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 04-NOV-2026, entry version 116. 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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z00027; CAA77321.1; -; Genomic_DNA. DR EMBL; K02503; AAA27433.1; -; Genomic_DNA. DR PIR; A04457; QQPSHT. DR RefSeq; WP_003131974.1; NZ_AP014651.1. DR AlphaFoldDB; P04140; -. DR GeneID; 305711250; -. DR GeneID; 94693671; -. DR eggNOG; COG2608; Bacteria. DR OMA; ACEEGSY; -. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015097; F:mercury ion transmembrane transporter activity; IEA:InterPro. DR Gene3D; 1.10.287.910; bacterial mercury transporter, merf; 1. DR InterPro; IPR003457; Transprt_MerT. DR NCBIfam; NF010314; merT; 1. 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 //