MERP_ENTAG
ID MERP_ENTAG Reviewed; 91 AA.
AC P0A217; O08125; P94701;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 62.
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 Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OG Plasmid pKLH272.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX NCBI_TaxID=549;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KH72;
RX PubMed=9159519; DOI=10.1046/j.1365-2958.1997.3261688.x;
RA Yurieva O., Kholodii G., Minakhin L., Gorlenko Z., Kalyaeva E., Mindlin S.,
RA Nikiforov V.;
RT "Intercontinental spread of promiscuous mercury-resistance transposons in
RT environmental bacteria.";
RL Mol. Microbiol. 24:321-329(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; Y08992; CAA70182.1; -; Genomic_DNA.
DR AlphaFoldDB; P0A217; -.
DR SMR; P0A217; -.
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_0000021672"
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; 9611 MW; E1298ECBCE2FBFD4 CRC64;
MKKLFAALAL AAVVAPVWAA TQTVTLSVPG MTCASCPITV KHALSKVEGV SKTDVSFDKR
QAVVTFDDAK TNVQKLTKAT EDAGYPSSLK R