EAMB_ECOUT
ID EAMB_ECOUT Reviewed; 195 AA.
AC Q1R8F4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Cysteine/O-acetylserine efflux protein {ECO:0000250|UniProtKB:P38101};
GN Name=eamB; OrderedLocusNames=UTI89_C2900;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE08360.1; -; Genomic_DNA.
DR RefSeq; WP_000189209.1; NC_007946.1.
DR AlphaFoldDB; Q1R8F4; -.
DR EnsemblBacteria; ABE08360; ABE08360; UTI89_C2900.
DR KEGG; eci:UTI89_C2900; -.
DR HOGENOM; CLU_079569_1_2_6; -.
DR OMA; NPKAWIM; -.
DR Proteomes; UP000001952; 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_0000318720"
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