ID   EAMB_ECOL6              Reviewed;         195 AA.
AC   Q8FF11;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Cysteine/O-acetylserine efflux protein {ECO:0000250|UniProtKB:P38101};
GN   Name=eamB; OrderedLocusNames=c3102;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Exporter of O-acetylserine (OAS) and cysteine.
CC       {ECO:0000250|UniProtKB:P38101}.
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:0000250|UniProtKB:P38101};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29660;
CC         Evidence={ECO:0000250|UniProtKB:P38101};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteine(in) = L-cysteine(out); Xref=Rhea:RHEA:29655,
CC         ChEBI:CHEBI:35235; Evidence={ECO:0000250|UniProtKB:P38101};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29656;
CC         Evidence={ECO:0000250|UniProtKB:P38101};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P38101}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the Rht family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN81551.1; -; Genomic_DNA.
DR   RefSeq; WP_000189209.1; NC_004431.1.
DR   AlphaFoldDB; Q8FF11; -.
DR   STRING; 199310.c3102; -.
DR   EnsemblBacteria; AAN81551; AAN81551; c3102.
DR   KEGG; ecc:c3102; -.
DR   eggNOG; COG1280; Bacteria.
DR   HOGENOM; CLU_079569_1_2_6; -.
DR   OMA; NPKAWIM; -.
DR   BioCyc; ECOL199310:C3102-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001123; LeuE-type.
DR   PANTHER; PTHR30086; PTHR30086; 1.
DR   Pfam; PF01810; LysE; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..195
FT                   /note="Cysteine/O-acetylserine efflux protein"
FT                   /id="PRO_0000318724"
FT   TOPO_DOM        1..7
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..46
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..69
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        91..104
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..141
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..176
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        195
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P38101"
SQ   SEQUENCE   195 AA;  21278 MW;  295DD583ADCA8584 CRC64;
     MTPTLLSAFW TYTLITAMTP GPNNILALSS ATSHGFRQST RVLAGMSLGF LIVMLLCAGI
     SFSLAVIDPA AVHLLSWAGA AYIVWLAWKI ATSPTKEDGL QTKPISFWAS FALQFVNVKI
     ILYGVTALST FVLPQTQALS WVVGVSVLLA MIGTFGNVCW ALAGHLFQRL FRQYGRQLNI
     VLALLLVYCA VRIFY