ID   MERP_PSEAI              Reviewed;          91 AA.
AC   P04131;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1986, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Mercuric transport protein periplasmic component {ECO:0000305};
DE   AltName: Full=Mercury scavenger protein {ECO:0000305};
DE   AltName: Full=Periplasmic mercury ion-binding protein {ECO:0000305};
DE   Flags: Precursor;
GN   Name=merP {ECO:0000303|PubMed:3038684};
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).
CC   -!- FUNCTION: Involved in mercury resistance (PubMed:3038684). Acts as a
CC       mercury scavenger that specifically binds to a mercuric ion in the
CC       periplasm and probably passes it to the cytoplasmic mercuric reductase
CC       MerA via the mercuric transport protein MerT (Probable).
CC       {ECO:0000269|PubMed:3038684, ECO:0000305|PubMed:6091128}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P13113}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P13113}.
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 MerP family. {ECO:0000305}.
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DR   EMBL; Z00027; CAA77322.1; -; Genomic_DNA.
DR   EMBL; K02503; AAA27434.1; -; Genomic_DNA.
DR   PIR; A03557; RGPSHA.
DR   AlphaFoldDB; P04131; -.
DR   SMR; P04131; -.
DR   eggNOG; COG2608; Bacteria.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0045340; F:mercury ion binding; IEA:InterPro.
DR   GO; GO:0015097; F:mercury ion transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd00371; HMA; 1.
DR   InterPro; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR011795; MerP.
DR   InterPro; IPR001802; MerP/CopZ.
DR   Pfam; PF00403; HMA; 1.
DR   PRINTS; PR00946; HGSCAVENGER.
DR   SUPFAM; SSF55008; SSF55008; 1.
DR   TIGRFAMs; TIGR02052; MerP; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
KW   Mercuric resistance; Mercury; Metal-binding; Periplasm; Plasmid; Signal;
KW   Transposable element.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..91
FT                   /note="Mercuric transport protein periplasmic component"
FT                   /id="PRO_0000021674"
FT   DOMAIN          22..88
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         33
FT                   /ligand="Hg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:16793"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         36
FT                   /ligand="Hg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:16793"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
SQ   SEQUENCE   91 AA;  9491 MW;  6D6DB86B5FCA20CE CRC64;
     MKKLFASLAL AAVVAPVWAA TQTVTLSVPG MTCSACPITV KKAISEVEGV SKVDVTFETR
     QAVVTFDDAK TSVQKLTKAT ADAGYPSSVK Q