MERT_PSEAI
ID MERT_PSEAI Reviewed; 116 AA.
AC P04140;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1986, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Mercuric transport protein MerT {ECO:0000305};
DE AltName: Full=Mercury ion transport protein {ECO:0000303|PubMed:8569683};
GN Name=merT;
OS Pseudomonas aeruginosa.
OG Plasmid pVS1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE FUNCTION.
RC TRANSPOSON=Tn501;
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=3038684; DOI=10.1016/0378-1119(87)90047-3;
RA Lund P.A., Brown N.L.;
RT "Role of the merT and merP gene products of transposon Tn501 in the
RT induction and expression of resistance to mercuric ions.";
RL Gene 52:207-214(1987).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF GLY-14; GLY-15; ALA-18; CYS-24; CYS-25 AND
RP GLY-27.
RX PubMed=8569683; DOI=10.1007/bf02191833;
RA Hobman J.L., Brown N.L.;
RT "Overexpression of MerT, the mercuric ion transport protein of transposon
RT Tn501, and genetic selection of mercury hypersensitivity mutations.";
RL Mol. Gen. Genet. 250:129-134(1996).
RN [4]
RP FUNCTION, INTERACTION WITH MERA, AND MUTAGENESIS OF CYS-76 AND CYS-82.
RX PubMed=17457514; DOI=10.1007/s10534-007-9097-4;
RA Schue M., Glendinning K.J., Hobman J.L., Brown N.L.;
RT "Evidence for direct interactions between the mercuric ion transporter
RT (MerT) and mercuric reductase (MerA) from the Tn501 mer operon.";
RL BioMetals 21:107-116(2008).
CC -!- FUNCTION: Involved in mercury resistance (PubMed:3038684,
CC PubMed:8569683). 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:3038684, ECO:0000269|PubMed:8569683,
CC ECO:0000305|PubMed:17457514, ECO:0000305|PubMed:6091128}.
CC -!- SUBUNIT: Interacts with MerA. {ECO:0000269|PubMed:17457514}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Merp-merT deletion mutant is unable to transport
CC mercury into the cytoplasm and shows almost complete loss of the
CC resistance phenotype. {ECO:0000269|PubMed:3038684}.
CC -!- SIMILARITY: Belongs to the MerT family. {ECO:0000305}.
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DR EMBL; Z00027; CAA77321.1; -; Genomic_DNA.
DR EMBL; K02503; AAA27433.1; -; Genomic_DNA.
DR PIR; A04457; QQPSHT.
DR RefSeq; WP_003131974.1; NZ_WXZW01000069.1.
DR AlphaFoldDB; P04140; -.
DR GeneID; 34794310; -.
DR eggNOG; COG2608; Bacteria.
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 1: Evidence at protein level;
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_0000096430"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
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:0000305"
FT BINDING 25
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000305"
FT BINDING 76
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000305"
FT BINDING 82
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000305"
FT MUTAGEN 14
FT /note="G->R: Abolishes mercury resistance."
FT /evidence="ECO:0000269|PubMed:8569683"
FT MUTAGEN 15
FT /note="G->R: Abolishes mercury resistance."
FT /evidence="ECO:0000269|PubMed:8569683"
FT MUTAGEN 18
FT /note="A->D: Abolishes mercury resistance."
FT /evidence="ECO:0000269|PubMed:8569683"
FT MUTAGEN 24
FT /note="C->R: Abolishes mercury resistance."
FT /evidence="ECO:0000269|PubMed:8569683"
FT MUTAGEN 25
FT /note="C->Y: Abolishes mercury resistance."
FT /evidence="ECO:0000269|PubMed:8569683"
FT MUTAGEN 27
FT /note="G->R: Abolishes mercury resistance."
FT /evidence="ECO:0000269|PubMed:8569683"
FT MUTAGEN 76
FT /note="C->S: Decreases mercury transport."
FT /evidence="ECO:0000269|PubMed:17457514"
FT MUTAGEN 82
FT /note="C->S: Decreases mercury transport."
FT /evidence="ECO:0000269|PubMed:17457514"
SQ SEQUENCE 116 AA; 12498 MW; 905B5492AFE08E6C CRC64;
MSEPKTGRGA LFTGGLAAIL ASACCLGPLV LIALGFSGAW IGNLAVLEPY RPIFIGVALV
ALFFAWRRIY RQAAACKPGE VCAIPQVRAT YKLIFWIVAA LVLVALGFPY VMPFFY
