ID   MERP_ACICA              Reviewed;          91 AA.
AC   Q52107;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
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 {ECO:0000303|PubMed:8302940};
OS   Acinetobacter calcoaceticus.
OG   Plasmid pKLH2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8302940; DOI=10.1006/plas.1993.1064;
RA   Kholodii G.Y., Lomovskaya O.L., Gorlenko Z.M., Mindlin S.Z., Yurieva O.V.,
RA   Nikiforov V.G.;
RT   "Molecular characterization of an aberrant mercury resistance transposable
RT   element from an environmental Acinetobacter strain.";
RL   Plasmid 30:303-308(1993).
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; AF213017; AAA19680.1; -; Genomic_DNA.
DR   RefSeq; WP_004178136.1; NZ_MOSW01000200.1.
DR   AlphaFoldDB; Q52107; -.
DR   SMR; Q52107; -.
DR   GeneID; 66271198; -.
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.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..91
FT                   /note="Mercuric transport protein periplasmic component"
FT                   /id="PRO_0000021670"
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;  9636 MW;  84321669C5305F6E CRC64;
     MKKLFASLAL AAFVAPVFAA TQTVTLSVPG MTCASCPITV KHALSKVEGV SKTDVSFDKR
     QAVVTFDDAK TNVQKLTKAT EDAGYPSSLK R