DLST_ECO57
ID DLST_ECO57 Reviewed; 443 AA.
AC Q8XAF5; Q7AAM0;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Serine transporter;
GN Name=dlsT {ECO:0000303|PubMed:26727373}; Synonyms=yhaO;
GN OrderedLocusNames=ECs3991, Z4463;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP FUNCTION IN D-SERINE TRANSPORT, FUNCTION IN VIRULENCE, BIOPHYSICOCHEMICAL
RP PROPERTIES, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=26727373; DOI=10.1371/journal.ppat.1005359;
RA Connolly J.P., Gabrielsen M., Goldstone R.J., Grinter R., Wang D.,
RA Cogdell R.J., Walker D., Smith D.G., Roe A.J.;
RT "A highly conserved bacterial D-serine uptake system links host metabolism
RT and virulence.";
RL PLoS Pathog. 12:E1005359-E1005359(2016).
CC -!- FUNCTION: Transports both D- and L-serine; allows growth of strain
CC CFT073 cells normally unable to transport D-serine on that substrate.
CC Transport relies on the H(+) gradient and is not competed by L-
CC threonine (PubMed:26727373). May play a role in L-cysteine
CC detoxification (By similarity). {ECO:0000250|UniProtKB:P42628,
CC ECO:0000269|PubMed:26727373}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=65.56 uM for D-serine {ECO:0000269|PubMed:26727373};
CC Vmax=30.2 nmol/min/mg enzyme {ECO:0000269|PubMed:26727373};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P42628, ECO:0000255,
CC ECO:0000305|PubMed:26727373}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: 40-fold induced under conditions that maximally induce
CC expression of the locus of effacement (LEE) large pathogenicity island
CC (PAI); part of the dlsT-yhaM operon. 3-fold induced by D-serine during
CC mid to late exponential growth. {ECO:0000269|PubMed:26727373}.
CC -!- DISRUPTION PHENOTYPE: Decreased secretion of a number of substrates for
CC the type III secretion system (TTSS) encoded in the locus of effacement
CC (LEE) including Tir, EspA and EspD; at least EspD is also decreased
CC intracellularly. Expression of 105 genes is altered; down-regulation of
CC LEE PAI (including the TTSS) plus other genes as well as up-regulation
CC of 21 genes. Decreased ability to form attachment/effacing lesions on
CC HeLa cells; those which form attachments condense host actin less well
CC (pedestal formation) (PubMed:26727373). {ECO:0000269|PubMed:26727373}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC SdaC/TdcC subfamily. {ECO:0000305}.
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DR EMBL; AE005174; AAG58242.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37414.1; -; Genomic_DNA.
DR PIR; F85972; F85972.
DR PIR; G91127; G91127.
DR RefSeq; NP_312018.1; NC_002695.1.
DR RefSeq; WP_000401586.1; NZ_SEKU01000004.1.
DR AlphaFoldDB; Q8XAF5; -.
DR SMR; Q8XAF5; -.
DR STRING; 155864.EDL933_4332; -.
DR EnsemblBacteria; AAG58242; AAG58242; Z4463.
DR EnsemblBacteria; BAB37414; BAB37414; ECs_3991.
DR GeneID; 916166; -.
DR KEGG; ece:Z4463; -.
DR KEGG; ecs:ECs_3991; -.
DR PATRIC; fig|386585.9.peg.4165; -.
DR eggNOG; COG0814; Bacteria.
DR HOGENOM; CLU_052043_3_0_6; -.
DR OMA; FPGSWAT; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042942; P:D-serine transport; IDA:UniProtKB.
DR GO; GO:0032329; P:serine transport; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Virulence.
FT CHAIN 1..443
FT /note="Serine transporter"
FT /id="PRO_0000437257"
FT TRANSMEM 38..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 443 AA; 48323 MW; 670BF2991168F1FA 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 FIIVFFYAVS FTLAMGHDEA VKAYEQNISA
LAIAAQFISG DGAAWVKVVS VILNIFAVMT AFFGVYLGFR EATQGIVMNI LRRKMPAEKI
NENLVQRGIM IFAILLAWSA IVLNAPVLSF TSICSPIFGL VGCLIPAWLV YKVPALHKYK
GMSLYLIIVT GLLLCVSPFL AFS
