CYCA_ECOLI
ID CYCA_ECOLI Reviewed; 470 AA.
AC P0AAE0; P39312; Q2M697;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=D-serine/D-alanine/glycine transporter {ECO:0000305};
DE AltName: Full=Amino acid carrier CycA {ECO:0000303|PubMed:15221223};
GN Name=cycA; Synonyms=dagA {ECO:0000303|PubMed:4574696}, ytfD;
GN OrderedLocusNames=b4208, JW4166;
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=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
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 [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 IDENTIFICATION AS CYCA.
RA Berlyn M., Rudd K.E.;
RL Unpublished observations (JUL-1995).
RN [5]
RP FUNCTION.
RX PubMed=4926674; DOI=10.1128/jb.105.3.1028-1035.1971;
RA Wargel R.J., Hadur C.A., Neuhaus F.C.;
RT "Mechanism of D-cycloserine action: transport mutants for D-alanine, D-
RT cycloserine, and glycine.";
RL J. Bacteriol. 105:1028-1035(1971).
RN [6]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=4574696; DOI=10.1128/jb.114.2.679-684.1973;
RA Cosloy S.D.;
RT "D-serine transport system in Escherichia coli K-12.";
RL J. Bacteriol. 114:679-684(1973).
RN [7]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=4583203; DOI=10.1128/jb.116.1.12-18.1973;
RA Robbins J.C., Oxender D.L.;
RT "Transport systems for alanine, serine, and glycine in Escherichia coli K-
RT 12.";
RL J. Bacteriol. 116:12-18(1973).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=15221223; DOI=10.1007/s00253-004-1636-0;
RA Schneider F., Kraemer R., Burkovski A.;
RT "Identification and characterization of the main beta-alanine uptake system
RT in Escherichia coli.";
RL Appl. Microbiol. Biotechnol. 65:576-582(2004).
RN [9]
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 [10]
RP INDUCTION.
RX PubMed=19118351; DOI=10.1099/mic.0.023598-0;
RA Pulvermacher S.C., Stauffer L.T., Stauffer G.V.;
RT "Role of the sRNA GcvB in regulation of cycA in Escherichia coli.";
RL Microbiology 155:106-114(2009).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
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, glycine and beta-alanine
CC (PubMed:4926674, PubMed:4574696, PubMed:4583203, PubMed:15221223,
CC PubMed:23316042). Also contributes to L-alanine uptake (PubMed:4574696,
CC PubMed:4583203). In addition, in minimal media, transports the broad
CC spectrum antibiotic D-cycloserine into the cell (PubMed:4926674,
CC PubMed:4574696, PubMed:23316042). Transports D-cycloserine only in
CC minimal media, and not in a complex medium, suggesting that CycA does
CC not play a role in D-cycloserine transport when E.coli is grown in a
CC complex or biologically relevant medium, probably due to competition
CC from other CycA substrates present in the medium (PubMed:23316042).
CC {ECO:0000269|PubMed:15221223, ECO:0000269|PubMed:23316042,
CC ECO:0000269|PubMed:4574696, ECO:0000269|PubMed:4583203,
CC ECO:0000269|PubMed:4926674}.
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:23316042, ECO:0000305|PubMed:4574696};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28905;
CC Evidence={ECO:0000305|PubMed:23316042, ECO:0000305|PubMed:4574696};
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:4574696};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70648;
CC Evidence={ECO:0000305|PubMed:4574696};
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:23316042, ECO:0000305|PubMed:4574696};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28901;
CC Evidence={ECO:0000305|PubMed:23316042, ECO:0000305|PubMed:4574696};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-alanine(in) + H(+)(in) = beta-alanine(out) + H(+)(out);
CC Xref=Rhea:RHEA:29459, ChEBI:CHEBI:15378, ChEBI:CHEBI:57966;
CC Evidence={ECO:0000269|PubMed:15221223};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29461;
CC Evidence={ECO:0000269|PubMed:15221223};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-alanine(in) = H(+)(out) + L-alanine(out);
CC Xref=Rhea:RHEA:29443, ChEBI:CHEBI:15378, ChEBI:CHEBI:57972;
CC Evidence={ECO:0000305|PubMed:4574696};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29445;
CC Evidence={ECO:0000305|PubMed:4574696};
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: Beta-alanine uptake is inhibited by carbonyl
CC cyanide m-chlorophenylhydrazone (CCCP), which dissipates the proton
CC motive force. {ECO:0000269|PubMed:15221223}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.4 mM for beta-alanine {ECO:0000269|PubMed:15221223};
CC Vmax=46 nmol/min/mg enzyme {ECO:0000269|PubMed:15221223};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: In complex media, expression is negatively regulated by Hfq
CC and the small non-translated RNA GcvB (PubMed:19118351). Hfq is
CC required for the GcvB effect (PubMed:19118351).
CC {ECO:0000269|PubMed:19118351}.
CC -!- DISRUPTION PHENOTYPE: Mutant exhibits increased resistance to D-
CC cycloserine when grown in a minimal medium, but no change in D-
CC cycloserine sensitivity compared to its parental strain when grown in a
CC complex medium. {ECO:0000269|PubMed:23316042}.
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; U14003; AAA97104.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77165.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78209.1; -; Genomic_DNA.
DR PIR; S56433; S56433.
DR RefSeq; NP_418629.1; NC_000913.3.
DR RefSeq; WP_000228346.1; NZ_STEB01000013.1.
DR AlphaFoldDB; P0AAE0; -.
DR SMR; P0AAE0; -.
DR BioGRID; 4262718; 171.
DR DIP; DIP-9359N; -.
DR IntAct; P0AAE0; 1.
DR STRING; 511145.b4208; -.
DR TCDB; 2.A.3.1.7; the amino acid-polyamine-organocation (apc) family.
DR jPOST; P0AAE0; -.
DR PaxDb; P0AAE0; -.
DR PRIDE; P0AAE0; -.
DR EnsemblBacteria; AAC77165; AAC77165; b4208.
DR EnsemblBacteria; BAE78209; BAE78209; BAE78209.
DR GeneID; 58461523; -.
DR GeneID; 948725; -.
DR KEGG; ecj:JW4166; -.
DR KEGG; eco:b4208; -.
DR PATRIC; fig|1411691.4.peg.2493; -.
DR EchoBASE; EB2397; -.
DR eggNOG; COG1113; Bacteria.
DR HOGENOM; CLU_007946_9_3_6; -.
DR InParanoid; P0AAE0; -.
DR OMA; FTHLWND; -.
DR PhylomeDB; P0AAE0; -.
DR BioCyc; EcoCyc:CYCA-MON; -.
DR BioCyc; MetaCyc:CYCA-MON; -.
DR PRO; PR:P0AAE0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0001761; F:beta-alanine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0042944; F:D-alanine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0042945; F:D-serine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0001762; P:beta-alanine transport; IMP:EcoCyc.
DR GO; GO:0042941; P:D-alanine transport; IMP:EcoCyc.
DR GO; GO:0042942; P:D-serine transport; IMP:EcoCyc.
DR GO; GO:0015816; P:glycine transport; IMP:EcoCyc.
DR GO; GO:0015808; P:L-alanine transport; IMP:EcoCyc.
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 Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..470
FT /note="D-serine/D-alanine/glycine transporter"
FT /id="PRO_0000054199"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..136
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..210
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..282
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..440
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
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
