MERC_ACIFR
ID MERC_ACIFR Reviewed; 144 AA.
AC P22905;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Mercuric transport protein MerC {ECO:0000305};
DE AltName: Full=Mercuric resistance protein MerC {ECO:0000305};
GN Name=merC {ECO:0000303|PubMed:2265748};
OS Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=920;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=E-15;
RX PubMed=2265748; DOI=10.1016/0378-1119(90)90349-v;
RA Inoue C., Sugawara K., Kusano T.;
RT "Thiobacillus ferrooxidans mer operon: sequence analysis of the promoter
RT and adjacent genes.";
RL Gene 96:115-120(1990).
RN [2]
RP SEQUENCE REVISION TO 130.
RA Inoue C., Sugawara K., Kusano T.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP INDUCTION.
RX PubMed=2185229; DOI=10.1128/jb.172.5.2688-2692.1990;
RA Kusano T., Ji G.Y., Inoue C., Silver S.;
RT "Constitutive synthesis of a transport function encoded by the Thiobacillus
RT ferrooxidans merC gene cloned in Escherichia coli.";
RL J. Bacteriol. 172:2688-2692(1990).
RN [4]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF
RP CYS-23; CYS-26; HIS-72; HIS-97; HIS-98; CYS-132 AND CYS-137.
RX PubMed=16041147; DOI=10.1271/bbb.69.1394;
RA Sasaki Y., Minakawa T., Miyazaki A., Silver S., Kusano T.;
RT "Functional dissection of a mercuric ion transporter, MerC, from
RT Acidithiobacillus ferrooxidans.";
RL Biosci. Biotechnol. Biochem. 69:1394-1402(2005).
CC -!- FUNCTION: Involved in mercuric ion uptake.
CC {ECO:0000269|PubMed:16041147, ECO:0000269|PubMed:2185229}.
CC -!- ACTIVITY REGULATION: Inhibited by the thiol-modifying reagent N-
CC ethylmaleimide (NEM). {ECO:0000269|PubMed:2185229}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for Hg(2+) {ECO:0000269|PubMed:2185229};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16041147}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:16041147}; Multi-pass membrane protein
CC {ECO:0000255, ECO:0000269|PubMed:16041147}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:2185229}.
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DR EMBL; D90110; BAA14138.2; -; Genomic_DNA.
DR PIR; JS0479; JS0479.
DR RefSeq; WP_009567170.1; NZ_QKQP01000005.1.
DR AlphaFoldDB; P22905; -.
DR STRING; 380394.Lferr_2106; -.
DR TCDB; 1.A.72.4.2; the mercuric ion pore (mer) superfamily.
DR GeneID; 66433446; -.
DR OMA; CASCFPA; -.
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; Membrane; Mercuric resistance; Mercury;
KW Metal-binding; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..144
FT /note="Mercuric transport protein MerC"
FT /id="PRO_0000096425"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16041147"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..46
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:16041147"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16041147"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..103
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:16041147"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16041147"
FT BINDING 23
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000305|PubMed:16041147"
FT BINDING 26
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000305|PubMed:16041147"
FT MUTAGEN 23
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16041147"
FT MUTAGEN 26
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16041147"
FT MUTAGEN 72
FT /note="H->E: Slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:16041147"
FT MUTAGEN 97
FT /note="H->E: No change in activity."
FT /evidence="ECO:0000269|PubMed:16041147"
FT MUTAGEN 98
FT /note="H->E: No change in activity."
FT /evidence="ECO:0000269|PubMed:16041147"
FT MUTAGEN 132
FT /note="C->S: No change in activity."
FT /evidence="ECO:0000269|PubMed:16041147"
FT MUTAGEN 137
FT /note="C->S: Slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:16041147"
SQ SEQUENCE 144 AA; 15526 MW; CD6829E430FFB898 CRC64;
MSAITRIIDK IGIVGTIVGS FSCAMCFPAA ASLGAAIGLG FLSQWEGLFV QWLIPIFASV
ALLATLAGWF SHRQWQRTLL GSIGPVLALV GVFGLTHHFL DKDLARVIFY TGLVVMFLVS
IWDMVNPANR RCATDGCETP APRS
