AROP_ECOLI
ID AROP_ECOLI Reviewed; 457 AA.
AC P15993; P75650;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Aromatic amino acid transport protein AroP {ECO:0000305};
DE AltName: Full=Aromatic amino acid:H(+) symporter AroP {ECO:0000305};
DE AltName: Full=General aromatic amino acid permease {ECO:0000303|PubMed:9150230};
DE AltName: Full=General aromatic transport system {ECO:0000303|PubMed:4919744};
GN Name=aroP {ECO:0000303|PubMed:4919744}; OrderedLocusNames=b0112, JW0108;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2408019; DOI=10.1093/nar/18.3.653;
RA Honore N., Cole S.T.;
RT "Nucleotide sequence of the aroP gene encoding the general aromatic amino
RT acid transport protein of Escherichia coli K-12: homology with yeast
RT transport proteins.";
RL Nucleic Acids Res. 18:653-653(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=K12;
RX PubMed=9150230; DOI=10.1128/jb.179.10.3317-3323.1997;
RA Cosgriff A.J., Pittard A.J.;
RT "A topological model for the general aromatic amino acid permease, AroP, of
RT Escherichia coli.";
RL J. Bacteriol. 179:3317-3323(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
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], AND SEQUENCE REVISION.
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, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=4919744; DOI=10.1128/jb.104.1.177-188.1970;
RA Brown K.D.;
RT "Formation of aromatic amino acid pools in Escherichia coli K-12.";
RL J. Bacteriol. 104:177-188(1970).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=3015892; DOI=10.1128/jb.167.2.749-753.1986;
RA Chye M.L., Guest J.R., Pittard J.;
RT "Cloning of the aroP gene and identification of its product in Escherichia
RT coli K-12.";
RL J. Bacteriol. 167:749-753(1986).
RN [8]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12;
RX PubMed=9209034; DOI=10.1128/jb.179.13.4206-4212.1997;
RA Wang P., Yang J., Pittard A.J.;
RT "Promoters and transcripts associated with the aroP gene of Escherichia
RT coli.";
RL J. Bacteriol. 179:4206-4212(1997).
RN [9]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=9765583; DOI=10.1128/jb.180.20.5466-5472.1998;
RA Wang P., Yang J., Ishihama A., Pittard A.J.;
RT "Demonstration that the TyrR protein and RNA polymerase complex formed at
RT the divergent P3 promoter inhibits binding of RNA polymerase to the major
RT promoter, P1, of the aroP gene of Escherichia coli.";
RL J. Bacteriol. 180:5466-5472(1998).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-103.
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 [11]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12;
RX PubMed=14614536;
RA Wang J.G., Fan C.S., Wu Y.Q., Jin R.L., Liu D.X., Shang L., Jiang P.H.;
RT "Regulation of aroP expression by tyrR gene in Escherichia coli.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:993-997(2003).
RN [12]
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 all three aromatic amino acids, phenylalanine,
CC tyrosine and tryptophan. {ECO:0000269|PubMed:10735864,
CC ECO:0000269|PubMed:4919744, ECO:0000269|PubMed:9150230}.
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:4919744, ECO:0000305|PubMed:9150230};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28925;
CC Evidence={ECO:0000305|PubMed:10735864, ECO:0000305|PubMed:4919744,
CC ECO:0000305|PubMed:9150230};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-tryptophan(in) = H(+)(out) + L-tryptophan(out);
CC Xref=Rhea:RHEA:28879, ChEBI:CHEBI:15378, ChEBI:CHEBI:57912;
CC Evidence={ECO:0000305|PubMed:10735864, ECO:0000305|PubMed:4919744};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28881;
CC Evidence={ECO:0000305|PubMed:10735864, ECO:0000305|PubMed:4919744};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-tyrosine(in) = H(+)(out) + L-tyrosine(out);
CC Xref=Rhea:RHEA:28875, ChEBI:CHEBI:15378, ChEBI:CHEBI:58315;
CC Evidence={ECO:0000305|PubMed:10735864, ECO:0000305|PubMed:4919744,
CC ECO:0000305|PubMed:9150230};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28877;
CC Evidence={ECO:0000305|PubMed:10735864, ECO:0000305|PubMed:4919744,
CC ECO:0000305|PubMed:9150230};
CC -!- ACTIVITY REGULATION: Strong, mutual inhibition of uptake by tyrosine,
CC phenylalanine, and tryptophan. Transport is also inhibited by the
CC aromatic analogs p-fluorophenylalanine, beta-2-thienylalanine and 5-
CC methyltryptophan. {ECO:0000269|PubMed:4919744}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.47 uM for phenylalanine {ECO:0000269|PubMed:4919744};
CC KM=0.40 uM for tryptophan {ECO:0000269|PubMed:4919744};
CC KM=0.57 uM for tyrosine {ECO:0000269|PubMed:4919744};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:3015892, ECO:0000269|PubMed:9150230}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:9150230}.
CC -!- INDUCTION: Contains three promoters, P1, P2 and P3 (PubMed:9209034,
CC PubMed:9765583). Repressed by the regulatory protein TyrR, which binds
CC to TyrR boxes (PubMed:9209034, PubMed:9765583, PubMed:14614536). In the
CC absence of TyrR, the RNA polymerase (RNAP) has a higher affinity for P1
CC than for P2 and P3 and occupies the P1 promoter region
CC (PubMed:9765583). When TyrR and its cofactors are present, TyrR
CC inhibits the binding of RNA polymerase to the P1 promoter by recruiting
CC RNA polymerase to the P3 promoter (PubMed:9765583). P1 is not repressed
CC by TyrR alone but is repressed in the presence of phenylalanine,
CC tyrosine or tryptophan (PubMed:9209034). P2 is partially repressed by
CC TyrR alone and totally repressed by TyrR in the presence of tyrosine,
CC phenylalanine or tryptophan (PubMed:9209034).
CC {ECO:0000269|PubMed:14614536, ECO:0000269|PubMed:9209034,
CC ECO:0000269|PubMed:9765583}.
CC -!- DISRUPTION PHENOTYPE: Mutants show reduced aromatic amino acids
CC transport and are resistant to p-fluorophenylalanine, beta-2-
CC thienylalanine and 5-methyltryptophan. {ECO:0000269|PubMed:4919744}.
CC -!- MISCELLANEOUS: The general aromatic transport system is not essential
CC for the supply of external aromatic amino acids to protein synthesis.
CC {ECO:0000269|PubMed:4919744}.
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; X17333; CAA35211.1; -; Genomic_DNA.
DR EMBL; U87285; AAC45299.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73223.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96681.2; -; Genomic_DNA.
DR PIR; H64733; QRECAA.
DR RefSeq; NP_414654.1; NC_000913.3.
DR RefSeq; WP_000969915.1; NZ_SSZK01000004.1.
DR AlphaFoldDB; P15993; -.
DR SMR; P15993; -.
DR BioGRID; 4259731; 11.
DR STRING; 511145.b0112; -.
DR TCDB; 2.A.3.1.3; the amino acid-polyamine-organocation (apc) family.
DR PaxDb; P15993; -.
DR PRIDE; P15993; -.
DR EnsemblBacteria; AAC73223; AAC73223; b0112.
DR EnsemblBacteria; BAB96681; BAB96681; BAB96681.
DR GeneID; 60903337; -.
DR GeneID; 946018; -.
DR KEGG; ecj:JW0108; -.
DR KEGG; eco:b0112; -.
DR PATRIC; fig|511145.12.peg.114; -.
DR EchoBASE; EB0082; -.
DR eggNOG; COG1113; Bacteria.
DR HOGENOM; CLU_007946_9_3_6; -.
DR InParanoid; P15993; -.
DR OMA; VIMYLTP; -.
DR PhylomeDB; P15993; -.
DR BioCyc; EcoCyc:AROP-MON; -.
DR BioCyc; MetaCyc:AROP-MON; -.
DR PRO; PR:P15993; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015192; F:L-phenylalanine transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015196; F:L-tryptophan transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0005302; F:L-tyrosine transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015823; P:phenylalanine transport; IDA:EcoCyc.
DR GO; GO:0015827; P:tryptophan transport; IDA:EcoCyc.
DR GO; GO:0015828; P:tyrosine transport; IDA: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; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..457
FT /note="Aromatic amino acid transport protein AroP"
FT /id="PRO_0000054193"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9150230"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9150230"
FT TOPO_DOM 40..42
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9150230"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9150230"
FT TOPO_DOM 64..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9150230"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9150230"
FT TOPO_DOM 120..124
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9150230"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9150230"
FT TOPO_DOM 146..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9150230"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9150230"
FT TOPO_DOM 169..192
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9150230"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9150230"
FT TOPO_DOM 214..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9150230"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9150230"
FT TOPO_DOM 261..279
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9150230"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9150230"
FT TOPO_DOM 301..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9150230"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9150230"
FT TOPO_DOM 352..359
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9150230"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9150230"
FT TOPO_DOM 381..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9150230"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9150230"
FT TOPO_DOM 424..426
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9150230"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9150230"
FT TOPO_DOM 448..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:9150230"
FT SITE 103
FT /note="Key residue for tryptophan transport"
FT /evidence="ECO:0000269|PubMed:10735864"
FT MUTAGEN 103
FT /note="Y->F: Decreases tryptophan transport to less than
FT 50% of wild-type levels and reduces the ability of
FT tryptophan to inhibit phenylalanine transport from 95 to
FT 62%."
FT /evidence="ECO:0000269|PubMed:10735864"
FT CONFLICT 28
FT /note="A -> S (in Ref. 1; CAA35211)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="G -> A (in Ref. 1; CAA35211 and 2; AAC45299)"
FT /evidence="ECO:0000305"
FT CONFLICT 398..399
FT /note="PA -> L (in Ref. 1; CAA35211)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="P -> R (in Ref. 1; CAA35211 and 2; AAC45299)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="A -> G (in Ref. 1; CAA35211)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="S -> W (in Ref. 1; CAA35211)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 49690 MW; B2F66D3F73CD78BE CRC64;
MMEGQQHGEQ LKRGLKNRHI QLIALGGAIG TGLFLGSASV IQSAGPGIIL GYAIAGFIAF
LIMRQLGEMV VEEPVAGSFS HFAYKYWGSF AGFASGWNYW VLYVLVAMAE LTAVGKYIQF
WYPEIPTWVS AAVFFVVINA INLTNVKVFG EMEFWFAIIK VIAVVAMIIF GGWLLFSGNG
GPQATVSNLW DQGGFLPHGF TGLVMMMAII MFSFGGLELV GITAAEADNP EQSIPKATNQ
VIYRILIFYI GSLAVLLSLM PWTRVTADTS PFVLIFHELG DTFVANALNI VVLTAALSVY
NSCVYCNSRM LFGLAQQGNA PKALASVDKR GVPVNTILVS ALVTALCVLI NYLAPESAFG
LLMALVVSAL VINWAMISLA HMKFRRAKQE QGVVTRFPAL LYPLGNWICL LFMAAVLVIM
LMTPGMAISV YLIPVWLIVL GIGYLFKEKT AKAVKAH
