ID   MERP_SHEPU              Reviewed;          91 AA.
AC   Q54463;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Mercuric transport protein periplasmic component {ECO:0000250|UniProtKB:P04129};
DE   AltName: Full=Mercury scavenger protein {ECO:0000250|UniProtKB:P04129};
DE   AltName: Full=Periplasmic mercury ion-binding protein {ECO:0000250|UniProtKB:P04129};
DE   Flags: Precursor;
GN   Name=merP;
OS   Shewanella putrefaciens (Pseudomonas putrefaciens).
OG   Plasmid IncJ pMERPH.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=24;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9167257; DOI=10.1111/j.1574-6976.1997.tb00300.x;
RA   Osborn A.M., Bruce K.D., Strike P., Ritchie D.A.;
RT   "Distribution, diversity and evolution of the bacterial mercury resistance
RT   (mer) operon.";
RL   FEMS Microbiol. Rev. 19:239-262(1997).
CC   -!- FUNCTION: Involved in mercury resistance. Acts as a mercury scavenger
CC       that specifically binds to a mercuric ion in the periplasm and probably
CC       passes it to the cytoplasmic mercuric reductase MerA via the mercuric
CC       transport protein MerT. {ECO:0000250|UniProtKB:P04129}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P13113}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P13113}.
CC   -!- SIMILARITY: Belongs to the MerP family. {ECO:0000305}.
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DR   EMBL; Z49196; CAA89055.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q54463; -.
DR   SMR; Q54463; -.
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   Pfam; PF00403; HMA; 1.
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.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..91
FT                   /note="Mercuric transport protein periplasmic component"
FT                   /id="PRO_0000021678"
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;  9742 MW;  75CC80DC3FD45162 CRC64;
     MKTLALMSLF VLTSLNALAA PKTVTLEVPT MNCVTCPFTV EKALQKVDGV SKAEVTFKTK
     LAVVTFDDEK STVKALTEAT TNAGYPSTLK E