PHEP_ECOLI
ID PHEP_ECOLI Reviewed; 458 AA.
AC P24207; P77090;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Phenylalanine-specific permease;
DE AltName: Full=Phenylalanine:H(+) symporter PheP {ECO:0000305};
GN Name=pheP {ECO:0000303|PubMed:1711024}; OrderedLocusNames=b0576, JW0565;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=1711024; DOI=10.1128/jb.173.12.3622-3629.1991;
RA Pi J., Wookey P.J., Pittard A.J.;
RT "Cloning and sequencing of the pheP gene, which encodes the phenylalanine-
RT specific transport system of Escherichia coli.";
RL J. Bacteriol. 173:3622-3629(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-26; PHE-87; PHE-90;
RP TYR-92; TYR-94; TRP-95; PHE-98; PHE-101; TRP-105; TYR-107; TRP-108;
RP PHE-111; GLU-118; LYS-168; GLU-226 AND ARG-252.
RX PubMed=8226700; DOI=10.1128/jb.175.22.7500-7504.1993;
RA Pi J., Wookey P.J., Pittard A.J.;
RT "Site-directed mutagenesis reveals the importance of conserved charged
RT residues for the transport activity of the PheP permease of Escherichia
RT coli.";
RL J. Bacteriol. 175:7500-7504(1993).
RN [7]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=8626334; DOI=10.1128/jb.178.9.2650-2655.1996;
RA Pi J., Pittard A.J.;
RT "Topology of the phenylalanine-specific permease of Escherichia coli.";
RL J. Bacteriol. 178:2650-2655(1996).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-54; PRO-341 AND
RP PRO-442.
RC STRAIN=K12;
RX PubMed=9791098; DOI=10.1128/jb.180.21.5515-5519.1998;
RA Pi J., Dogovski C., Pittard A.J.;
RT "Functional consequences of changing proline residues in the phenylalanine-
RT specific permease of Escherichia coli.";
RL J. Bacteriol. 180:5515-5519(1998).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF PHE-111.
RC STRAIN=K12;
RX PubMed=10735864; DOI=10.1128/jb.182.8.2207-2217.2000;
RA Cosgriff A.J., Brasier G., Pi J., Dogovski C., Sarsero J.P., Pittard A.J.;
RT "A study of AroP-PheP chimeric proteins and identification of a residue
RT involved in tryptophan transport.";
RL J. Bacteriol. 182:2207-2217(2000).
RN [10]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Permease that is involved in the active transport across the
CC cytoplasmic membrane of phenylalanine (PubMed:10735864, PubMed:1711024,
CC PubMed:8226700, PubMed:9791098). Can also transport tyrosine, but not
CC tryptophan (PubMed:10735864). {ECO:0000269|PubMed:10735864,
CC ECO:0000269|PubMed:1711024, ECO:0000269|PubMed:8226700,
CC ECO:0000269|PubMed:9791098}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-phenylalanine(in) = H(+)(out) + L-
CC phenylalanine(out); Xref=Rhea:RHEA:28923, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000305|PubMed:10735864,
CC ECO:0000305|PubMed:1711024, ECO:0000305|PubMed:8226700};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28925;
CC Evidence={ECO:0000305|PubMed:10735864, ECO:0000305|PubMed:1711024,
CC ECO:0000305|PubMed:8226700};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:8626334, ECO:0000269|PubMed:9791098}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:8626334}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40774.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M58000; AAA24334.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40774.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73677.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35216.1; -; Genomic_DNA.
DR PIR; A39431; A39431.
DR RefSeq; NP_415108.1; NC_000913.3.
DR RefSeq; WP_000786319.1; NZ_SSZK01000024.1.
DR AlphaFoldDB; P24207; -.
DR SMR; P24207; -.
DR BioGRID; 4259879; 6.
DR DIP; DIP-10479N; -.
DR IntAct; P24207; 2.
DR STRING; 511145.b0576; -.
DR TCDB; 2.A.3.1.1; the amino acid-polyamine-organocation (apc) family.
DR PaxDb; P24207; -.
DR PRIDE; P24207; -.
DR EnsemblBacteria; AAC73677; AAC73677; b0576.
DR EnsemblBacteria; BAA35216; BAA35216; BAA35216.
DR GeneID; 945199; -.
DR KEGG; ecj:JW0565; -.
DR KEGG; eco:b0576; -.
DR PATRIC; fig|1411691.4.peg.1698; -.
DR EchoBASE; EB0702; -.
DR eggNOG; COG1113; Bacteria.
DR HOGENOM; CLU_007946_9_3_6; -.
DR InParanoid; P24207; -.
DR OMA; MFAYLAV; -.
DR PhylomeDB; P24207; -.
DR BioCyc; EcoCyc:PHEP-MON; -.
DR BioCyc; MetaCyc:PHEP-MON; -.
DR PRO; PR:P24207; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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 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; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..458
FT /note="Phenylalanine-specific permease"
FT /id="PRO_0000054206"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8626334"
FT TRANSMEM 28..48
FT /note="Helical; Name=I"
FT /evidence="ECO:0000305|PubMed:8626334"
FT TOPO_DOM 49..50
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8626334"
FT TRANSMEM 51..71
FT /note="Helical; Name=II"
FT /evidence="ECO:0000305|PubMed:8626334"
FT TOPO_DOM 72..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8626334"
FT TRANSMEM 106..126
FT /note="Helical; Name=III"
FT /evidence="ECO:0000305|PubMed:8626334"
FT TOPO_DOM 127..132
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8626334"
FT TRANSMEM 133..153
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000305|PubMed:8626334"
FT TOPO_DOM 154..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8626334"
FT TRANSMEM 161..181
FT /note="Helical; Name=V"
FT /evidence="ECO:0000305|PubMed:8626334"
FT TOPO_DOM 182..196
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8626334"
FT TRANSMEM 197..217
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000305|PubMed:8626334"
FT TOPO_DOM 218..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8626334"
FT TRANSMEM 251..271
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000305|PubMed:8626334"
FT TOPO_DOM 272..288
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8626334"
FT TRANSMEM 289..309
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000305|PubMed:8626334"
FT TOPO_DOM 310..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8626334"
FT TRANSMEM 342..362
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000305|PubMed:8626334"
FT TOPO_DOM 363..367
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8626334"
FT TRANSMEM 368..388
FT /note="Helical; Name=X"
FT /evidence="ECO:0000305|PubMed:8626334"
FT TOPO_DOM 389..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8626334"
FT TRANSMEM 412..432
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000305|PubMed:8626334"
FT TOPO_DOM 433..434
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8626334"
FT TRANSMEM 435..455
FT /note="Helical; Name=XII"
FT /evidence="ECO:0000305|PubMed:8626334"
FT TOPO_DOM 456..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:8626334"
FT MUTAGEN 26
FT /note="R->G,S,Q: Strong decrease in phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 54
FT /note="P->A: 50% of wild-type phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:9791098"
FT MUTAGEN 54
FT /note="P->G: No change in phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:9791098"
FT MUTAGEN 54
FT /note="P->L: 26% of wild-type phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:9791098"
FT MUTAGEN 87
FT /note="F->L: No effect on phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 90
FT /note="F->L: 65% of wild-type phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 92
FT /note="Y->L: 41% of wild-type phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 94
FT /note="Y->L: 69% of wild-type phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 95
FT /note="W->L: 10% of wild-type phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 98
FT /note="F->L: No effect on phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 101
FT /note="F->L: 38% of wild-type phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 105
FT /note="W->L: 39% of wild-type phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 107
FT /note="Y->L: No effect on phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 108
FT /note="W->L: 71% of wild-type phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 111
FT /note="F->L: 60% of wild-type phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 111
FT /note="F->Y: Enables the transport of tryptophan to almost
FT the same steady-state level as that of phenylalanine."
FT /evidence="ECO:0000269|PubMed:10735864"
FT MUTAGEN 118
FT /note="E->G,L,V,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 168
FT /note="K->L,R: Strong decrease in phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 168
FT /note="K->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 226
FT /note="E->A,Q,K,R,W: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 252
FT /note="R->D,E,F,W,P: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8226700"
FT MUTAGEN 341
FT /note="P->A: 5% of wild-type phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:9791098"
FT MUTAGEN 341
FT /note="P->G,Q,K,R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9791098"
FT MUTAGEN 341
FT /note="P->S: 3% of wild-type phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:9791098"
FT MUTAGEN 341
FT /note="P->T: 17% of wild-type phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:9791098"
FT MUTAGEN 442
FT /note="P->A: 46% of wild-type phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:9791098"
FT MUTAGEN 442
FT /note="P->G: 52% of wild-type phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:9791098"
FT MUTAGEN 442
FT /note="P->L: 43% of wild-type phenylalanine transport
FT activity."
FT /evidence="ECO:0000269|PubMed:9791098"
SQ SEQUENCE 458 AA; 50677 MW; 69D865369249A1A8 CRC64;
MKNASTVSED TASNQEPTLH RGLHNRHIQL IALGGAIGTG LFLGIGPAIQ MAGPAVLLGY
GVAGIIAFLI MRQLGEMVVE EPVSGSFAHF AYKYWGPFAG FLSGWNYWVM FVLVGMAELT
AAGIYMQYWF PDVPTWIWAA AFFIIINAVN LVNVRLYGET EFWFALIKVL AIIGMIGFGL
WLLFSGHGGE KASIDNLWRY GGFFATGWNG LILSLAVIMF SFGGLELIGI TAAEARDPEK
SIPKAVNQVV YRILLFYIGS LVVLLALYPW VEVKSNSSPF VMIFHNLDSN VVASALNFVI
LVASLSVYNS GVYSNSRMLF GLSVQGNAPK FLTRVSRRGV PINSLMLSGA ITSLVVLINY
LLPQKAFGLL MALVVATLLL NWIMICLAHL RFRAAMRRQG RETQFKALLY PFGNYLCIAF
LGMILLLMCT MDDMRLSAIL LPVWIVFLFM AFKTLRRK
