MERP_SALTI
ID MERP_SALTI Reviewed; 91 AA.
AC P0A216; O08125; P94701;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
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; OrderedLocusNames=HCM1.153;
OS Salmonella typhi.
OG Plasmid pHCM1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
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; AL513383; CAD09748.1; -; Genomic_DNA.
DR RefSeq; NP_569362.1; NC_003384.1.
DR AlphaFoldDB; P0A216; -.
DR SMR; P0A216; -.
DR KEGG; sty:HCM1.153; -.
DR PATRIC; fig|220341.7.peg.5190; -.
DR HOGENOM; CLU_134973_2_1_6; -.
DR OMA; NHCKMTV; -.
DR Proteomes; UP000000541; Plasmid pHCM1.
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_0000021676"
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
