MERT_STRLI
ID MERT_STRLI Reviewed; 100 AA.
AC P30345;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Mercuric transport protein;
DE AltName: Full=Mercury ion transport protein;
GN Name=merT;
OS Streptomyces lividans.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1916;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=66 / 1326;
RX PubMed=1494353; DOI=10.1007/bf00279645;
RA Sedlmeier R., Altenbuchner J.;
RT "Cloning and DNA sequence analysis of the mercury resistance genes of
RT Streptomyces lividans.";
RL Mol. Gen. Genet. 236:76-85(1992).
CC -!- FUNCTION: Involved in mercuric transport. Passes a mercury ion from the
CC MerP protein to the mercuric reductase MerA.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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DR EMBL; X65467; CAA46463.1; -; Genomic_DNA.
DR PIR; S30171; S30171.
DR AlphaFoldDB; P30345; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046689; P:response to mercury ion; IEA:UniProtKB-KW.
PE 4: Predicted;
KW Cell membrane; Membrane; Mercuric resistance; Mercury; Metal-binding;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..100
FT /note="Mercuric transport protein"
FT /id="PRO_0000096437"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 31
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000255"
FT BINDING 32
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000255"
FT BINDING 82
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000255"
FT BINDING 83
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000255"
SQ SEQUENCE 100 AA; 10353 MW; 55C540DA4CC215E4 CRC64;
MTPPPTQPGD RRGGLLGTLA VVGVALLPII CCAGPVLLAS GALAGLGGVL VSPWLLAPAA
VLLAGALTWW LRRRRTGNGD ACCLPAPRTD QHDRDLLRKQ