DSDX_ECOL6
ID DSDX_ECOL6 Reviewed; 445 AA.
AC A0A0H2VAP9;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=D-serine transporter DsdX {ECO:0000303|PubMed:16952954};
DE AltName: Full=D-serine-specific permease {ECO:0000303|PubMed:16952954};
GN Name=dsdX; OrderedLocusNames=c2900;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=16952954; DOI=10.1128/jb.00634-06;
RA Anfora A.T., Welch R.A.;
RT "DsdX is the second D-serine transporter in uropathogenic Escherichia coli
RT clinical isolate CFT073.";
RL J. Bacteriol. 188:6622-6628(2006).
CC -!- FUNCTION: Protein that allows transport of D-serine across the inner
CC membrane, does not transport D-alanine nor probably glycine. Is
CC probably a H(+) symporter, as CCCP inhibits transport. Transports D-
CC serine more efficiently than CycA. {ECO:0000269|PubMed:16952954}.
CC -!- ACTIVITY REGULATION: Uptake of D-serine is inhibited by carbonyl
CC cyanide m-chlorophenylhydrazone (CCCP), and at high concentrations of
CC D-threonine, stimulated by D-cycloserine and not affected by D-alanine
CC or glycine. {ECO:0000269|PubMed:16952954}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=58.75 uM for D-serine {ECO:0000269|PubMed:16952954};
CC Vmax=75.96 nmol/min/mg enzyme {ECO:0000269|PubMed:16952954};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P08555}; Multi-pass membrane protein.
CC -!- DISRUPTION PHENOTYPE: Single deletion, grows on D-serine, D-serine plus
CC glycerol and D-alanine. A double dsdX-cycA deletion grows in D-serine
CC plus glycerol, but not D-serine or D-alanine alone, growth on D-serine
CC (but not D-alanine) is restored by dsdX, while growth on both D-alanine
CC and D-serine is restored by cycA. Double dsdX-cycA deletion cannot take
CC up D-serine. {ECO:0000269|PubMed:16952954}.
CC -!- MISCELLANEOUS: E.coli CFT073, a uropathogenic strain (UPEC), was
CC originally isolated from urine, which has a high concentration of D-
CC serine. D-serine is toxic to bacteria. The abililty to take up D-serine
CC coupled with the activity of D-serine dehydratase (dsdA) may allow use
CC of this amino acid as a carbon source in a sugar-poor environment.
CC {ECO:0000305|PubMed:16952954}.
CC -!- SIMILARITY: Belongs to the GntP permease family. {ECO:0000305}.
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DR EMBL; AE014075; AAN81350.1; -; Genomic_DNA.
DR RefSeq; WP_000556042.1; NC_004431.1.
DR AlphaFoldDB; A0A0H2VAP9; -.
DR STRING; 199310.c2900; -.
DR EnsemblBacteria; AAN81350; AAN81350; c2900.
DR KEGG; ecc:c2900; -.
DR eggNOG; COG2610; Bacteria.
DR HOGENOM; CLU_027949_0_0_6; -.
DR OMA; YFGMTVK; -.
DR Proteomes; UP000001410; 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:0042945; F:D-serine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015128; F:gluconate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042942; P:D-serine transport; IDA:UniProtKB.
DR InterPro; IPR003474; Glcn_transporter.
DR PANTHER; PTHR30354; PTHR30354; 1.
DR Pfam; PF02447; GntP_permease; 1.
DR PIRSF; PIRSF002746; Gluconate_transporter; 1.
DR TIGRFAMs; TIGR00791; gntP; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..445
FT /note="D-serine transporter DsdX"
FT /id="PRO_0000439179"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 445 AA; 47107 MW; 6BB0DA8CB0B3923E CRC64;
MHSQIWVVST LLISIVLIVL TIVKFKFHPF LALLLASFFV GTMMGMGPLD MVNAIESGIG
GTLGFLAAVI GLGTILGKMM EVSGAAERIG LTLQRCRWLS ADVIMVLVGL ICGITLFVEV
GVVLLIPLAF SIAKKTNTSL LKLAIPLCTA LMAVHCVVPP HPAALYVANK LGADIGSVIV
YGLLVGLMAS LIGGPLFLKF LGQRLPFKPV PTEFADLKVR DEKTLPSLGA TLFTVLLPIA
LMLVKTIAEL NMARESGLYT LLEFIGNPIT ATFIAVFVAY YVLGIRQHMS MGTMLTHTEN
GFGSIANILL IIGAGGAFNA ILKSSSLADT LAVILSNMHM HPILLAWLVA LILHAAVGSA
TVAMMGATAI VAPMLPLYPD ISPEIIAIAI GSGAIGCTIV TDSLFWLVKQ YCGATLNETF
KYYTTATFIA SVIALAGTFL LSFII
