TYRP_SHIFL
ID TYRP_SHIFL Reviewed; 403 AA.
AC P0AAD5; P18199; P76309;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Tyrosine-specific transport system {ECO:0000250|UniProtKB:P0AAD4};
DE AltName: Full=Tyrosine permease {ECO:0000250|UniProtKB:P0AAD4};
DE AltName: Full=Tyrosine:H(+) symporter {ECO:0000250|UniProtKB:P0AAD4};
GN Name=tyrP; OrderedLocusNames=SF1953, S2046;
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: Transports tyrosine across the cytoplasmic membrane. The
CC transport system is energized by the proton motive force.
CC {ECO:0000250|UniProtKB:P0AAD4}.
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:P0AAD4};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AAD4}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC Mtr/TnaB/TyrP permease subfamily. {ECO:0000305}.
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DR EMBL; AE005674; AAN43504.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17334.1; -; Genomic_DNA.
DR RefSeq; NP_707797.1; NC_004337.2.
DR RefSeq; WP_000797560.1; NZ_UIQL01000018.1.
DR AlphaFoldDB; P0AAD5; -.
DR STRING; 198214.SF1953; -.
DR EnsemblBacteria; AAN43504; AAN43504; SF1953.
DR EnsemblBacteria; AAP17334; AAP17334; S2046.
DR GeneID; 1025130; -.
DR GeneID; 58461789; -.
DR KEGG; sfl:SF1953; -.
DR KEGG; sfx:S2046; -.
DR PATRIC; fig|198214.7.peg.2332; -.
DR HOGENOM; CLU_038102_3_0_6; -.
DR OMA; PHIHQVN; -.
DR OrthoDB; 935253at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR InterPro; IPR018227; Amino_acid_transport_2.
DR InterPro; IPR013061; Trp/try_permease_CS.
DR InterPro; IPR013059; Trp_tyr_transpt.
DR PANTHER; PTHR46997; PTHR46997; 1.
DR Pfam; PF03222; Trp_Tyr_perm; 1.
DR PRINTS; PR00166; AROAAPRMEASE.
DR TIGRFAMs; TIGR00837; araaP; 1.
DR PROSITE; PS00594; AROMATIC_AA_PERMEASE_1; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..403
FT /note="Tyrosine-specific transport system"
FT /id="PRO_0000093807"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..34
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..121
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..183
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..274
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..331
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..403
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AAD4"
SQ SEQUENCE 403 AA; 42819 MW; 7BECCAA833679796 CRC64;
MKNRTLGSVF IVAGTTIGAG MLAMPLAAAG VGFSVTLILL IGLWALMCYT ALLLLEVYQH
VPADTGLGTL AKRYLGRYGQ WLTGFSMMFL MYALTAAYIS GAGELLASSI SDWTGISMSA
TAGVLLFTFV AGGVVCVGTS LVDLFNRFLF SAKIIFLVVM LVLLLPHIHK VNLLTLPLQQ
GLALSAIPVI FTSFGFHGSV PSIVSYMDGN IRKLRWVFII GSAIPLVAYI FWQVATLGSI
DSTTFMGLLA NHAGLNGLLQ ALREMVASPH VELAVHLFAD LALATSFLGV ALGLFDYLAD
LFQRSNTVGG RLQTGAITFL PPLAFALFYP RGFVMALGYA GVALAVLALI IPSLLTWQSR
KHNPQAGYRV KGGRPALVVV FLCGIAVIGV QFLIAAGLLP EVG
