ID   MERT_SHEPU              Reviewed;         115 AA.
AC   Q54462;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 60.
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;
OS   Shewanella putrefaciens (Pseudomonas putrefaciens).
OG   Plasmid IncJ pMERPH.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=24;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9167257; DOI=10.1111/j.1574-6976.1997.tb00300.x;
RA   Osborn A.M., Bruce K.D., Strike P., Ritchie D.A.;
RT   "Distribution, diversity and evolution of the bacterial mercury resistance
RT   (mer) operon.";
RL   FEMS Microbiol. Rev. 19:239-262(1997).
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; Z49196; CAA89054.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q54462; -.
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..115
FT                   /note="Mercuric transport protein MerT"
FT                   /id="PRO_0000096434"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         23
FT                   /ligand="Hg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:16793"
FT                   /evidence="ECO:0000250|UniProtKB:P04140"
FT   BINDING         24
FT                   /ligand="Hg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:16793"
FT                   /evidence="ECO:0000250|UniProtKB:P04140"
FT   BINDING         75
FT                   /ligand="Hg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:16793"
FT                   /evidence="ECO:0000250|UniProtKB:P04140"
FT   BINDING         81
FT                   /ligand="Hg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:16793"
FT                   /evidence="ECO:0000250|UniProtKB:P04140"
SQ   SEQUENCE   115 AA;  12555 MW;  C4ADC83CD389074E CRC64;
     MSKSNPNFPI IGGVIAAIGA GLCCAGPFVL LLLGVSGSWI GNLTLLEPYR PIFILLVLAL
     FGFAGWKVYR PVEDCEPGTS CAVPQVRKRR QVIFWLTALT ALVLVTSNYW IVWFA