MTR_ECOLI
ID MTR_ECOLI Reviewed; 414 AA.
AC P0AAD2; P22306; Q2M949;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Tryptophan-specific transport protein;
DE AltName: Full=Tryptophan permease;
GN Name=mtr; OrderedLocusNames=b3161, JW3130;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1987112; DOI=10.1128/jb.173.1.108-115.1991;
RA Heatwole V.M., Somerville R.L.;
RT "Cloning, nucleotide sequence, and characterization of mtr, the structural
RT gene for a tryptophan-specific permease of Escherichia coli K-12.";
RL J. Bacteriol. 173:108-115(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2061290; DOI=10.1128/jb.173.13.4133-4143.1991;
RA Sarsero J.P., Wookey P.J., Pittard A.J.;
RT "Regulation of expression of the Escherichia coli K-12 mtr gene by TyrR
RT protein and Trp repressor.";
RL J. Bacteriol. 173:4133-4143(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX PubMed=1904443; DOI=10.1128/jb.173.11.3601-3604.1991;
RA Heatwole V.M., Somerville R.L.;
RT "The tryptophan-specific permease gene, mtr, is differentially regulated by
RT the tryptophan and tyrosine repressors in Escherichia coli K-12.";
RL J. Bacteriol. 173:3601-3604(1991).
RN [6]
RP TOPOLOGY.
RX PubMed=7814318; DOI=10.1128/jb.177.2.297-306.1995;
RA Sarsero J.P., Pittard A.J.;
RT "Membrane topology analysis of Escherichia coli K-12 Mtr permease by
RT alkaline phosphatase and beta-galactosidase fusions.";
RL J. Bacteriol. 177:297-306(1995).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Involved in transporting tryptophan across the cytoplasmic
CC membrane.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- INDUCTION: By phenylalanine under the control of regulatory protein
CC TyrR.
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; M59862; AAA24182.1; -; Genomic_DNA.
DR EMBL; M58338; AAA24183.1; -; Genomic_DNA.
DR EMBL; U18997; AAA57964.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76195.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77207.1; -; Genomic_DNA.
DR PIR; A39187; A39187.
DR RefSeq; NP_417630.1; NC_000913.3.
DR RefSeq; WP_000224351.1; NZ_LN832404.1.
DR AlphaFoldDB; P0AAD2; -.
DR SMR; P0AAD2; -.
DR BioGRID; 4259278; 178.
DR STRING; 511145.b3161; -.
DR TCDB; 2.A.42.1.2; the hydroxy/aromatic amino acid permease (haaap) family.
DR jPOST; P0AAD2; -.
DR PaxDb; P0AAD2; -.
DR PRIDE; P0AAD2; -.
DR EnsemblBacteria; AAC76195; AAC76195; b3161.
DR EnsemblBacteria; BAE77207; BAE77207; BAE77207.
DR GeneID; 947675; -.
DR KEGG; ecj:JW3130; -.
DR KEGG; eco:b3161; -.
DR PATRIC; fig|1411691.4.peg.3569; -.
DR EchoBASE; EB0612; -.
DR eggNOG; COG0814; Bacteria.
DR HOGENOM; CLU_038102_2_1_6; -.
DR InParanoid; P0AAD2; -.
DR OMA; LVKYYDR; -.
DR PhylomeDB; P0AAD2; -.
DR BioCyc; EcoCyc:MTR-MON; -.
DR BioCyc; MetaCyc:MTR-MON; -.
DR PRO; PR:P0AAD2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0022804; F:active transmembrane transporter activity; EXP:EcoCyc.
DR GO; GO:0005300; F:high-affinity tryptophan transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015293; F:symporter activity; IDA:EcoCyc.
DR GO; GO:0003333; P:amino acid transmembrane transport; IDA:EcoCyc.
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 1: Evidence at protein level;
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_0000093797"
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
