ID   EAMB_SALTI              Reviewed;         195 AA.
AC   Q8Z4J7; Q7CBN2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Cysteine/O-acetylserine efflux protein {ECO:0000250|UniProtKB:P38101};
GN   Name=eamB; OrderedLocusNames=STY2838, t0265;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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; AE014613; AAO67991.1; -; Genomic_DNA.
DR   EMBL; AL513382; CAD02794.1; -; Genomic_DNA.
DR   RefSeq; NP_457120.1; NC_003198.1.
DR   RefSeq; WP_000188410.1; NZ_UCTX01000011.1.
DR   AlphaFoldDB; Q8Z4J7; -.
DR   STRING; 220341.16503803; -.
DR   EnsemblBacteria; AAO67991; AAO67991; t0265.
DR   KEGG; stt:t0265; -.
DR   KEGG; sty:STY2838; -.
DR   PATRIC; fig|220341.7.peg.2887; -.
DR   eggNOG; COG1280; Bacteria.
DR   HOGENOM; CLU_079569_1_2_6; -.
DR   OMA; NPKAWIM; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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_0000318730"
FT   TOPO_DOM        1..9
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..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;  21335 MW;  EF30142B85995E85 CRC64;
     MTPMLLSAFW TYTLITALTP GPNNILALSA ATAHGFRQSI RVLAGMSLGF LVVMLLCAGI
     AFSLAVIDPA IIHLLSWVGA AYILWLAWKI ATSPAADEKV RPKPVGFWVS FGLQFVNVKI
     ILYGITALST FVLPQTQALN WVIGVSILLA LIGTFGNVCW ALAGHLFQRA FRHYGRQLNI
     ILALLLVYCA VRIFY