EAMB_ECO57
ID EAMB_ECO57 Reviewed; 195 AA.
AC Q8XA19; Q7ABJ3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Cysteine/O-acetylserine efflux protein {ECO:0000250|UniProtKB:P38101};
GN Name=eamB; OrderedLocusNames=Z3861, ECs3444;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG57694.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36867.1; -; Genomic_DNA.
DR PIR; B85904; B85904.
DR PIR; D91059; D91059.
DR RefSeq; NP_311471.1; NC_002695.1.
DR RefSeq; WP_000189215.1; NZ_SDVX01000004.1.
DR AlphaFoldDB; Q8XA19; -.
DR STRING; 155864.EDL933_3743; -.
DR EnsemblBacteria; AAG57694; AAG57694; Z3861.
DR EnsemblBacteria; BAB36867; BAB36867; ECs_3444.
DR GeneID; 914882; -.
DR KEGG; ece:Z3861; -.
DR KEGG; ecs:ECs_3444; -.
DR PATRIC; fig|386585.9.peg.3599; -.
DR eggNOG; COG1280; Bacteria.
DR HOGENOM; CLU_079569_1_2_6; -.
DR OMA; NPKAWIM; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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_0000318722"
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; 21301 MW; 54DA47EF23488F07 CRC64;
MTPTLLSAFW TYTLITAMTP GPNNILALSS ATTHGFHQST RVLAGMSLGF LIVMLLCAGI
SFSLAVIDPA AVHLLSWAGA AYIVWLAWKI ATSPTKEDGL QTKPISFWAS FALQFVNVKI
ILYGVTALST FVLPQTQALS WIVGVSVLLA MIGTFGNVCW ALAGHLFQRL FRQYGRQLNI
VLALLLIYCA VRIFY
