FYWP_LACLM
ID FYWP_LACLM Reviewed; 457 AA.
AC A2RMP5;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Aromatic amino acid permease FywP {ECO:0000305};
GN Name=fywP {ECO:0000303|PubMed:23144255};
GN OrderedLocusNames=llmg_2011 {ECO:0000312|EMBL:CAL98579.1};
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=MG1363;
RX PubMed=23144255; DOI=10.1128/jb.01948-12;
RA Trip H., Mulder N.L., Lolkema J.S.;
RT "Cloning, expression, and functional characterization of secondary amino
RT acid transporters of Lactococcus lactis.";
RL J. Bacteriol. 195:340-350(2013).
CC -!- FUNCTION: Involved in phenylalanine and tyrosine uptake. Has also
CC affinity for tryptophan. Plays no significant role in the excretion of
CC accumulated phenylalanine. {ECO:0000269|PubMed:23144255}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene reduces the efficiency of
CC growth at low concentrations of the aromatic amino acids.
CC {ECO:0000269|PubMed:23144255}.
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; AM406671; CAL98579.1; -; Genomic_DNA.
DR RefSeq; WP_011835738.1; NZ_WJVF01000004.1.
DR AlphaFoldDB; A2RMP5; -.
DR SMR; A2RMP5; -.
DR STRING; 416870.llmg_2011; -.
DR EnsemblBacteria; CAL98579; CAL98579; llmg_2011.
DR KEGG; llm:llmg_2011; -.
DR eggNOG; COG1113; Bacteria.
DR HOGENOM; CLU_007946_9_3_9; -.
DR OMA; PKFLDYV; -.
DR PhylomeDB; A2RMP5; -.
DR BioCyc; LLAC416870:LLMG_RS10065-MON; -.
DR Proteomes; UP000000364; 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:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR Pfam; PF00324; AA_permease; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..457
FT /note="Aromatic amino acid permease FywP"
FT /id="PRO_0000442539"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 457 AA; 49432 MW; A930040BF887FF0B CRC64;
MENSTGLKSS LKTRHIVMLS LGGAIGSGLF LGSGKVIAQA GPSVLLSYVL AGLTLYVVMY
GVGKMVIHQD DHKAGMAGVV APFIGDHWAH FADWVYWATW MAVLIAEEAG VSTFLAILIP
GVPLWVFALV VAVLGTAINL WSVKAFAETE YWLAFIKVAV ILLLIALGIY LLVINDAHLG
FVADSAQKVT TKSTAPSFAP NGFSGFLTSL LVVIFSFGGS ELAAITVAET ENPKVAIPRA
IRGVLIRIIS FYVIPIFLFL HLLPWSEVSN PDAASPFATI FARVGIPHAD KIVLVIIVIA
IFSAVNSAIY ATSRSLYSRI QGSSTYVGKK LGKLSKNQVP TNAILVSSFV LFIGVLLSAV
LGDGFWQFVA GSISFTISIV WILLLVAALV LYFKHKEVTN WFVKLATLVV LIALSLVFIM
QIITNPWTLS VFALVICLLS YFSYRKKKSI IEKTFIL