ID TCYP_ECOLI Reviewed; 463 AA.
AC P77529;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 27-MAR-2024, entry version 160.
DE RecName: Full=L-cystine transporter TcyP {ECO:0000305};
DE AltName: Full=S-sulfocysteine transporter {ECO:0000303|PubMed:27481704};
GN Name=tcyP {ECO:0000303|PubMed:26350134}; Synonyms=ydjN;
GN OrderedLocusNames=b1729, JW1718;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
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 [3]
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 [4]
RP FUNCTION, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, AND CATALYTIC
RP ACTIVITY.
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 [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, AND
RP CATALYTIC ACTIVITY.
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 [6]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
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).
RN [7]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=27481704; DOI=10.1093/femsle/fnw185;
RA Yamazaki S., Takei K., Nonaka G.;
RT "ydjN encodes an S-sulfocysteine transporter required by Escherichia coli
RT for growth on S-sulfocysteine as a sulfur source.";
RL FEMS Microbiol. Lett. 363:0-0(2016).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=28533366; DOI=10.1073/pnas.1703576114;
RA Mironov A., Seregina T., Nagornykh M., Luhachack L.G., Korolkova N.,
RA Lopes L.E., Kotova V., Zavilgelsky G., Shakulov R., Shatalin K., Nudler E.;
RT "Mechanism of H2S-mediated protection against oxidative stress in
RT Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:6022-6027(2017).
CC -!- FUNCTION: Involved in L-cystine import (PubMed:25139244,
CC PubMed:25837721, PubMed:26350134, PubMed:27481704). Low affinity L-
CC cystine transporter that is mainly involved in L-cystine uptake from
CC outside as a nutrient (PubMed:25837721). Is the primary transporter at
CC high concentrations of cystine (PubMed:26350134). Probably functions as
CC a proton symporter (Probable). Can also transport D-cystine, cysteine
CC and homocystine as a methionine precursor (PubMed:25139244,
CC PubMed:26350134). Mediates accumulation of the toxic compounds L-
CC selenaproline (SCA) and L-selenocystine (SeCys) (PubMed:25139244). Can
CC also transport S-sulfocysteine and is required for growth on S-
CC sulfocysteine as a sulfur source (PubMed:27481704). Plays the principal
CC role in the 3-mercaptopyruvate sulfurtransferase (3MST)-mediated
CC generation of endogenous hydrogen sulfide (H2S) (PubMed:28533366).
CC {ECO:0000269|PubMed:25139244, ECO:0000269|PubMed:25837721,
CC ECO:0000269|PubMed:26350134, ECO:0000269|PubMed:27481704,
CC ECO:0000269|PubMed:28533366, ECO:0000305|PubMed:26350134}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-cystine(out) = H(+)(in) + L-cystine(in);
CC Xref=Rhea:RHEA:66172, ChEBI:CHEBI:15378, ChEBI:CHEBI:35491;
CC Evidence={ECO:0000269|PubMed:25139244, ECO:0000269|PubMed:25837721,
CC ECO:0000269|PubMed:26350134};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66173;
CC Evidence={ECO:0000269|PubMed:25139244, ECO:0000269|PubMed:25837721,
CC ECO:0000269|PubMed:26350134};
CC -!- ACTIVITY REGULATION: Inhibited by L-cystine and L-cysteine, and to a
CC lesser extent by D-cystine. {ECO:0000269|PubMed:25139244}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 uM for cystine {ECO:0000269|PubMed:25837721};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Transcription is controlled by CysB (PubMed:26350134,
CC PubMed:27481704, PubMed:28533366). Highly expressed in sulfate medium
CC and repressed in cystine medium (PubMed:26350134).
CC {ECO:0000269|PubMed:26350134, ECO:0000269|PubMed:27481704,
CC ECO:0000269|PubMed:28533366}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene decreases uptake of
CC cystine (PubMed:25837721). The mutant cannot grow on S-sulfocysteine
CC (PubMed:27481704). The tcyP-tcyJ double mutant is unable to import
CC cystine (PubMed:26350134, PubMed:27481704). The tcyP-tcyL double mutant
CC cannot grow in the minimal medium containing L-cystine as a sole sulfur
CC source (PubMed:25837721). The tcyP-tcyJ and tcyP-tcyL double mutants
CC are completely resistant to both L-selenaproline and L-selenocystine
CC (PubMed:25139244). {ECO:0000269|PubMed:25139244,
CC ECO:0000269|PubMed:25837721, ECO:0000269|PubMed:26350134,
CC ECO:0000269|PubMed:27481704}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. {ECO:0000305}.
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DR EMBL; U00096; AAC74799.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15509.1; -; Genomic_DNA.
DR PIR; A64932; A64932.
DR RefSeq; NP_416243.1; NC_000913.3.
DR RefSeq; WP_001010696.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P77529; -.
DR SMR; P77529; -.
DR BioGRID; 4259522; 189.
DR DIP; DIP-11776N; -.
DR STRING; 511145.b1729; -.
DR TCDB; 2.A.23.1.8; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
DR jPOST; P77529; -.
DR PaxDb; 511145-b1729; -.
DR EnsemblBacteria; AAC74799; AAC74799; b1729.
DR GeneID; 946238; -.
DR KEGG; ecj:JW1718; -.
DR KEGG; eco:b1729; -.
DR PATRIC; fig|1411691.4.peg.527; -.
DR EchoBASE; EB3746; -.
DR eggNOG; COG1823; Bacteria.
DR HOGENOM; CLU_019375_0_1_6; -.
DR InParanoid; P77529; -.
DR OMA; GIMFVVH; -.
DR OrthoDB; 7778689at2; -.
DR PhylomeDB; P77529; -.
DR BioCyc; EcoCyc:G6934-MONOMER; -.
DR BioCyc; MetaCyc:G6934-MONOMER; -.
DR PRO; PR:P77529; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015184; F:L-cystine transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0000099; F:sulfur amino acid transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015811; P:L-cystine transport; IDA:EcoCyc.
DR GO; GO:0000101; P:sulfur amino acid transport; IDA:EcoCyc.
DR GO; GO:0006791; P:sulfur utilization; IMP:EcoCyc.
DR Gene3D; 1.10.3860.10; Sodium:dicarboxylate symporter; 1.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR PANTHER; PTHR42865:SF5; L-CYSTINE TRANSPORTER TCYP; 1.
DR PANTHER; PTHR42865; PROTON/GLUTAMATE-ASPARTATE SYMPORTER; 1.
DR Pfam; PF00375; SDF; 1.
DR PRINTS; PR00173; EDTRNSPORT.
DR SUPFAM; SSF118215; Proton glutamate symport protein; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..463
FT /note="L-cystine transporter TcyP"
FT /id="PRO_0000202121"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 463 AA; 48662 MW; 7D45D8A354D2885C CRC64;
MNFPLIANIV VFVVLLFALA QTRHKQWSLA KKVLVGLVMG VVFGLALHTI YGSDSQVLKD
SVQWFNIVGN GYVQLLQMIV MPLVFASILS AVARLHNASQ LGKISFLTIG TLLFTTLIAA
LVGVLVTNLF GLTAEGLVQG GAETARLNAI ESNYVGKVSD LSVPQLVLSF IPKNPFADLT
GANPTSIISV VIFAAFLGVA ALKLLKDDAP KGERVLAAID TLQSWVMKLV RLVMQLTPYG
VLALMTKVVA GSNLQDIIKL GSFVVASYLG LLIMFAVHGI LLGINGVSPL KYFRKVWPVL
TFAFTSRSSA ASIPLNVEAQ TRRLGVPESI ASFAASFGAT IGQNGCAGLY PAMLAVMVAP
TVGINPLDPM WIATLVGIVT VSSAGVAGVG GGATFAALIV LPAMGLPVTL VALLISVEPL
IDMGRTALNV SGSMTAGTLT SQWLKQTDKA ILDSEDDAEL AHH
//
