CYCA_ECOL6
ID CYCA_ECOL6 Reviewed; 470 AA.
AC A0A0H2VDI7;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=D-serine/D-alanine/glycine transporter;
GN Name=cycA; OrderedLocusNames=c5307;
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).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=23316042; DOI=10.1128/jb.01598-12;
RA Baisa G., Stabo N.J., Welch R.A.;
RT "Characterization of Escherichia coli D-cycloserine transport and resistant
RT mutants.";
RL J. Bacteriol. 195:1389-1399(2013).
CC -!- FUNCTION: Permease that is involved in the transport across the
CC cytoplasmic membrane of D-alanine, D-serine and glycine
CC (PubMed:16952954, PubMed:23316042). Is the only transporter of D-
CC alanine (PubMed:16952954). Transports D-serine less efficiently than
CC DsdX (PubMed:16952954). In addition, in minimal media, transports the
CC broad spectrum antibiotic D-cycloserine into the cell
CC (PubMed:23316042). Transports D-cycloserine only in minimal media, and
CC not in a complex medium, suggesting that CycA does not play a role in
CC D-cycloserine transport when E.coli is grown in a complex or
CC biologically relevant medium, probably due to competition from other
CC CycA substrates present in the medium (PubMed:23316042).
CC {ECO:0000269|PubMed:16952954, ECO:0000269|PubMed:23316042}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-alanine(in) + H(+)(in) = D-alanine(out) + H(+)(out);
CC Xref=Rhea:RHEA:28903, ChEBI:CHEBI:15378, ChEBI:CHEBI:57416;
CC Evidence={ECO:0000305|PubMed:16952954, ECO:0000305|PubMed:23316042};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28905;
CC Evidence={ECO:0000305|PubMed:16952954, ECO:0000305|PubMed:23316042};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-serine(out) + H(+)(out) = D-serine(in) + H(+)(in);
CC Xref=Rhea:RHEA:70647, ChEBI:CHEBI:15378, ChEBI:CHEBI:35247;
CC Evidence={ECO:0000305|PubMed:16952954};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70648;
CC Evidence={ECO:0000305|PubMed:16952954};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine(in) + H(+)(in) = glycine(out) + H(+)(out);
CC Xref=Rhea:RHEA:28899, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305;
CC Evidence={ECO:0000305|PubMed:16952954, ECO:0000305|PubMed:23316042};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28901;
CC Evidence={ECO:0000305|PubMed:16952954, ECO:0000305|PubMed:23316042};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-cycloserine(in) + H(+)(in) = D-cycloserine(out) + H(+)(out);
CC Xref=Rhea:RHEA:70703, ChEBI:CHEBI:15378, ChEBI:CHEBI:75929;
CC Evidence={ECO:0000305|PubMed:23316042};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70705;
CC Evidence={ECO:0000305|PubMed:23316042};
CC -!- ACTIVITY REGULATION: Uptake of D-serine is inhibited by D-alanine, D-
CC cycloserine, glycine and at high concentrations of D-threonine.
CC {ECO:0000269|PubMed:16952954}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=82.40 uM for D-serine {ECO:0000269|PubMed:16952954};
CC Vmax=58.90 nmol/min/mg enzyme with D-serine as substrate
CC {ECO:0000269|PubMed:16952954};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AAE0}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Single deletion, grows on D-serine or D-serine
CC plus glycerol but not D-alanine. A double dsdX-cycA deletion grows in
CC D-serine plus glycerol, but not D-serine or D-alanine alone, growth on
CC D-serine (but not D-alanine) is restored by dsdX (PubMed:16952954).
CC Mutant exhibits increased resistance to D-cycloserine when grown in a
CC minimal medium, but no change in D-cycloserine sensitivity compared to
CC its parental strain when grown in a complex medium or human urine
CC (PubMed:23316042). {ECO:0000269|PubMed:16952954,
CC ECO:0000269|PubMed:23316042}.
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 amino acid-polyamine-organocation (APC)
CC superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family.
CC {ECO:0000305}.
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DR EMBL; AE014075; AAN83728.1; -; Genomic_DNA.
DR RefSeq; WP_000228366.1; NC_004431.1.
DR AlphaFoldDB; A0A0H2VDI7; -.
DR SMR; A0A0H2VDI7; -.
DR STRING; 199310.c5307; -.
DR EnsemblBacteria; AAN83728; AAN83728; c5307.
DR KEGG; ecc:c5307; -.
DR eggNOG; COG1113; Bacteria.
DR HOGENOM; CLU_007946_9_3_6; -.
DR OMA; FTHLWND; -.
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:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..470
FT /note="D-serine/D-alanine/glycine transporter"
FT /id="PRO_0000439180"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 470 AA; 51660 MW; 0917C948269C5DB1 CRC64;
MVDQVKVVAD DQAPAEQSLR RNLTNRHIQL IAIGGAIGTG LFMGSGKTIS LAGPSIIFVY
MIIGFMLFFV MRAMGELLLS NLEYKSFSDF ASDLLGPWAG YFTGWTYWFC WVVTGMADVV
AITAYAQFWF PGLSDWVASL SVIILLLVLN LATVKMFGEM EFWFAMIKIV AIVSLIVVGL
VMVAMHFQSP TGVEASFAHL WNDGGWFPKG LSGFFAGFQI AVFAFVGIEL VGTTAAETKD
PEKSLPRAIN SIPIRIIMFY VFSLIVIMSV TPWSSVVPEK SPFVELFVLV GLPAAASVIN
FVVLTSAASS ANSGVFSTSR MLFGLAQEGV APKAFAKLSK RAVPAKGLTF SCICLLGGVV
MLYVNPSVIG AFTMITTVSA ILFMFVWTII LCSYLVYRKQ RPHLHEKSIY KMPLGKLMCW
VCMAFFVFVL VLLTLEDDTR QALLVTPLWF IALGLGWLFI GKKRAAELRK
