CYCA_ECO57
ID CYCA_ECO57 Reviewed; 470 AA.
AC P0AAE1; P39312;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=D-serine/D-alanine/glycine transporter;
GN Name=cycA; OrderedLocusNames=Z5819, ECs5186;
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).
CC -!- FUNCTION: Permease that is involved in the transport across the
CC cytoplasmic membrane of D-alanine, D-serine and glycine.
CC {ECO:0000250|UniProtKB:A0A0H2VDI7}.
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:0000250|UniProtKB:A0A0H2VDI7};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28905;
CC Evidence={ECO:0000250|UniProtKB:A0A0H2VDI7};
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:0000250|UniProtKB:A0A0H2VDI7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70648;
CC Evidence={ECO:0000250|UniProtKB:A0A0H2VDI7};
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:0000250|UniProtKB:A0A0H2VDI7};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28901;
CC Evidence={ECO:0000250|UniProtKB:A0A0H2VDI7};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AAE0}; Multi-pass membrane protein
CC {ECO:0000255}.
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; AE005174; AAG59406.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38609.1; -; Genomic_DNA.
DR PIR; B86118; B86118.
DR PIR; B91277; B91277.
DR RefSeq; NP_313213.1; NC_002695.1.
DR RefSeq; WP_000228346.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AAE1; -.
DR SMR; P0AAE1; -.
DR STRING; 155864.EDL933_5554; -.
DR PRIDE; P0AAE1; -.
DR EnsemblBacteria; AAG59406; AAG59406; Z5819.
DR EnsemblBacteria; BAB38609; BAB38609; ECs_5186.
DR GeneID; 58461523; -.
DR GeneID; 913962; -.
DR KEGG; ece:Z5819; -.
DR KEGG; ecs:ECs_5186; -.
DR PATRIC; fig|386585.9.peg.5421; -.
DR eggNOG; COG1113; Bacteria.
DR HOGENOM; CLU_007946_9_3_6; -.
DR OMA; FTHLWND; -.
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: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 3: Inferred from homology;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..470
FT /note="D-serine/D-alanine/glycine transporter"
FT /id="PRO_0000054200"
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 137..157
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; F9279E48D838EAF8 CRC64;
MVDQVKVVAD DQAPAEQSLR RNLTNRHIQL IAIGGAIGTG LFMGSGKTIS LAGPSIIFVY
MIIGFMLFFV MRAMGELLLS NLEYKSFSDF ASDLLGPWAG YFTGWTYWFC WVVTGMADVV
AITAYAQFWF PDLSDWVASL AVIVLLLTLN LATVKMFGEM EFWFAMIKIV AIVSLIVVGL
VMVAMHFQSP TGVEASFAHL WNDGGWFPKG LSGFFAGFQI AVFAFVGIEL VGTTAAETKD
PEKSLPRAIN SIPIRIIMFY VFALIVIMSV TPWSSVVPEK SPFVELFVLV GLPAAASVIN
FVVLTSAASS ANSGVFSTSR MLFGLAQEGV APKAFAKLSK RAVPAKGLTF SCICLLGGVV
MLYVNPSVIG AFTMITTVSA ILFMFVWTII LCSYLVYRKQ RPHLHEKSIY KMPLGKLMCW
VCMAFFVFVV VLLTLEDDTR QALLVTPLWF IALGLGWLFI GKKRAAELRK
