TYRP_ECOLI
ID TYRP_ECOLI Reviewed; 403 AA.
AC P0AAD4; P18199; P76309;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Tyrosine-specific transport system {ECO:0000303|PubMed:6090409};
DE AltName: Full=Tyrosine permease {ECO:0000305};
DE AltName: Full=Tyrosine:H(+) symporter {ECO:0000305};
GN Name=tyrP {ECO:0000303|PubMed:6090409}; OrderedLocusNames=b1907, JW1895;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3049553; DOI=10.1128/jb.170.10.4946-4949.1988;
RA Wookey P.J., Pittard A.J.;
RT "DNA sequence of the gene (tyrP) encoding the tyrosine-specific transport
RT system of Escherichia coli.";
RL J. Bacteriol. 170:4946-4949(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
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 FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND TRANSCRIPTIONAL REGULATION BY TYRR.
RC STRAIN=K12;
RX PubMed=6090409; DOI=10.1128/jb.160.1.169-174.1984;
RA Wookey P.J., Pittard J., Forrest S.M., Davidson B.E.;
RT "Cloning of the tyrP gene and further characterization of the tyrosine-
RT specific transport system in Escherichia coli K-12.";
RL J. Bacteriol. 160:169-174(1984).
RN [6]
RP TRANSCRIPTIONAL REGULATION BY TYRR.
RC STRAIN=K12;
RX PubMed=1860819; DOI=10.1128/jb.173.16.5068-5078.1991;
RA Andrews A.E., Lawley B., Pittard A.J.;
RT "Mutational analysis of repression and activation of the tyrP gene in
RT Escherichia coli.";
RL J. Bacteriol. 173:5068-5078(1991).
RN [7]
RP TRANSCRIPTIONAL REGULATION BY TYRR.
RX PubMed=15049824; DOI=10.1111/j.1365-2958.2003.03965.x;
RA Yang J., Hwang J.S., Camakaris H., Irawaty W., Ishihama A., Pittard J.;
RT "Mode of action of the TyrR protein: repression and activation of the tyrP
RT promoter of Escherichia coli.";
RL Mol. Microbiol. 52:243-256(2004).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
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: Transports tyrosine across the cytoplasmic membrane
CC (PubMed:6090409). The transport system is energized by the proton
CC motive force (PubMed:6090409). {ECO:0000269|PubMed:6090409}.
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:0000269|PubMed:6090409};
CC -!- ACTIVITY REGULATION: Inhibited by the uncoupler carbonyl cyanide m-
CC chlorophenylhydrazone (CCCP). {ECO:0000269|PubMed:6090409}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.9 uM for tyrosine {ECO:0000269|PubMed:6090409};
CC Vmax=14 nmol/min/mg enzyme {ECO:0000269|PubMed:6090409};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:6090409}; Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Repressed by tyrosine and induced by phenylalanine under the
CC control of the regulatory protein TyrR (PubMed:6090409, PubMed:1860819,
CC PubMed:15049824). The promoter region of tyrP contains two adjacent
CC TyrR boxes, which are the targets for the action of TyrR
CC (PubMed:1860819, PubMed:15049824). In the presence of tyrosine and ATP,
CC binding of hexameric TyrR to both TyrR boxes inhibits binding of RNA
CC polymerase (RNAP) to the tyrP promoter and leads to tyrosine-mediated
CC repression of the gene (PubMed:1860819, PubMed:15049824). In the
CC presence of phenylalanine, TyrR binds as a dimer to the upstream box,
CC which enhances the binding of RNAP to the tyrP promoter and leads to
CC phenylalanine-mediated activation (PubMed:1860819).
CC {ECO:0000269|PubMed:15049824, ECO:0000269|PubMed:1860819,
CC ECO:0000269|PubMed:6090409}.
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; M23240; AAA24705.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74977.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15730.1; -; Genomic_DNA.
DR PIR; C64954; GRECY.
DR RefSeq; NP_416420.1; NC_000913.3.
DR RefSeq; WP_000797560.1; NZ_STEB01000026.1.
DR AlphaFoldDB; P0AAD4; -.
DR BioGRID; 4262055; 8.
DR DIP; DIP-48105N; -.
DR IntAct; P0AAD4; 1.
DR STRING; 511145.b1907; -.
DR TCDB; 2.A.42.1.1; the hydroxy/aromatic amino acid permease (haaap) family.
DR PaxDb; P0AAD4; -.
DR PRIDE; P0AAD4; -.
DR EnsemblBacteria; AAC74977; AAC74977; b1907.
DR EnsemblBacteria; BAA15730; BAA15730; BAA15730.
DR GeneID; 58461789; -.
DR GeneID; 946412; -.
DR KEGG; ecj:JW1895; -.
DR KEGG; eco:b1907; -.
DR PATRIC; fig|1411691.4.peg.340; -.
DR EchoBASE; EB1034; -.
DR eggNOG; COG0814; Bacteria.
DR HOGENOM; CLU_038102_3_0_6; -.
DR InParanoid; P0AAD4; -.
DR OMA; PHIHQVN; -.
DR PhylomeDB; P0AAD4; -.
DR BioCyc; EcoCyc:TYRP-MON; -.
DR PRO; PR:P0AAD4; -.
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: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 1: Evidence at protein level;
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_0000093804"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..34
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..121
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..183
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..274
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..331
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..403
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT CONFLICT 131..135
FT /note="AGGVV -> RRVAWL (in Ref. 1; AAA24705)"
FT /evidence="ECO:0000305"
FT CONFLICT 222..224
FT /note="SAI -> ECD (in Ref. 1; AAA24705)"
FT /evidence="ECO:0000305"
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
