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 17-JUN-2020, entry version 119. 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:0000244|PDB:1AFI, ECO:0000244|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:0000244|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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; P04129; -. DR GeneID; 4999095; -. 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 23..89 FT /note="HMA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280" FT METAL 33 FT /note="Mercury" FT /evidence="ECO:0000269|PubMed:9188683" FT METAL 36 FT /note="Mercury" FT /evidence="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:0000244|PDB:1AFI" FT TURN 29..32 FT /evidence="ECO:0000244|PDB:2HQI" FT STRAND 33..35 FT /evidence="ECO:0000244|PDB:1AFI" FT HELIX 36..45 FT /evidence="ECO:0000244|PDB:1AFI" FT STRAND 48..56 FT /evidence="ECO:0000244|PDB:1AFI" FT TURN 57..60 FT /evidence="ECO:0000244|PDB:1AFI" FT STRAND 61..66 FT /evidence="ECO:0000244|PDB:1AFI" FT TURN 68..70 FT /evidence="ECO:0000244|PDB:1AFI" FT HELIX 73..83 FT /evidence="ECO:0000244|PDB:1AFI" FT STRAND 88..90 FT /evidence="ECO:0000244|PDB:2HQI" SQ SEQUENCE 91 AA; 9414 MW; 822183AC323031A5 CRC64; MKKLFASLAL AAAVAPVWAA TQTVTLAVPG MTCAACPITV KKALSKVEGV SKVDVGFEKR EAVVTFDDTK ASVQKLTKAT ADAGYPSSVK Q //