AROP_SHIFL
ID AROP_SHIFL Reviewed; 457 AA.
AC P59737;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 114.
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=SF0109, S0111;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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: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; AE005674; AAN41773.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP15654.1; -; Genomic_DNA.
DR RefSeq; NP_706066.1; NC_004337.2.
DR RefSeq; WP_000969912.1; NZ_WPGW01000007.1.
DR AlphaFoldDB; P59737; -.
DR SMR; P59737; -.
DR STRING; 198214.SF0109; -.
DR EnsemblBacteria; AAN41773; AAN41773; SF0109.
DR EnsemblBacteria; AAP15654; AAP15654; S0111.
DR GeneID; 1024518; -.
DR GeneID; 58392248; -.
DR KEGG; sfl:SF0109; -.
DR KEGG; sfx:S0111; -.
DR PATRIC; fig|198214.7.peg.123; -.
DR HOGENOM; CLU_007946_9_3_6; -.
DR OMA; VIMYLTP; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000054198"
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..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 421..425
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 457 AA; 49676 MW; B3A7782F71BD5FBE CRC64;
MMEGQQHGEQ LKRGLKNRHI QLIALGGAIG TGLFLGSASV IQSAGPGIIL GYAIAGFIAF
LIMRQLGEMV VEEPVAGSFS HFAYKYWGSF AGFASGWNYW VLYVLVAMAE LTAVGKYIQF
WYPEIPTWVS AAVFFVVINA INLTNVKVFG 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 LFMAAVLVIM
LMTPGMAISV YLIPVWLIVL GIGYLFKEKT AKAVKAH
