ID N9C798_9GAMM Unreviewed; 451 AA.
AC N9C798;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=F941_02865 {ECO:0000313|EMBL:ENV81722.1};
OS Acinetobacter bouvetii DSM 14964 = CIP 107468.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1120925 {ECO:0000313|EMBL:ENV81722.1, ECO:0000313|Proteomes:UP000018460};
RN [1] {ECO:0000313|EMBL:ENV81722.1, ECO:0000313|Proteomes:UP000018460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 107468 {ECO:0000313|EMBL:ENV81722.1,
RC ECO:0000313|Proteomes:UP000018460};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter bouvetii CIP 107468.";
RL Submitted (FEB-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENV81722.1}.
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DR EMBL; APQD01000021; ENV81722.1; -; Genomic_DNA.
DR RefSeq; WP_005012721.1; NZ_KB892277.1.
DR AlphaFoldDB; N9C798; -.
DR PATRIC; fig|1120925.3.peg.3006; -.
DR eggNOG; COG1113; Bacteria.
DR OrthoDB; 5297508at2; -.
DR Proteomes; UP000018460; Unassembled WGS sequence.
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 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 19..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 397..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..421
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
SQ SEQUENCE 451 AA; 50565 MW; 895DF40AB876310D CRC64;
MNSETPQLQR RLKNRHIQLI AMGGAIGTGL FLGSAHIIES AGPSIILGYM IGGLIAFLIM
RQLGEMIVHE PVTGSFSYFA FKYWGKFSGF LTGWNYWILY ILVVMTELTA IGKYVNYWWP
HIPAWVSVLV FFAVITLANL ANVKLYAESE FWLSMIKVVA IVAMILFGVY LLMTADAGST
ASISNLWTHG GFFPHGFEGL FYMLAFMMFA FGGIELISMA AAETEDPEKN IPKAVNQTVI
RVFLFYICSL AVLLSLVPWN QLELGGLDHS PFVMIFQQMG IDWAAHLLNF IILTASVSVC
NSGMYANSRM LLGLAEQGNA PKVFTQVNQH GTPIAAVLFS ALLIFGCVLL NYFLPEKALS
YLIYIVVAAA VLNWMLISLI HLKFRKAMKQ QGIQTKFLAL FAPFTNYFVL AFMLMILYIM
WTQGFMLSVL MLPVWILLLF VLFKIMQAKK A
//
