ID   FRLA_ECOLI              Reviewed;         445 AA.
AC   P45539; P76686; Q2M736;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   10-JUN-2026, entry version 172.
DE   RecName: Full=Probable fructoselysine/psicoselysine transporter FrlA;
GN   Name=frlA {ECO:0000303|PubMed:12147680}; Synonyms=yhfM;
GN   OrderedLocusNames=b3370, JW3333;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
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   [2]
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   [3]
RP   FUNCTION, PATHWAY, AND INDUCTION.
RX   PubMed=12147680; DOI=10.1074/jbc.m200863200;
RA   Wiame E., Delpierre G., Collard F., Van Schaftingen E.;
RT   "Identification of a pathway for the utilization of the Amadori product
RT   fructoselysine in Escherichia coli.";
RL   J. Biol. Chem. 277:42523-42529(2002).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=14641112; DOI=10.1042/bj20031527;
RA   Wiame E., Van Schaftingen E.;
RT   "Fructoselysine 3-epimerase, an enzyme involved in the metabolism of the
RT   unusual Amadori compound psicoselysine in Escherichia coli.";
RL   Biochem. J. 378:1047-1052(2004).
CC   -!- FUNCTION: Is likely involved in the transport of fructoselysine and
CC       psicoselysine to the cytoplasm, where they are degraded.
CC       {ECO:0000305|PubMed:12147680, ECO:0000305|PubMed:14641112}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-(D-fructosyl)-L-lysine(in) = N(6)-(D-fructosyl)-L-
CC         lysine(out); Xref=Rhea:RHEA:28454, ChEBI:CHEBI:61393;
CC         Evidence={ECO:0000305|PubMed:12147680, ECO:0000305|PubMed:14641112};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28456;
CC         Evidence={ECO:0000305|PubMed:12147680, ECO:0000305|PubMed:14641112};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-(D-psicosyl)-L-lysine(in) = N(6)-(D-psicosyl)-L-
CC         lysine(out); Xref=Rhea:RHEA:28450, ChEBI:CHEBI:61403;
CC         Evidence={ECO:0000305|PubMed:14641112};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28452;
CC         Evidence={ECO:0000305|PubMed:14641112};
CC   -!- PATHWAY: Carbohydrate metabolism; fructoselysine degradation.
CC       {ECO:0000269|PubMed:14641112, ECO:0000305|PubMed:12147680}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- INDUCTION: Induced by fructoselysine. Makes part of the frl operon with
CC       FrlB, FrlC, FrlD and FrlR. {ECO:0000305|PubMed:12147680}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC       fructoselysine or psicoselysine, where they do grow on glucose.
CC       {ECO:0000269|PubMed:14641112}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. {ECO:0000305}.
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DR   EMBL; U18997; AAA58167.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U00096; AAC76395.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77920.1; -; Genomic_DNA.
DR   PIR; E65131; E65131.
DR   RefSeq; NP_417829.2; NC_000913.3.
DR   RefSeq; WP_000535505.1; NZ_CP009789.1.
DR   AlphaFoldDB; P45539; -.
DR   SMR; P45539; -.
DR   BioGRID; 4262479; 5.
DR   DIP; DIP-12322N; -.
DR   FunCoup; P45539; 505.
DR   IntAct; P45539; 1.
DR   STRING; 511145.b3370; -.
DR   TCDB; 2.A.3.8.17; the amino acid-polyamine-organocation (apc) family.
DR   PaxDb; 511145-b3370; -.
DR   EnsemblBacteria; AAC76395; AAC76395; b3370.
DR   GeneID; 93778627; -.
DR   GeneID; 947878; -.
DR   KEGG; ecj:JW3333; -.
DR   KEGG; eco:b3370; -.
DR   KEGG; ecoc:C3026_18300; -.
DR   PATRIC; fig|1411691.4.peg.3359; -.
DR   EchoBASE; EB2745; -.
DR   eggNOG; COG0531; Bacteria.
DR   HOGENOM; CLU_007946_3_4_6; -.
DR   InParanoid; P45539; -.
DR   OMA; TYWVISF; -.
DR   PhylomeDB; P45539; -.
DR   BioCyc; EcoCyc:YHFM-MONOMER; -.
DR   BioCyc; MetaCyc:YHFM-MONOMER; -.
DR   UniPathway; UPA00784; -.
DR   PRO; PR:P45539; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P45539; -.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR   GO; GO:1901281; P:fructoselysine catabolic process; IMP:EcoCyc.
DR   FunFam; 1.20.1740.10:FF:000048; Fructoselysine transporter frlA; 1.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR050598; AminoAcid_Transporter.
DR   NCBIfam; NF008466; PRK11357.1; 1.
DR   PANTHER; PTHR11785; AMINO ACID TRANSPORTER; 1.
DR   PANTHER; PTHR11785:SF512; SOBREMESA, ISOFORM B; 1.
DR   Pfam; PF13520; AA_permease_2; 1.
DR   PIRSF; PIRSF006060; AA_transporter; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..445
FT                   /note="Probable fructoselysine/psicoselysine transporter
FT                   FrlA"
FT                   /id="PRO_0000054247"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        389..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   445 AA;  47577 MW;  B98DF5944A5E1FEF CRC64;
     MGSQELQRKL GFWAVLAIAV GTTVGSGIFV SVGEVAKAAG TPWLTVLAFV IGGLIVIPQM
     CVYAELSTAY PENGADYVYL KNAGSRPLAF LSGWASFWAN DAPSLSIMAL AIVSNLGFLT
     PIDPLLGKFI AAGLIIAFML LHLRSVEGGA AFQTLITIAK IIPFTIVIGL GIFWFKAENF
     AAPTTTAIGA TGSFMALLAG ISATSWSYTG MASICYMTGE IKNPGKTMPR ALIGSCLLVL
     VLYTLLALVI SGLMPFDKLA NSETPISDAL TWIPALGSTA GIFVAITAMI VILGSLSSCV
     MYQPRLEYAM AKDNLFFKCF GHVHPKYNTP DVSIILQGAL GIFFIFVSDL TSLLGYFTLV
     MCFKNTLTFG SIIWCRKRDD YKPLWRTPAF GLMTTLAIAS SLILVASTFV WAPIPGLICA
     VIVIATGLPA YAFWAKRSRQ LNALS
//