ID MERP_SHIFL STANDARD; PRT; 91 AA. AC P04129; P07042; DT 01-NOV-1986 (Rel. 03, Created) DT 01-NOV-1986 (Rel. 03, Last sequence update) DT 01-OCT-2004 (Rel. 45, Last annotation update) DE Mercuric transport protein periplasmic component precursor DE (Periplasmic mercury ion binding protein) (Mercury scavenger protein). GN Name=merP; OS Shigella flexneri. OG Plasmid IncFII NR1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85014891; PubMed=6091128; 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: RT the beginning of the operon including the regulatory region and the RT first two structural genes."; RL Proc. Natl. Acad. Sci. U.S.A. 81:5975-5979(1984). RN [2] RP SEQUENCE FROM N.A. RC TRANSPOSON=Tn21; RX MEDLINE=85159407; 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 RT plasmid NR1."; RL J. Mol. Appl. Genet. 2:601-619(1984). RN [3] RP STRUCTURE BY NMR. RX MEDLINE=97332449; 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 RT periplasmic protein from the bacterial mercury detoxification RT system."; RL Biochemistry 36:6885-6895(1997). RN [4] RP STRUCTURE BY NMR. RX MEDLINE=98313266; PubMed=9649312; DOI=10.1021/bi9803628; RA Qian H., Sahlman L., Eriksson P.O., Hambraeus C., Edlund U., RA 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: Mercury scavenger that specifically binds to one mercury CC ion and which passes it to the mercuric reductase (merA) via the CC merT protein. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Periplasmic (Probable). CC -!- SIMILARITY: Contains 1 HMA domain. 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; -. DR EMBL; K03089; AAB59076.1; -. DR PIR; A03556; RGEBHD. DR PDB; 1AFI; NMR; @=-. DR PDB; 1AFJ; NMR; @=-. DR PDB; 1DVW; NMR; A=25-42. DR PDB; 2HQI; NMR; @=20-91. DR InterPro; IPR000428; Cu_bind. DR InterPro; IPR006121; HeavyMe_transpt. DR InterPro; IPR001802; HG_scavenger. DR InterPro; IPR006191; Metal_bind. DR Pfam; PF00403; HMA; 1. DR PRINTS; PR00944; CUEXPORT. DR PRINTS; PR00946; HGSCAVENGER. DR PROSITE; PS01047; HMA_1; 1. DR PROSITE; PS50846; HMA_2; 1. KW 3D-structure; Mercuric resistance; Metal-binding; Periplasmic; KW Plasmid; Signal; Transport; Transposable element. FT SIGNAL 1 19 FT CHAIN 20 91 Mercuric transport protein periplasmic FT component. FT DOMAIN 23 89 HMA. FT METAL 33 33 Mercury (Potential). FT METAL 36 36 Mercury (Potential). FT CONFLICT 51 51 S -> T (in Ref. 2). FT STRAND 22 27 FT TURN 29 30 FT TURN 34 36 FT HELIX 37 47 FT STRAND 50 56 FT TURN 57 60 FT STRAND 61 66 FT TURN 68 70 FT HELIX 73 83 FT TURN 84 84 FT STRAND 88 89 SQ SEQUENCE 91 AA; 9414 MW; 822183AC323031A5 CRC64; MKKLFASLAL AAAVAPVWAA TQTVTLAVPG MTCAACPITV KKALSKVEGV SKVDVGFEKR EAVVTFDDTK ASVQKLTKAT ADAGYPSSVK Q //