YJEH_ECOLI
ID YJEH_ECOLI Reviewed; 418 AA.
AC P39277; Q2M6G3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=L-methionine/branched-chain amino acid exporter YjeH {ECO:0000305};
GN Name=yjeH; OrderedLocusNames=b4141, JW4101;
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 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
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 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).
RN [5]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF THR-24; GLY-25 AND TRP-195.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=26319875; DOI=10.1128/aem.02242-15;
RA Liu Q., Liang Y., Zhang Y., Shang X., Liu S., Wen J., Wen T.;
RT "YjeH is a novel exporter of L-methionine and branched-chain amino acids in
RT Escherichia coli.";
RL Appl. Environ. Microbiol. 81:7753-7766(2015).
CC -!- FUNCTION: Catalyzes the efflux of L-methionine. Can also export L-
CC leucine, L-isoleucine and L-valine. Activity is dependent on
CC electrochemical potential. {ECO:0000269|PubMed:26319875}.
CC -!- ACTIVITY REGULATION: Efflux is inhibited by carbonyl cyanide m-
CC chlorophenylhydrazone (CCCP). {ECO:0000269|PubMed:26319875}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:26319875}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced in the presence of intracellular L-methionine, L-
CC leucine or L-isoleucine. {ECO:0000269|PubMed:26319875}.
CC -!- DISRUPTION PHENOTYPE: Deletion increases the susceptibility to DL-
CC ethionine, DL-norleucine and DL-norvaline. Deletion also results in
CC intracellular accumulation and a reduced rate of export of methionine
CC in the presence of extracellular Met-Met dipeptides.
CC {ECO:0000269|PubMed:26319875}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. Amino acid efflux (AAE) (TC 2.A.3.13) family.
CC {ECO:0000305}.
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DR EMBL; U14003; AAA97040.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77101.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78143.1; -; Genomic_DNA.
DR PIR; S56369; S56369.
DR RefSeq; NP_418565.1; NC_000913.3.
DR RefSeq; WP_000015837.1; NZ_STEB01000014.1.
DR AlphaFoldDB; P39277; -.
DR SMR; P39277; -.
DR BioGRID; 4262197; 12.
DR BioGRID; 852948; 1.
DR DIP; DIP-12573N; -.
DR IntAct; P39277; 4.
DR STRING; 511145.b4141; -.
DR TCDB; 2.A.3.13.1; the amino acid-polyamine-organocation (apc) family.
DR PaxDb; P39277; -.
DR PRIDE; P39277; -.
DR EnsemblBacteria; AAC77101; AAC77101; b4141.
DR EnsemblBacteria; BAE78143; BAE78143; BAE78143.
DR GeneID; 66671947; -.
DR GeneID; 948656; -.
DR KEGG; ecj:JW4101; -.
DR KEGG; eco:b4141; -.
DR PATRIC; fig|1411691.4.peg.2559; -.
DR EchoBASE; EB2363; -.
DR eggNOG; COG0531; Bacteria.
DR HOGENOM; CLU_007946_18_0_6; -.
DR InParanoid; P39277; -.
DR OMA; WWVGSRG; -.
DR PhylomeDB; P39277; -.
DR BioCyc; EcoCyc:B4141-MON; -.
DR BioCyc; MetaCyc:B4141-MON; -.
DR PRO; PR:P39277; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0000102; F:L-methionine secondary active transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0005294; F:neutral L-amino acid secondary active transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEP:EcoCyc.
DR GO; GO:1903714; P:isoleucine transmembrane transport; IMP:EcoCyc.
DR GO; GO:1903785; P:L-valine transmembrane transport; IMP:EcoCyc.
DR GO; GO:0015820; P:leucine transport; IMP:EcoCyc.
DR GO; GO:0015821; P:methionine transport; IMP:EcoCyc.
DR InterPro; IPR002293; AA/rel_permease1.
DR Pfam; PF13520; AA_permease_2; 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..418
FT /note="L-methionine/branched-chain amino acid exporter
FT YjeH"
FT /id="PRO_0000169738"
FT TOPO_DOM 1..15
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..89
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..147
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..219
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..317
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..378
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT MUTAGEN 24
FT /note="T->Y: Strong decrease in methionine efflux."
FT /evidence="ECO:0000269|PubMed:26319875"
FT MUTAGEN 25
FT /note="G->F: Strong decrease in methionine efflux."
FT /evidence="ECO:0000269|PubMed:26319875"
FT MUTAGEN 195
FT /note="W->A: Strong decrease in methionine efflux."
FT /evidence="ECO:0000269|PubMed:26319875"
SQ SEQUENCE 418 AA; 44778 MW; 9244E8281BC54AC3 CRC64;
MSGLKQELGL AQGIGLLSTS LLGTGVFAVP ALAALVAGNN SLWAWPVLII LVFPIAIVFA
ILGRHYPSAG GVAHFVGMAF GSRLERVTGW LFLSVIPVGL PAALQIAAGF GQAMFGWHSW
QLLLAELGTL ALVWYIGTRG ASSSANLQTV IAGLIVALIV AIWWAGDIKP ANIPFPAPGN
IELTGLFAAL SVMFWCFVGL EAFAHLASEF KNPERDFPRA LMIGLLLAGL VYWGCTVVVL
HFDAYGEKMA AAASLPKIVV QLFGVGALWI ACVIGYLACF ASLNIYIQSF ARLVWSQAQH
NPDHYLARLS SRHIPNNALN AVLGCCVVST LVIHALEINL DALIIYANGI FIMIYLLCML
AGCKLLQGRY RLLAVVGGLL CVLLLAMVGW KSLYALIMLA GLWLLLPKRK TPENGITT
