MTR_SHIFL
ID MTR_SHIFL Reviewed; 414 AA.
AC P0AAD3; P22306;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Tryptophan-specific transport protein;
DE AltName: Full=Tryptophan permease;
GN Name=mtr; OrderedLocusNames=SF3202, S3419;
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: Involved in transporting tryptophan across the cytoplasmic
CC membrane. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- INDUCTION: By phenylalanine under the control of regulatory protein
CC TyrR. {ECO:0000250}.
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; AAN44669.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18483.1; -; Genomic_DNA.
DR RefSeq; NP_708962.1; NC_004337.2.
DR RefSeq; WP_000224351.1; NZ_WPGW01000004.1.
DR AlphaFoldDB; P0AAD3; -.
DR SMR; P0AAD3; -.
DR STRING; 198214.SF3202; -.
DR EnsemblBacteria; AAN44669; AAN44669; SF3202.
DR EnsemblBacteria; AAP18483; AAP18483; S3419.
DR GeneID; 1027142; -.
DR KEGG; sfl:SF3202; -.
DR KEGG; sfx:S3419; -.
DR PATRIC; fig|198214.7.peg.3801; -.
DR HOGENOM; CLU_038102_2_1_6; -.
DR OMA; LVKYYDR; -.
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 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; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..414
FT /note="Tryptophan-specific transport protein"
FT /id="PRO_0000093799"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 11..34
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 35..38
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 39..61
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 62..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 87..109
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 110..122
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 123..145
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 146..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 152..174
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 175..188
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 189..210
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 211..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 228..251
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 252..281
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 282..303
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 304..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 322..343
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 344..365
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 366..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 387..409
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 410..414
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 44333 MW; 87BF42540862FDD0 CRC64;
MATLTTTQTS PSLLGGVVII GGTIIGAGMF SLPVVMSGAW FFWSMAALIF TWFCMLHSGL
MILEANLNYR IGSSFDTITK DLLGKGWNVV NGISIAFVLY ILTYAYISAS GSILHHTFAE
MSLNVPARAA GFGFALLVAF VVWLSTKAVS RMTAIVLGAK VITFFLTFGS LLGHVQPATL
FNVAESNASY APYLLMTLPF CLASFGYHGN VPSLMKYYGK DPKTIVKCLV YGTLMALALY
TIWLLATMGN IPRPEFIGIA EKGGNIDVLV QALSGVLNSR SLDLLLVVFS NFAVASSFLG
VTLGLFDYLA DLFGFDDSAV GRLKTALLTF APPVVGGLLF PNGFLYAIGY AGLAATIWAA
IVPALLARAS RKRFGSPKFR VWGGKPMIAL ILVFGVGNAL VHILSSFNLL PVYQ
