TCYN_ECOLI
ID TCYN_ECOLI Reviewed; 250 AA.
AC P37774; P76314;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=L-cystine transport system ATP-binding protein TcyN {ECO:0000305};
DE EC=7.4.2.12 {ECO:0000305|PubMed:26350134};
GN Name=tcyN {ECO:0000303|PubMed:26350134}; Synonyms=yecC;
GN OrderedLocusNames=b1917, JW1902;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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=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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 176-250.
RX PubMed=3515318; DOI=10.1093/nar/14.5.2301;
RA Sharma S., Stark T.F., Beattie W.G., Moses R.E.;
RT "Multiple control elements for the uvrC gene unit of Escherichia coli.";
RL Nucleic Acids Res. 14:2301-2318(1986).
RN [5]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [6]
RP FUNCTION.
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 [7]
RP FUNCTION, AND ACTIVITY REGULATION.
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 [8]
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, 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).
RN [10]
RP FUNCTION IN THREONINE EXPORT.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=28911185; DOI=10.1093/femsle/fnx174;
RA Xu Y., Liu Y., Li F., Cao G., Zheng P., Sun J., Wen J., Zhang D.;
RT "Identification of a new gene yecC involved in threonine export in
RT Escherichia coli.";
RL FEMS Microbiol. Lett. 364:0-0(2017).
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). Could also facilitate threonine efflux
CC (PubMed:28911185). Responsible for energy coupling to the transport
CC system (Probable). {ECO:0000269|PubMed:20351115,
CC ECO:0000269|PubMed:25139244, ECO:0000269|PubMed:25837721,
CC ECO:0000269|PubMed:26350134, ECO:0000269|PubMed:28911185, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-cystine(out) = ADP + H(+) + L-cystine(in) +
CC phosphate; Xref=Rhea:RHEA:62576, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:35491,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.4.2.12;
CC Evidence={ECO:0000305|PubMed:26350134};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-cystine(out) + H2O = ADP + D-cystine(in) + H(+) +
CC phosphate; Xref=Rhea:RHEA:62580, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:145813, ChEBI:CHEBI:456216; EC=7.4.2.12;
CC Evidence={ECO:0000305|PubMed:26350134};
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: Cell inner membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Expression is induced by H(2)O(2).
CC {ECO:0000269|PubMed:25837721}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene decreases uptake of
CC cystine. {ECO:0000269|PubMed:25837721}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC74984.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15737.1; -; Genomic_DNA.
DR EMBL; X03691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B64955; B64955.
DR RefSeq; NP_416427.1; NC_000913.3.
DR RefSeq; WP_001272991.1; NZ_LN832404.1.
DR AlphaFoldDB; P37774; -.
DR SMR; P37774; -.
DR BioGRID; 4260366; 18.
DR ComplexPortal; CPX-4406; L-cystine ABC transporter complex.
DR DIP; DIP-11822N; -.
DR IntAct; P37774; 5.
DR STRING; 511145.b1917; -.
DR TCDB; 3.A.1.3.10; the atp-binding cassette (abc) superfamily.
DR jPOST; P37774; -.
DR PaxDb; P37774; -.
DR PRIDE; P37774; -.
DR EnsemblBacteria; AAC74984; AAC74984; b1917.
DR EnsemblBacteria; BAA15737; BAA15737; BAA15737.
DR GeneID; 946422; -.
DR KEGG; ecj:JW1902; -.
DR KEGG; eco:b1917; -.
DR PATRIC; fig|1411691.4.peg.332; -.
DR EchoBASE; EB2251; -.
DR eggNOG; COG1126; Bacteria.
DR HOGENOM; CLU_000604_1_22_6; -.
DR InParanoid; P37774; -.
DR OMA; EGTTMLM; -.
DR PhylomeDB; P37774; -.
DR BioCyc; EcoCyc:EG12347-MON; -.
DR BioCyc; MetaCyc:EG12347-MON; -.
DR PRO; PR:P37774; -.
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:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015424; F:ABC-type amino acid transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0015184; F:L-cystine transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:1903712; P:cysteine transmembrane transport; IC:ComplexPortal.
DR GO; GO:0015811; P:L-cystine transport; IDA:EcoCyc.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR030679; ABC_ATPase_HisP-typ.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR PIRSF; PIRSF039085; ABC_ATPase_HisP; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; ATP-binding; Cell inner membrane; Cell membrane;
KW Membrane; Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..250
FT /note="L-cystine transport system ATP-binding protein TcyN"
FT /id="PRO_0000093166"
FT DOMAIN 4..244
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 250 AA; 27677 MW; F05E07F160121C60 CRC64;
MSAIEVKNLV KKFHGQTVLH GIDLEVKPGE VVAIIGPSGS GKTTLLRSIN LLEQPEAGTI
TVGDITIDTA RSLSQQKSLI RQLRQHVGFV FQNFNLFPHR TVLENIIEGP VIVKGEPKEE
ATARARELLA KVGLAGKETS YPRRLSGGQQ QRVAIARALA MRPEVILFDE PTSALDPELV
GEVLNTIRQL AQEKRTMVIV THEMSFARDV ADRAIFMDQG RIVEQGAAKA LFADPEQPRT
RQFLEKFLLQ
