ID A0A087VW82_9BIFI Unreviewed; 498 AA.
AC A0A087VW82;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=BINDI_1329 {ECO:0000313|EMBL:AIC92583.1};
OS Bifidobacterium indicum LMG 11587 = DSM 20214.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1341694 {ECO:0000313|EMBL:AIC92583.1, ECO:0000313|Proteomes:UP000028569};
RN [1] {ECO:0000313|EMBL:AIC92583.1, ECO:0000313|Proteomes:UP000028569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11587 {ECO:0000313|EMBL:AIC92583.1,
RC ECO:0000313|Proteomes:UP000028569};
RX PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL Appl. Environ. Microbiol. 80:6290-6302(2014).
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}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family.
CC {ECO:0000256|ARBA:ARBA00008583}.
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DR EMBL; CP006018; AIC92583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087VW82; -.
DR KEGG; bii:BINDI_1329; -.
DR HOGENOM; CLU_007946_9_3_11; -.
DR OrthoDB; 5297508at2; -.
DR Proteomes; UP000028569; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000028569};
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 35..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 403..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 446..464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 470..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..475
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 54319 MW; 6E0009EC809B70CD CRC64;
MGQAGNTQTS GTEQGADGSR DTSNQMERGL SNRHVQFIAI GGTIGTGLFL GSGKSIALTG
PSIILVYIGV GLVMYLLMRA IGELMYRSPN QHTFIAFITR YLGKGWGSFA GWSYWIVLIL
IGMSELTAVG TYFVTFFGTF GINLEAWRGL IEVCFLAAMV SVNLIAVKVF GETEFWFSMI
KITLILAMIV TAVVMVIVGF RYPAVQMPGL DQVSPAGHAG LDNILNGLSL APNGWLAFFM
SFQMVFFAYE MIEFVGVTVS ETQNPRKVLP KAINQIIIRV LIFYVGALMA IMMIVPWRSF
KPNADGTFAS PFVMVFRYAG VDWAAGLVFF VVITAACSSL NSLLYSAGRN LFQLAAGGGS
PLMRSLYTIS RRGRVPARAI ILSGVLILLS PILHALPGFE NTFVLFTSAS SAVIIFIYIL
TLLAHHRYRA SDDFMPDGFL MPAYKVTGPI AIIFFLVIYV SLFFAPDTRI PAIFGLCWLA
VFGGICLWKH RNAVGVAG
//
