AROP_ECOL6
ID AROP_ECOL6 Reviewed; 456 AA.
AC Q8FL49;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Aromatic amino acid transport protein AroP {ECO:0000250|UniProtKB:P15993};
DE AltName: Full=Aromatic amino acid:H(+) symporter AroP {ECO:0000250|UniProtKB:P15993};
DE AltName: Full=General aromatic amino acid permease {ECO:0000250|UniProtKB:P15993};
GN Name=aroP; OrderedLocusNames=c0131;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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:0000250|UniProtKB:P15993}.
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:0000250|UniProtKB:P15993};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28925;
CC Evidence={ECO:0000250|UniProtKB:P15993};
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:0000250|UniProtKB:P15993};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28881;
CC Evidence={ECO:0000250|UniProtKB:P15993};
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:0000250|UniProtKB:P15993};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28877;
CC Evidence={ECO:0000250|UniProtKB:P15993};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P15993}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P15993}.
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; AE014075; AAN78629.1; -; Genomic_DNA.
DR RefSeq; WP_000399017.1; NC_004431.1.
DR AlphaFoldDB; Q8FL49; -.
DR SMR; Q8FL49; -.
DR STRING; 199310.c0131; -.
DR EnsemblBacteria; AAN78629; AAN78629; c0131.
DR KEGG; ecc:c0131; -.
DR eggNOG; COG1113; Bacteria.
DR HOGENOM; CLU_007946_9_3_6; -.
DR OMA; VIMYLTP; -.
DR BioCyc; ECOL199310:C0131-MON; -.
DR Proteomes; UP000001410; 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 InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..456
FT /note="Aromatic amino acid transport protein AroP"
FT /id="PRO_0000054194"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..41
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..116
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..200
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..270
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..357
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..424
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 456 AA; 49559 MW; F014783258C762D7 CRC64;
MEGQQHGEQL KRGLKNRHIQ LIALGGAIGT GLFLGSASVI QSAGPGIILG YAIAGFIAFL
IMRQLGEMVV EEPVAGSFSH FAYKYWGSFA GFASGWNYWV LYVLVAMAEL TAVGKYIQFW
YPEIPTWVSA AVFFVVINAI NLTNVKVFGE MEFWFAIIKV IAVVAMIIFG AWLLFSGNGG
PQASVSNLWD QGGFLPHGFT GLVMMMAIIM FSFGGLELVG ITAAEADNPE QSIPKATNQV
IYRILIFYIG SLAVLLSLMP WTRVTADTSP FVLIFHELGD TFVANALNIV VLTAALSVYN
SCVYCNSRML FGLAQQGNAP KALASVDKRG VPVNTILVSA LVTALCVLIN YLAPESAFGL
LMALVVSALV INWAMISLAH MKFRRAKQEQ GVVTRFPALL YPLGNWICLL FMAAVLVIML
MTPGMAISVY LIPVWLIVLG IGYLFKEKTA KAVKAH
