EAMB_SHIF8
ID EAMB_SHIF8 Reviewed; 195 AA.
AC Q0T1S8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Cysteine/O-acetylserine efflux protein {ECO:0000250|UniProtKB:P38101};
GN Name=eamB; OrderedLocusNames=SFV_2641;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(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; CP000266; ABF04737.1; -; Genomic_DNA.
DR RefSeq; WP_000187873.1; NC_008258.1.
DR AlphaFoldDB; Q0T1S8; -.
DR EnsemblBacteria; ABF04737; ABF04737; SFV_2641.
DR GeneID; 58391026; -.
DR KEGG; sfv:SFV_2641; -.
DR HOGENOM; CLU_079569_1_2_6; -.
DR OMA; NPKAWIM; -.
DR BioCyc; SFLE373384:SFV_RS14685-MON; -.
DR Proteomes; UP000000659; 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_0000318734"
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