AROP_CORGL
ID AROP_CORGL Reviewed; 463 AA.
AC Q46065;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Aromatic amino acid transport protein AroP;
DE AltName: Full=General aromatic amino acid permease;
GN Name=aroP {ECO:0000303|PubMed:7592354}; OrderedLocusNames=Cgl1107, cg1257;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=7592354; DOI=10.1128/jb.177.20.5991-5993.1995;
RA Wehrmann A., Morakkabati S., Kraemer R., Sahm H., Eggeling L.;
RT "Functional analysis of sequences adjacent to dapE of Corynebacterium
RT glutamicum reveals the presence of aroP, which encodes the aromatic amino
RT acid transporter.";
RL J. Bacteriol. 177:5991-5993(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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:0000305|PubMed:7592354}.
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:7592354};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28925;
CC Evidence={ECO:0000305|PubMed:7592354};
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:7592354};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28881;
CC Evidence={ECO:0000305|PubMed:7592354};
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:7592354};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28877;
CC Evidence={ECO:0000305|PubMed:7592354};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutants show reduced aromatic amino acids uptake.
CC {ECO:0000269|PubMed:7592354}.
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; X85965; CAA59950.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98500.1; -; Genomic_DNA.
DR EMBL; BX927151; CAF19813.1; -; Genomic_DNA.
DR PIR; S52754; S52754.
DR RefSeq; NP_600335.2; NC_003450.3.
DR RefSeq; WP_011014125.1; NC_006958.1.
DR AlphaFoldDB; Q46065; -.
DR SMR; Q46065; -.
DR STRING; 196627.cg1257; -.
DR TCDB; 2.A.3.1.12; the amino acid-polyamine-organocation (apc) family.
DR KEGG; cgb:cg1257; -.
DR KEGG; cgl:Cgl1107; -.
DR PATRIC; fig|196627.13.peg.1086; -.
DR eggNOG; COG1113; Bacteria.
DR HOGENOM; CLU_007946_9_2_11; -.
DR OMA; CIAYMNV; -.
DR Proteomes; UP000000582; 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 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..463
FT /note="Aromatic amino acid transport protein AroP"
FT /id="PRO_0000054192"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 463 AA; 49268 MW; 3071063590264F08 CRC64;
MAKSNEGLGT GLRTRHLTMM GLGSAIGAGL FLGTGVGIRA AGPAVLLAYI IAGAIVVLVM
QMLGEMAAAR PASGSFSRYG EDAFGHWAGF SLGWLYWFML IMVMGAEMTG AAAIMGAWFG
VEPWIPSLVC VVFFAVVNLV AVRGFGEFEY WFAFIKVAVI IAFLIIGIAL IFGWLPGSTF
VGTSNFIGDH GFMPNGISGV AAGLLAVAFA FGGIEIVTIA AAESDKPREA ISLAVRAVIW
RISVFYLGSV LVITFLMPYE SINGADTAAE SPFTQILAMA NIPGTVGFME AIIVLALLSA
FNAQIYATSR LVFSMANRQD APRVFSKLST SHVPTNAVLL SMFFAFVSVG LQYWNPAGLL
DFLLNAVGGC LIVVWAMITL SQLKLRKELQ ANDEISTVRM WAHPWLGILT LVLLAGLVAL
MLGDAASRSQ VYSVAIVYGF LVLLSFVTVN SPLRGGRTPS DLN
