DLST_ECOLI
ID DLST_ECOLI Reviewed; 443 AA.
AC P42628; Q2M997; Q6BF46;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable serine transporter;
GN Name=dlsT; Synonyms=yhaO; OrderedLocusNames=b3110, JW5519;
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 / 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 [2]
RP SEQUENCE REVISION.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
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 SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
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, INDUCTION BY CYSTEINE, OPERON, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=27435271; DOI=10.1099/mic.0.000337;
RA Shimada T., Tanaka K., Ishihama A.;
RT "Transcription factor DecR (YbaO) controls detoxification of L-cysteine in
RT Escherichia coli.";
RL Microbiology 162:1698-1707(2016).
CC -!- FUNCTION: Plays a role in L-cysteine detoxification (PubMed:27435271).
CC May transport both D- and L-serine (By similarity).
CC {ECO:0000250|UniProtKB:Q8XAF5, ECO:0000269|PubMed:27435271}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein.
CC -!- INDUCTION: Transcription induced by L-cysteine (in vivo), under control
CC of DecR. Member of the dlsT(yhaO)-yhaM operon.
CC {ECO:0000269|PubMed:16397293}.
CC -!- DISRUPTION PHENOTYPE: No change in sensitivity to excess L-cysteine.
CC Cells produce about 15% of wild-type levels of hydrogen sulfide in the
CC presence of excess cysteine. {ECO:0000269|PubMed:27435271}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC SdaC/TdcC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57914.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE77159.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U18997; AAA57914.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAT48168.3; -; Genomic_DNA.
DR EMBL; AP009048; BAE77159.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000401598.1; NZ_STEB01000001.1.
DR RefSeq; YP_026203.3; NC_000913.3.
DR AlphaFoldDB; P42628; -.
DR SMR; P42628; -.
DR BioGRID; 4259267; 129.
DR STRING; 511145.b3110; -.
DR TCDB; 2.A.42.2.4; the hydroxy/aromatic amino acid permease (haaap) family.
DR PaxDb; P42628; -.
DR PRIDE; P42628; -.
DR EnsemblBacteria; AAT48168; AAT48168; b3110.
DR EnsemblBacteria; BAE77159; BAE77159; BAE77159.
DR GeneID; 66672988; -.
DR GeneID; 947628; -.
DR KEGG; ecj:JW5519; -.
DR KEGG; eco:b3110; -.
DR PATRIC; fig|1411691.4.peg.3619; -.
DR EchoBASE; EB2609; -.
DR eggNOG; COG0814; Bacteria.
DR HOGENOM; CLU_052043_3_0_6; -.
DR OMA; FPGSWAT; -.
DR PhylomeDB; P42628; -.
DR BioCyc; EcoCyc:YHAO-MON; -.
DR PRO; PR:P42628; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0009093; P:cysteine catabolic process; IMP:UniProtKB.
DR GO; GO:1901367; P:response to L-cysteine; IEP:EcoCyc.
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..443
FT /note="Probable serine transporter"
FT /id="PRO_0000093817"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..110
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..182
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..264
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 443 AA; 48315 MW; B24A2D8E1A61E631 CRC64;
MEIASNKGVI ADASTPAGRA GMSESEWREA IKFDSTDTGW VIMSIGMAIG AGIVFLPVQV
GLMGLWVFLL SSVIGYPAMY LFQRLFINTL AESPECKDYP SVISGYLGKN WGILLGALYF
VMLVIWMFVY STAITNDSAS YLHTFGVTEG LLSDSPFYGL VLICILVAIS SRGEKLLFKI
STGMVLTKLL VVAALGVSMV GMWHLYNVGS LPPLGLLVKN AIITLPFTLT SILFIQTLSP
MVISYRSREK SIEVARHKAL RAMNIAFGIL FVTVFFYAVS FTLAMGHDEA VKAYEQNISA
LAIAAQFISG DGAAWVKVVS VILNIFAVMT AFFGVYLGFR EATQGIVMNI LRRKMPAEKI
NENLVQRGIM IFAILLAWSA IVLNAPVLSF TSICSPIFGM VGCLIPAWLV YKVPALHKYK
GMSLYLIIVT GLLLCVSPFL AFS
