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YDDG_ECOLI
ID   YDDG_ECOLI              Reviewed;         293 AA.
AC   P46136; P76124; P77342;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 3.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Aromatic amino acid exporter YddG {ECO:0000305};
GN   Name=yddG; OrderedLocusNames=b1473, JW1469;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
RC   STRAIN=K12;
RX   PubMed=1834669; DOI=10.1016/s0021-9258(18)54583-x;
RA   Berg B.L., Li J., Heider J., Stewart V.;
RT   "Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I.
RT   Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA)
RT   encodes selenocysteine.";
RL   J. Biol. Chem. 266:22380-22385(1991).
RN   [5]
RP   IDENTIFICATION.
RX   PubMed=7567469; DOI=10.1093/nar/23.17.3554;
RA   Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.;
RT   "Detection of new genes in a bacterial genome using Markov models for three
RT   gene classes.";
RL   Nucleic Acids Res. 23:3554-3562(1995).
RN   [6]
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).
RN   [7]
RP   FUNCTION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=17784858; DOI=10.1111/j.1574-6968.2007.00894.x;
RA   Doroshenko V., Airich L., Vitushkina M., Kolokolova A., Livshits V.,
RA   Mashko S.;
RT   "YddG from Escherichia coli promotes export of aromatic amino acids.";
RL   FEMS Microbiol. Lett. 275:312-318(2007).
RN   [8]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RC   STRAIN=K12;
RX   PubMed=21042032; DOI=10.1159/000320699;
RA   Airich L.G., Tsyrenzhapova I.S., Vorontsova O.V., Feofanov A.V.,
RA   Doroshenko V.G., Mashko S.V.;
RT   "Membrane topology analysis of the Escherichia coli aromatic amino acid
RT   efflux protein YddG.";
RL   J. Mol. Microbiol. Biotechnol. 19:189-197(2010).
RN   [9]
RP   FUNCTION.
RC   STRAIN=K12;
RX   PubMed=27281193; DOI=10.1038/nature17991;
RA   Tsuchiya H., Doki S., Takemoto M., Ikuta T., Higuchi T., Fukui K.,
RA   Usuda Y., Tabuchi E., Nagatoishi S., Tsumoto K., Nishizawa T., Ito K.,
RA   Dohmae N., Ishitani R., Nureki O.;
RT   "Structural basis for amino acid export by DMT superfamily transporter
RT   YddG.";
RL   Nature 534:417-420(2016).
CC   -!- FUNCTION: Amino acid transporter with broad substrate specificity
CC       (PubMed:17784858, PubMed:27281193). Can transport various amino acids,
CC       including phenylalanine, tyrosine, tryptophan, L-threonine, L-
CC       methionine, L-lysine, L-glutamate, L-valine and L-isoleucine
CC       (PubMed:17784858, PubMed:27281193). Overexpression confers resistance
CC       to phenylalanine and increases export of phenylalanine, tyrosine and
CC       tryptophan (PubMed:17784858). {ECO:0000269|PubMed:17784858,
CC       ECO:0000269|PubMed:27281193}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-phenylalanine(in) = L-phenylalanine(out);
CC         Xref=Rhea:RHEA:27950, ChEBI:CHEBI:58095;
CC         Evidence={ECO:0000305|PubMed:17784858};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosine(in) = L-tyrosine(out); Xref=Rhea:RHEA:68572,
CC         ChEBI:CHEBI:58315; Evidence={ECO:0000305|PubMed:17784858};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tryptophan(in) = L-tryptophan(out); Xref=Rhea:RHEA:70947,
CC         ChEBI:CHEBI:57912; Evidence={ECO:0000305|PubMed:17784858};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine(in) = L-threonine(out); Xref=Rhea:RHEA:35019,
CC         ChEBI:CHEBI:57926; Evidence={ECO:0000305|PubMed:27281193};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-methionine(in) = L-methionine(out); Xref=Rhea:RHEA:70939,
CC         ChEBI:CHEBI:57844; Evidence={ECO:0000305|PubMed:27281193};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysine(in) = L-lysine(out); Xref=Rhea:RHEA:70935,
CC         ChEBI:CHEBI:32551; Evidence={ECO:0000305|PubMed:27281193};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336,
CC         ChEBI:CHEBI:29985; Evidence={ECO:0000305|PubMed:27281193};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-valine(in) = L-valine(out); Xref=Rhea:RHEA:29703,
CC         ChEBI:CHEBI:57762; Evidence={ECO:0000305|PubMed:27281193};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-isoleucine(in) = L-isoleucine(out); Xref=Rhea:RHEA:70943,
CC         ChEBI:CHEBI:58045; Evidence={ECO:0000305|PubMed:27281193};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:21042032}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:21042032}.
CC   -!- SIMILARITY: Belongs to the drug/metabolite transporter (DMT)
CC       superfamily. Aromatic amino acid/paraquat exporter (ArAA/P-E) (TC
CC       2.A.7.17) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA15122.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U00096; AAD13437.3; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15122.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M75029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; D64900; D64900.
DR   RefSeq; NP_415990.5; NC_000913.3.
DR   RefSeq; WP_000198205.1; NZ_SSZK01000038.1.
DR   AlphaFoldDB; P46136; -.
DR   SMR; P46136; -.
DR   BioGRID; 4260205; 15.
DR   STRING; 511145.b1473; -.
DR   TCDB; 2.A.7.17.2; the drug/metabolite transporter (dmt) superfamily.
DR   PaxDb; P46136; -.
DR   PRIDE; P46136; -.
DR   EnsemblBacteria; AAD13437; AAD13437; b1473.
DR   EnsemblBacteria; BAA15122; BAA15122; BAA15122.
DR   GeneID; 945942; -.
DR   KEGG; ecj:JW1469; -.
DR   KEGG; eco:b1473; -.
DR   PATRIC; fig|511145.12.peg.1539; -.
DR   EchoBASE; EB2574; -.
DR   eggNOG; COG0697; Bacteria.
DR   HOGENOM; CLU_058959_1_1_6; -.
DR   InParanoid; P46136; -.
DR   OMA; VALWFHY; -.
DR   PhylomeDB; P46136; -.
DR   BioCyc; EcoCyc:EG12713-MON; -.
DR   BioCyc; MetaCyc:EG12713-MON; -.
DR   PRO; PR:P46136; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:EcoCyc.
DR   GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; IMP:EcoCyc.
DR   GO; GO:0032973; P:amino acid export across plasma membrane; IDA:EcoCyc.
DR   InterPro; IPR000620; EamA_dom.
DR   Pfam; PF00892; EamA; 2.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..293
FT                   /note="Aromatic amino acid exporter YddG"
FT                   /id="PRO_0000168943"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:21042032"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..33
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000269|PubMed:21042032"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..62
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:21042032"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        84..92
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000269|PubMed:21042032"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..118
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:21042032"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        140..155
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000269|PubMed:21042032"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        177..182
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:21042032"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..218
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000269|PubMed:21042032"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        240..243
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:21042032"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        265..267
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000269|PubMed:21042032"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        289..293
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:15919996,
FT                   ECO:0000269|PubMed:21042032"
FT   DOMAIN          6..137
FT                   /note="EamA 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          158..285
FT                   /note="EamA 2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   293 AA;  31539 MW;  45E02F367F3E562C CRC64;
     MTRQKATLIG LIAIVLWSTM VGLIRGVSEG LGPVGGAAAI YSLSGLLLIF TVGFPRIRQI
     PKGYLLAGSL LFVSYEICLA LSLGYAATHH QAIEVGMVNY LWPSLTILFA ILFNGQKTNW
     LIVPGLLLAL VGVCWVLGGD NGLHYDEIIN NITTSPLSYF LAFIGAFIWA AYCTVTNKYA
     RGFNGITVFV LLTGASLWVY YFLTPQPEMI FSTPVMIKLI SAAFTLGFAY AAWNVGILHG
     NVTIMAVGSY FTPVLSSALA AVLLSAPLSF SFWQGALMVC GGSLLCWLAT RRG
 
 
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