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 16-OCT-2001 (Rel. 40, Last annotation update) DE Mercuric transport protein periplasmic component precursor DE (Periplasmic mercury ion binding protein) (Mercury scavenger protein). GN MERP. OS Shigella flexneri. OG Plasmid IncFII NR1. OC Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC 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 RT Tn501: the beginning of the operon including the regulatory region RT and the 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; 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; 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 HG(2+) 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 HEAVY-METAL-ASSOCIATED (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; 23-JUL-97. DR PDB; 1AFJ; 23-JUL-97. DR PDB; 2HQI; 11-NOV-98. DR InterPro; IPR001802; HG_scavenger. DR InterPro; IPR001934; HMA. DR Pfam; PF00403; HMA; 1. DR PRINTS; PR00946; HGSCAVENGER. DR PROSITE; PS01047; HMA; 1. KW Transport; Mercuric resistance; Periplasmic; Metal-binding; Signal; KW Transposable element; Plasmid; 3D-structure. FT SIGNAL 1 19 FT CHAIN 20 91 MERCURIC TRANSPORT PROTEIN PERIPLASMIC FT COMPONENT. FT DOMAIN 28 57 HMA. FT METAL 33 33 HG(2+) (POTENTIAL). FT METAL 36 36 HG(2+) (POTENTIAL). FT CONFLICT 51 51 S -> T (IN REF. 2). SQ SEQUENCE 91 AA; 9414 MW; 822183AC323031A5 CRC64; MKKLFASLAL AAAVAPVWAA TQTVTLAVPG MTCAACPITV KKALSKVEGV SKVDVGFEKR EAVVTFDDTK ASVQKLTKAT ADAGYPSSVK Q //