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Database: UniProt
Entry: A0A1I0SAX6_9BACT
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ID   A0A1I0SAX6_9BACT        Unreviewed;       477 AA.
AC   A0A1I0SAX6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Aromatic amino acid transport protein AroP {ECO:0000256|ARBA:ARBA00040443};
DE   AltName: Full=Aromatic amino acid:H(+) symporter AroP {ECO:0000256|ARBA:ARBA00041728};
DE   AltName: Full=General aromatic amino acid permease {ECO:0000256|ARBA:ARBA00042267};
GN   ORFNames=SAMN04488122_5682 {ECO:0000313|EMBL:SEW53786.1};
OS   Chitinophaga arvensicola.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=29529 {ECO:0000313|EMBL:SEW53786.1, ECO:0000313|Proteomes:UP000199310};
RN   [1] {ECO:0000313|EMBL:SEW53786.1, ECO:0000313|Proteomes:UP000199310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3695 {ECO:0000313|EMBL:SEW53786.1,
RC   ECO:0000313|Proteomes:UP000199310};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00037317}.
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:0000256|ARBA:ARBA00035783};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28925;
CC         Evidence={ECO:0000256|ARBA:ARBA00035783};
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:0000256|ARBA:ARBA00036067};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28881;
CC         Evidence={ECO:0000256|ARBA:ARBA00036067};
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:0000256|ARBA:ARBA00036013};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28877;
CC         Evidence={ECO:0000256|ARBA:ARBA00036013};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; FOJG01000002; SEW53786.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0SAX6; -.
DR   STRING; 29529.SAMN04488122_5682; -.
DR   OrthoDB; 9780162at2; -.
DR   Proteomes; UP000199310; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006865; P:amino acid transport; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR   InterPro; IPR004841; AA-permease/SLC12A_dom.
DR   InterPro; IPR004840; Amoino_acid_permease_CS.
DR   PANTHER; PTHR43495:SF4; AROMATIC AMINO ACID TRANSPORT PROTEIN AROP; 1.
DR   PANTHER; PTHR43495; GABA PERMEASE; 1.
DR   Pfam; PF00324; AA_permease; 1.
DR   PIRSF; PIRSF006060; AA_transporter; 1.
DR   PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE   4: Predicted;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        21..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        86..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        127..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        156..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        252..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        302..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        360..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        385..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        424..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        452..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..470
FT                   /note="Amino acid permease/ SLC12A"
FT                   /evidence="ECO:0000259|Pfam:PF00324"
SQ   SEQUENCE   477 AA;  52425 MW;  41B7185FDAA9E3F3 CRC64;
     MKATNENTGA DHLKRGLQNR HIQLIALGGA IGTGLFLGIG PAAVLAGPSV ILGYALAGVI
     AFFIMRQLGE MVVEEPVSGS FSHFAYKYWG TFAGFASGWN YWILYILVSM SELTAIGVYV
     HFWWPEIPLW SSSLFFFIAI NALNLSSVKV YGEAEFWFSI IKVVAIIAMI CFGTYLLISG
     SGGEQASIQN LWNDGGFFPK GLLESDGKGG FQGLFAAIAL IMFSFGGLEL IGITAAEADK
     PEKTIPKATN QVIYRILIFY VGALIILFAL SPWRSITTTS SPFVMVFESL KGFQFTLMGH
     TVYFTSLIAN VLNLIVLTAA LSVYNSCVYS NSRMLYGLAR QGNAPAFLSK LNHNHVPVKA
     ILVSGLFAAI CIVINKVIPE KALEVLMSLV VSTLIINWLM ISVVHLKFKQ HKTAANIRTK
     FPSFIYPVSN YICLVFLVGI LVLMWITGMK LPVALIPGWV IFLYLCYLLV KRNNRQG
//
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