EAMB_SALCH
ID EAMB_SALCH Reviewed; 195 AA.
AC Q57L56;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Cysteine/O-acetylserine efflux protein {ECO:0000250|UniProtKB:P38101};
GN Name=eamB; OrderedLocusNames=SCH_2650;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX66556.1; -; Genomic_DNA.
DR RefSeq; WP_000188414.1; NC_006905.1.
DR AlphaFoldDB; Q57L56; -.
DR EnsemblBacteria; AAX66556; AAX66556; SCH_2650.
DR KEGG; sec:SCH_2650; -.
DR HOGENOM; CLU_079569_1_2_6; -.
DR OMA; NPKAWIM; -.
DR Proteomes; UP000000538; 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_0000318728"
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; 21293 MW; B63E83C2FB104EE3 CRC64;
MTPMLLSAFW TYTLITALTP GPNNILALSA ATAHGFRQSI RVLAGMSLGF LVVMLLCAGI
AFSLAVIDPA IIHLLSWVGA AYILWLAWKI ATSPAADENA RPKPVGFWVS FGLQFVNVKI
ILYGITALST FVLPQTQALN WVIGVSILLA LIGTFGNVCW ALAGHLFQRA FRHYGRQLNI
ILALLLVYCA VRIFY