ID   MERP_SERMA              Reviewed;          91 AA.
AC   P13113;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 107.
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:2666393};
OS   Serratia marcescens.
OG   Plasmid pDU1358.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2666393; DOI=10.1128/jb.171.8.4241-4247.1989;
RA   Nucifora G., Chu L., Silver S., Misra T.K.;
RT   "Mercury operon regulation by the merR gene of the organomercurial
RT   resistance system of plasmid pDU1358.";
RL   J. Bacteriol. 171:4241-4247(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 20-24, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   HG(2+)-BINDING.
RX   PubMed=1555597; DOI=10.1111/j.1432-1033.1992.tb16790.x;
RA   Sahlman L., Jonsson B.H.;
RT   "Purification and properties of the mercuric-ion-binding protein MerP.";
RL   Eur. J. Biochem. 205:375-381(1992).
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:0000305|PubMed:1555597}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1555597}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:1555597}.
CC   -!- SIMILARITY: Belongs to the MerP family. {ECO:0000305}.
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DR   EMBL; M24940; AAA98223.1; -; Genomic_DNA.
DR   PIR; C33858; C33858.
DR   RefSeq; WP_000732290.1; NZ_SWIB01000042.1.
DR   AlphaFoldDB; P13113; -.
DR   SMR; P13113; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Mercuric resistance; Mercury; Metal-binding;
KW   Periplasm; Plasmid; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:1555597"
FT   CHAIN           20..91
FT                   /note="Mercuric transport protein periplasmic component"
FT                   /id="PRO_0000021677"
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;  9548 MW;  21EB0D79E9795069 CRC64;
     MKKLFASLAI AAVVAPVWAA TQTVTLSVPG MTCSACPITV KKAISKVEGV SKVNVTFETR
     EAVVTFDDAK TSVQKLTKAT EDAGYPSSVK K