MERT_SHIFL
ID MERT_SHIFL Reviewed; 116 AA.
AC P0A220; P04336;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Mercuric transport protein MerT {ECO:0000305};
DE AltName: Full=Mercury ion transport protein {ECO:0000305};
GN Name=merT;
OS Shigella flexneri.
OG Plasmid IncFII R100 (NR1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE FUNCTION.
RX PubMed=6091128; DOI=10.1073/pnas.81.19.5975;
RA Misra T.K., Brown N.L., Fritzinger D.C., Pridmore R.D., Barnes W.M.,
RA Haberstroh L., Silver S.;
RT "Mercuric ion-resistance operons of plasmid R100 and transposon Tn501: the
RT beginning of the operon including the regulatory region and the first two
RT structural genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5975-5979(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=Tn21;
RX PubMed=6530603;
RA Barrineau P., Gilbert P., Jackson W.J., Jones C.S., Summers A.O.,
RA Wisdom S.;
RT "The DNA sequence of the mercury resistance operon of the IncFII plasmid
RT NR1.";
RL J. Mol. Appl. Genet. 2:601-619(1984).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=1328156; DOI=10.1128/jb.174.20.6377-6385.1992;
RA Hamlett N.V., Landale E.C., Davis B.H., Summers A.O.;
RT "Roles of the Tn21 merT, merP, and merC gene products in mercury resistance
RT and mercury binding.";
RL J. Bacteriol. 174:6377-6385(1992).
CC -!- FUNCTION: Involved in mercury resistance (PubMed:6091128,
CC PubMed:1328156). Probably transfers a mercuric ion from the periplasmic
CC Hg(2+)-binding protein MerP to the cytoplasmic mercuric reductase MerA
CC (Probable). {ECO:0000269|PubMed:1328156, ECO:0000269|PubMed:6091128,
CC ECO:0000305|PubMed:6091128}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutation decreases resistance to mercury.
CC {ECO:0000269|PubMed:1328156}.
CC -!- SIMILARITY: Belongs to the MerT family. {ECO:0000305}.
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DR EMBL; J01730; AAA92261.1; -; Genomic_DNA.
DR EMBL; K03089; AAB59075.1; -; Genomic_DNA.
DR PIR; A04458; QQEBHT.
DR RefSeq; WP_001294663.1; NZ_WPET01000167.1.
DR AlphaFoldDB; P0A220; -.
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;
KW Transposable element.
FT CHAIN 1..116
FT /note="Mercuric transport protein MerT"
FT /id="PRO_0000096435"
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
