EAMB_ECOLI
ID EAMB_ECOLI Reviewed; 195 AA.
AC P38101;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cysteine/O-acetylserine efflux protein {ECO:0000305};
GN Name=eamB; Synonyms=yfiK; OrderedLocusNames=b2578, JW2562;
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;
RA Nashimoto H.;
RT "Non-ribosomal proteins affecting the assembly of ribosomes in Escherichia
RT coli.";
RL (In) Nierhaus K.H. (eds.);
RL The translational apparatus, pp.185-195, Plenum Press, New York (1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nashimoto H., Saito N.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=12562784; DOI=10.1128/jb.185.4.1161-1166.2003;
RA Franke I., Resch A., Dassler T., Maier T., Boeck A.;
RT "YfiK from Escherichia coli promotes export of O-acetylserine and
RT cysteine.";
RL J. Bacteriol. 185:1161-1166(2003).
RN [7]
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: Exporter of O-acetylserine (OAS) and cysteine.
CC {ECO:0000269|PubMed:12562784}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O-acetyl-L-serine(in) = O-acetyl-L-serine(out);
CC Xref=Rhea:RHEA:29659, ChEBI:CHEBI:58340;
CC Evidence={ECO:0000269|PubMed:12562784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29660;
CC Evidence={ECO:0000269|PubMed:12562784};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteine(in) = L-cysteine(out); Xref=Rhea:RHEA:29655,
CC ChEBI:CHEBI:35235; Evidence={ECO:0000269|PubMed:12562784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29656;
CC Evidence={ECO:0000269|PubMed:12562784};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:12562784,
CC ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the Rht family. {ECO:0000305}.
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DR EMBL; D13169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D64044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; AAC75631.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16464.1; -; Genomic_DNA.
DR PIR; A65036; A65036.
DR RefSeq; NP_417073.1; NC_000913.3.
DR RefSeq; WP_000189207.1; NZ_LN832404.1.
DR AlphaFoldDB; P38101; -.
DR BioGRID; 4261635; 13.
DR STRING; 511145.b2578; -.
DR TCDB; 2.A.76.1.4; the resistance to homoserine/threonine (rhtb) family.
DR PaxDb; P38101; -.
DR PRIDE; P38101; -.
DR EnsemblBacteria; AAC75631; AAC75631; b2578.
DR EnsemblBacteria; BAA16464; BAA16464; BAA16464.
DR GeneID; 947065; -.
DR KEGG; ecj:JW2562; -.
DR KEGG; eco:b2578; -.
DR PATRIC; fig|1411691.4.peg.4156; -.
DR EchoBASE; EB2339; -.
DR eggNOG; COG1280; Bacteria.
DR HOGENOM; CLU_079569_1_2_6; -.
DR InParanoid; P38101; -.
DR OMA; NPKAWIM; -.
DR PhylomeDB; P38101; -.
DR BioCyc; EcoCyc:EG12445-MON; -.
DR BioCyc; MetaCyc:EG12445-MON; -.
DR PRO; PR:P38101; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR GO; GO:0033228; P:cysteine export across plasma membrane; IMP:EcoCyc.
DR InterPro; IPR001123; LeuE-type.
DR PANTHER; PTHR30086; PTHR30086; 1.
DR Pfam; PF01810; LysE; 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..195
FT /note="Cysteine/O-acetylserine efflux protein"
FT /id="PRO_0000094743"
FT TOPO_DOM 1..7
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..69
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..141
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 177..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 195 AA; 21248 MW; 5F86B828DDDEC090 CRC64;
MTPTLLSAFW TYTLITAMTP GPNNILALSS ATSHGFRQST RVLAGMSLGF LIVMLLCAGI
SFSLAVIDPA AVHLLSWAGA AYIVWLAWKI ATSPTKEDGL QAKPISFWAS FALQFVNVKI
ILYGVTALST FVLPQTQALS WVVGVSVLLA MIGTFGNVCW ALAGHLFQRL FRQYGRQLNI
VLALLLVYCA VRIFY
