ID   EAMB_SHIFL              Reviewed;         195 AA.
AC   Q83K22; Q7C0E0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Cysteine/O-acetylserine efflux protein {ECO:0000250|UniProtKB:P38101};
GN   Name=eamB; OrderedLocusNames=SF2640, S2813;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(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; AE005674; AAN44136.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17960.1; -; Genomic_DNA.
DR   RefSeq; NP_708429.1; NC_004337.2.
DR   RefSeq; WP_000187873.1; NZ_UIQL01000049.1.
DR   AlphaFoldDB; Q83K22; -.
DR   STRING; 198214.SF2640; -.
DR   EnsemblBacteria; AAN44136; AAN44136; SF2640.
DR   EnsemblBacteria; AAP17960; AAP17960; S2813.
DR   GeneID; 1025669; -.
DR   GeneID; 58391026; -.
DR   KEGG; sfl:SF2640; -.
DR   KEGG; sfx:S2813; -.
DR   PATRIC; fig|198214.7.peg.3150; -.
DR   HOGENOM; CLU_079569_1_2_6; -.
DR   OMA; NPKAWIM; -.
DR   OrthoDB; 1945085at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..195
FT                   /note="Cysteine/O-acetylserine efflux protein"
FT                   /id="PRO_0000318733"
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;  21260 MW;  D77D7B0A152ED16C CRC64;
     MTPILLSAFW TYTLITAMTP GPNNILALSS ATSHGFRQST RVLAGMSLGF LIVMLLCAGI
     SFSLAVIDPA AVHLLSWAGA AYIVWLAWKI ATSPTKEDGL QAKPISFWAS FALQFVNVKI
     ILYGVTALST FVLPQTQALS WVVGVSVLLA MIGTFGNVCW ALAGHLFQRL FRQYGRQLNI
     VLALLLVYCA VRIFY