AROP_ECO57
ID AROP_ECO57 Reviewed; 457 AA.
AC Q8X968;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=Z0122, ECs0116;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG54416.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33539.1; -; Genomic_DNA.
DR PIR; D85494; D85494.
DR PIR; D90643; D90643.
DR RefSeq; NP_308143.1; NC_002695.1.
DR RefSeq; WP_010904500.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X968; -.
DR SMR; Q8X968; -.
DR STRING; 155864.EDL933_0113; -.
DR EnsemblBacteria; AAG54416; AAG54416; Z0122.
DR EnsemblBacteria; BAB33539; BAB33539; ECs_0116.
DR GeneID; 913640; -.
DR KEGG; ece:Z0122; -.
DR KEGG; ecs:ECs_0116; -.
DR PATRIC; fig|386585.9.peg.214; -.
DR eggNOG; COG1113; Bacteria.
DR HOGENOM; CLU_007946_9_3_6; -.
DR OMA; VIMYLTP; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..457
FT /note="Aromatic amino acid transport protein AroP"
FT /id="PRO_0000054195"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..42
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..117
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..201
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..271
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..358
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 457 AA; 49663 MW; 20A0C2A5075BC7A7 CRC64;
MMEGQQHGEQ LKRGLKNRHI QLIALGGAIG TGLFLGSASV IQSAGPGIIL GYAIAGFIAF
LIMRQLGEMV VEEPVAGSFS HFAYKYWGSF AGFASGWNYW VLYVLVAMAE LTAVGKYIQF
WYPEIPTWVS AAVFFVVINA INLTNVTVFG EMEFWFAIIK VIAVVAMIIF GGWLLFSGNG
GPQASVSNLW DQGGFLPHGF TGLVMMMAII MFSFGGLELV GITAAEADNP EQSIPKATNQ
VIYRILIFYI GSLAVLLSLM PWTRVTADTS PFVLIFHELG DTFVANALNI VVLTAALSVY
NSCVYCNSRM LFGLAQQGNA PKALASVDKR GVPVNTILVS ALVTALCVLI NYLAPESAFG
LLMALVVSAL VINWAMISLA HMKFRRAKQE QGVVTRFPAL LYPLGNWICL LFMAVVLVIM
LMTPGMAISV YLIPVWLVVL GIGYLFKEKT AKAVKAH
