MERC_SHIFL
ID MERC_SHIFL Reviewed; 140 AA.
AC Q50919;
DT 20-DEC-2017, 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 MerC {ECO:0000305};
DE AltName: Full=Mercuric resistance protein MerC {ECO:0000305};
GN Name=merC {ECO:0000303|PubMed:1328156};
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].
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 [2]
RP PROTEIN SEQUENCE OF 2-6, FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, AND HG(2+)-BINDING.
RX PubMed=9368013; DOI=10.1074/jbc.272.47.29518;
RA Sahlman L., Wong W., Powlowski J.;
RT "A mercuric ion uptake role for the integral inner membrane protein, MerC,
RT involved in bacterial mercuric ion resistance.";
RL J. Biol. Chem. 272:29518-29526(1997).
RN [3]
RP 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 mercuric ion uptake and binding. MerC-mediated
CC Hg(2+) uptake does not require MerP. {ECO:0000269|PubMed:9368013}.
CC -!- ACTIVITY REGULATION: Uptake of Hg(2+) is decreased by iodoacetamide and
CC iodoacetate, and is completely inhibited by the thiol-modifying reagent
CC N-ethylmaleimide (NEM). {ECO:0000269|PubMed:9368013}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:9368013};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutation does not affect resistance to mercury.
CC {ECO:0000269|PubMed:1328156}.
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DR EMBL; K03089; AAB59077.1; -; Genomic_DNA.
DR RefSeq; WP_001340589.1; NZ_WPET01000167.1.
DR AlphaFoldDB; Q50919; -.
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; IPR004891; Mercury-R_MerC.
DR Pfam; PF03203; MerC; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing; Membrane;
KW Mercuric resistance; Mercury; Metal-binding; Plasmid; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9368013"
FT CHAIN 2..140
FT /note="Mercuric transport protein MerC"
FT /id="PRO_0000442699"
FT TOPO_DOM 2..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9368013"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..46
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9368013"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9368013"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..106
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9368013"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9368013"
FT BINDING 22
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000305|PubMed:9368013"
FT BINDING 25
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000305|PubMed:9368013"
SQ SEQUENCE 140 AA; 14964 MW; E2A7E3EC78D9C24A CRC64;
MGLMTRIADK TGALGSVVSA MGCAACFPAL ASFGAAIGLG FLSQYEGLFI SRLLPLFAAL
AFLANALGWF SHRQWLRSLL GMIGPAIVFA ATVWLLGNWW TANLMYVGLA LMIGVSIWDF
VSPAHRRCGP DGCELPAKRL
