MERP_SHIFL
ID MERP_SHIFL Reviewed; 91 AA.
AC P04129; P07042;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1986, sequence version 1.
DT 03-AUG-2022, entry version 126.
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:1328156};
OS Shigella flexneri.
OG Plasmid IncFII R100 (NR1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE FUNCTION.
RX PubMed=6091128; DOI=10.1073/pnas.81.19.5975;
RA Misra T.K., Brown N.L., Fritzinger D.C., Pridmore R.D., Barnes W.M.,
RA Haberstroh L., Silver S.;
RT "Mercuric ion-resistance operons of plasmid R100 and transposon Tn501: the
RT beginning of the operon including the regulatory region and the first two
RT structural genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5975-5979(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=Tn21;
RX PubMed=6530603;
RA Barrineau P., Gilbert P., Jackson W.J., Jones C.S., Summers A.O.,
RA Wisdom S.;
RT "The DNA sequence of the mercury resistance operon of the IncFII plasmid
RT NR1.";
RL J. Mol. Appl. Genet. 2:601-619(1984).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=1328156; DOI=10.1128/jb.174.20.6377-6385.1992;
RA Hamlett N.V., Landale E.C., Davis B.H., Summers A.O.;
RT "Roles of the Tn21 merT, merP, and merC gene products in mercury resistance
RT and mercury binding.";
RL J. Bacteriol. 174:6377-6385(1992).
RN [4]
RP FUNCTION.
RX PubMed=9368013; DOI=10.1074/jbc.272.47.29518;
RA Sahlman L., Wong W., Powlowski J.;
RT "A mercuric ion uptake role for the integral inner membrane protein, MerC,
RT involved in bacterial mercuric ion resistance.";
RL J. Biol. Chem. 272:29518-29526(1997).
RN [5] {ECO:0007744|PDB:1AFI, ECO:0007744|PDB:1AFJ}
RP STRUCTURE BY NMR OF 20-91, AND HG(2+)-BINDING.
RX PubMed=9188683; DOI=10.1021/bi9631632;
RA Steele R.A., Opella S.J.;
RT "Structures of the reduced and mercury-bound forms of MerP, the periplasmic
RT protein from the bacterial mercury detoxification system.";
RL Biochemistry 36:6885-6895(1997).
RN [6] {ECO:0007744|PDB:2HQI}
RP STRUCTURE BY NMR OF 20-91, AND FUNCTION.
RX PubMed=9649312; DOI=10.1021/bi9803628;
RA Qian H., Sahlman L., Eriksson P.O., Hambraeus C., Edlund U., Sethson I.;
RT "NMR solution structure of the oxidized form of MerP, a mercuric ion
RT binding protein involved in bacterial mercuric ion resistance.";
RL Biochemistry 37:9316-9322(1998).
CC -!- FUNCTION: Involved in mercury resistance (PubMed:1328156). Acts as a
CC mercury scavenger that specifically binds to a mercuric ion in the
CC periplasm and probably passes it to the cytoplasmic mercuric reductase
CC MerA via the mercuric transport protein MerT (PubMed:9368013,
CC PubMed:9649312). {ECO:0000269|PubMed:1328156,
CC ECO:0000269|PubMed:9368013, ECO:0000269|PubMed:9649312,
CC ECO:0000305|PubMed:6091128}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P13113}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mutation decreases resistance to mercury.
CC {ECO:0000269|PubMed:1328156}.
CC -!- SIMILARITY: Belongs to the MerP family. {ECO:0000305}.
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DR EMBL; J01730; AAA92262.1; -; Genomic_DNA.
DR EMBL; K03089; AAB59076.1; -; Genomic_DNA.
DR PIR; A03556; RGEBHD.
DR PIR; S09524; S09524.
DR RefSeq; WP_000732292.1; NZ_WPET01000167.1.
DR PDB; 1AFI; NMR; -; A=20-91.
DR PDB; 1AFJ; NMR; -; A=20-91.
DR PDB; 1DVW; NMR; -; A=25-42.
DR PDB; 2HQI; NMR; -; A=20-91.
DR PDBsum; 1AFI; -.
DR PDBsum; 1AFJ; -.
DR PDBsum; 1DVW; -.
DR PDBsum; 2HQI; -.
DR AlphaFoldDB; P04129; -.
DR SMR; P04129; -.
DR EvolutionaryTrace; P04129; -.
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 3D-structure; Mercuric resistance; Mercury; Metal-binding; Periplasm;
KW Plasmid; Signal; Transposable element.
FT SIGNAL 1..19
FT CHAIN 20..91
FT /note="Mercuric transport protein periplasmic component"
FT /id="PRO_0000021679"
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 ECO:0000269|PubMed:9188683"
FT BINDING 36
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:9188683"
FT CONFLICT 51
FT /note="S -> T (in Ref. 2; AAB59076)"
FT /evidence="ECO:0000305"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:1AFI"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:2HQI"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1AFI"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:1AFI"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:1AFI"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:1AFI"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:1AFI"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1AFI"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:1AFI"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2HQI"
SQ SEQUENCE 91 AA; 9414 MW; 822183AC323031A5 CRC64;
MKKLFASLAL AAAVAPVWAA TQTVTLAVPG MTCAACPITV KKALSKVEGV SKVDVGFEKR
EAVVTFDDTK ASVQKLTKAT ADAGYPSSVK Q
