ID   MERT_ACICA              Reviewed;         116 AA.
AC   Q52106;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 68.
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 {ECO:0000303|PubMed:8302940};
OS   Acinetobacter calcoaceticus.
OG   Plasmid pKLH2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8302940; DOI=10.1006/plas.1993.1064;
RA   Kholodii G.Y., Lomovskaya O.L., Gorlenko Z.M., Mindlin S.Z., Yurieva O.V.,
RA   Nikiforov V.G.;
RT   "Molecular characterization of an aberrant mercury resistance transposable
RT   element from an environmental Acinetobacter strain.";
RL   Plasmid 30:303-308(1993).
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}.
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DR   EMBL; AF213017; AAA19679.1; -; Genomic_DNA.
DR   RefSeq; WP_001294659.1; NZ_MOSW01000200.1.
DR   AlphaFoldDB; Q52106; -.
DR   GeneID; 66271199; -.
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_0000096427"
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;  12510 MW;  2930A92CF88EB10F CRC64;
     MSEPQNGRGA LFAGGLAAIL ASACCLGPLV LIALGFSGAW IGNLTVLEPY RPIFIGAALV
     ALFFAWRRIV RPTAACKPGE VCAIPQVRTT YKLIFWFVAV LVLVALGFPY VMPFFY