMed:25139244, PubMed:26350134). The double disruption
CC of eamA and tcyJ increases cellular levels of lipid peroxides
CC (PubMed:25837721). {ECO:0000269|PubMed:20351115,
CC ECO:0000269|PubMed:25139244, ECO:0000269|PubMed:25837721,
CC ECO:0000269|PubMed:26350134}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC {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; U18539; AAC43545.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74987.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15740.1; -; Genomic_DNA.
DR PIR; E64955; E64955.
DR RefSeq; NP_416430.1; NC_000913.3.
DR RefSeq; WP_001296168.1; NZ_SSUV01000013.1.
DR AlphaFoldDB; P0AEM9; -.
DR SMR; P0AEM9; -.
DR BioGRID; 4261251; 71.
DR ComplexPortal; CPX-4406; L-cystine ABC transporter complex.
DR DIP; DIP-47980N; -.
DR IntAct; P0AEM9; 9.
DR STRING; 511145.b1920; -.
DR TCDB; 3.A.1.3.10; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P0AEM9; -.
DR jPOST; P0AEM9; -.
DR PaxDb; P0AEM9; -.
DR PRIDE; P0AEM9; -.
DR EnsemblBacteria; AAC74987; AAC74987; b1920.
DR EnsemblBacteria; BAA15740; BAA15740; BAA15740.
DR GeneID; 948833; -.
DR KEGG; ecj:JW1905; -.
DR KEGG; eco:b1920; -.
DR PATRIC; fig|511145.12.peg.2002; -.
DR EchoBASE; EB2545; -.
DR eggNOG; COG0834; Bacteria.
DR HOGENOM; CLU_019602_18_5_6; -.
DR InParanoid; P0AEM9; -.
DR OMA; QPTKWDG; -.
DR PhylomeDB; P0AEM9; -.
DR BioCyc; EcoCyc:G7039-MON; -.
DR BioCyc; MetaCyc:G7039-MON; -.
DR PRO; PR:P0AEM9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0016597; F:amino acid binding; IDA:EcoCyc.
DR GO; GO:0015184; F:L-cystine transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IEA:InterPro.
DR GO; GO:1903712; P:cysteine transmembrane transport; IC:ComplexPortal.
DR GO; GO:0015811; P:L-cystine transport; IDA:EcoCyc.
DR GO; GO:0006791; P:sulfur utilization; IEP:EcoCyc.
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 1: Evidence at protein level;
KW Amino-acid transport; Direct protein sequencing; Periplasm;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:8450713,
FT ECO:0000269|PubMed:8774726, ECO:0000269|PubMed:9298646"
FT CHAIN 30..266
FT /note="L-cystine-binding protein TcyJ"
FT /id="PRO_0000031755"
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
