MERT_SALTI
ID MERT_SALTI Reviewed; 116 AA.
AC P0A219; P04336;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Mercuric transport protein MerT {ECO:0000250|UniProtKB:P04140};
DE AltName: Full=Mercury ion transport protein {ECO:0000250|UniProtKB:P04140};
GN Name=merT; OrderedLocusNames=HCM1.234c;
OS Salmonella typhi.
OG Plasmid pHCM1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
CC -!- FUNCTION: Involved in mercury resistance. Probably transfers a mercuric
CC ion from the periplasmic Hg(2+)-binding protein MerP to the cytoplasmic
CC mercuric reductase MerA. {ECO:0000250|UniProtKB:P04140}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the MerT family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL513383; CAD09816.1; -; Genomic_DNA.
DR RefSeq; NP_569424.1; NC_003384.1.
DR RefSeq; WP_001294663.1; NZ_WSUR01000067.1.
DR AlphaFoldDB; P0A219; -.
DR KEGG; sty:HCM1.234c; -.
DR PATRIC; fig|220341.7.peg.5251; -.
DR HOGENOM; CLU_151729_0_0_6; -.
DR OMA; MEPERVN; -.
DR Proteomes; UP000000541; Plasmid pHCM1.
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:0015097; F:mercury ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR003457; Transprt_MerT.
DR Pfam; PF02411; MerT; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Mercuric resistance; Mercury;
KW Metal-binding; Plasmid; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..116
FT /note="Mercuric transport protein MerT"
FT /id="PRO_0000096432"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 24
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000250|UniProtKB:P04140"
FT BINDING 25
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000250|UniProtKB:P04140"
FT BINDING 76
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000250|UniProtKB:P04140"
FT BINDING 82
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000250|UniProtKB:P04140"
SQ SEQUENCE 116 AA; 12521 MW; 8CF0744F4B0F6EE4 CRC64;
MSEPQNGRGA LFAGGLAAIL ASTCCLGPLV LVALGFSGAW IGNLTVLEPY RPLFIGAALV
ALFFAWKRIY RPVQACKPGE VCAIPQVRAT YKLIFWIVAV LVLVALGFPY VVPFFY
