TCYL_ECOLI
ID TCYL_ECOLI Reviewed; 222 AA.
AC P0AFT2; O07985; P76315;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=L-cystine transport system permease protein TcyL {ECO:0000305};
GN Name=tcyL {ECO:0000303|PubMed:26350134}; Synonyms=yecS;
GN OrderedLocusNames=b1918, JW1903;
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 TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, AND SUBUNIT.
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). Responsible for the translocation of the substrate
CC across the membrane (Probable). {ECO:0000269|PubMed:20351115,
CC ECO:0000269|PubMed:25139244, ECO:0000269|PubMed:25837721,
CC ECO:0000269|PubMed:26350134, ECO:0000305}.
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
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
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 (PubMed:25837721). The tcyL-tcyP double mutant cannot grow in
CC the minimal medium containing L-cystine as a sole sulfur source is
CC completely resistant to both L-selenaproline and L-selenocystine
CC (PubMed:25837721, PubMed:25139244). {ECO:0000269|PubMed:25139244,
CC ECO:0000269|PubMed:25837721}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. HisMQ subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC74985.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15738.1; -; Genomic_DNA.
DR PIR; C64955; C64955.
DR RefSeq; NP_416428.1; NC_000913.3.
DR RefSeq; WP_001158220.1; NZ_STEB01000026.1.
DR AlphaFoldDB; P0AFT2; -.
DR SMR; P0AFT2; -.
DR BioGRID; 4261651; 23.
DR ComplexPortal; CPX-4406; L-cystine ABC transporter complex.
DR IntAct; P0AFT2; 1.
DR STRING; 511145.b1918; -.
DR TCDB; 3.A.1.3.10; the atp-binding cassette (abc) superfamily.
DR jPOST; P0AFT2; -.
DR PaxDb; P0AFT2; -.
DR PRIDE; P0AFT2; -.
DR EnsemblBacteria; AAC74985; AAC74985; b1918.
DR EnsemblBacteria; BAA15738; BAA15738; BAA15738.
DR GeneID; 66674192; -.
DR GeneID; 949105; -.
DR KEGG; ecj:JW1903; -.
DR KEGG; eco:b1918; -.
DR PATRIC; fig|1411691.4.peg.331; -.
DR EchoBASE; EB3791; -.
DR eggNOG; COG0765; Bacteria.
DR HOGENOM; CLU_019602_1_4_6; -.
DR InParanoid; P0AFT2; -.
DR OMA; QWEAGYS; -.
DR PhylomeDB; P0AFT2; -.
DR BioCyc; EcoCyc:G7037-MON; -.
DR BioCyc; MetaCyc:G7037-MON; -.
DR PRO; PR:P0AFT2; -.
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:0015184; F:L-cystine transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
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 CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR010065; AA_ABC_transptr_permease_3TM.
DR InterPro; IPR043429; ArtM/GltK/GlnP/TcyL/YhdX-like.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR30614; PTHR30614; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR TIGRFAMs; TIGR01726; HEQRo_perm_3TM; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..222
FT /note="L-cystine transport system permease protein TcyL"
FT /id="PRO_0000060250"
FT TOPO_DOM 1..22
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..182
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 19..207
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 222 AA; 24801 MW; F926C4E00C5145D5 CRC64;
MQESIQLVID SLPFLLKGAG YTLQLSIGGM FFGLLLGFIL ALMRLSPIWP VRWLARFYIS
IFRGTPLIAQ LFMIYYGLPQ FGIELDPIPS AMIGLSLNTA AYAAETLRAA ISSIDKGQWE
AAASIGMTPW QTMRRAILPQ AARVALPPLS NSFISLVKDT SLAATIQVPE LFRQAQLITS
RTLEVFTMYL AASLIYWIMA TVLSTLQNHF ENQLNRQERE PK
