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-1994 (REL. 30, LAST ANNOTATION UPDATE) DE MERCURIC TRANSPORT PROTEIN PERIPLASMIC COMPONENT PRECURSOR. GN MERP. OS SHIGELLA FLEXNERI. OG PLASMID NR1 (R100). OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 85014891. RA MISRA T.K., BROWN N.L., FRITZINGER D.C., PRIDMORE R.D., BARNES W.M., RA HABERSTROH L., SILVER S.; 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. RA BARRINEAU P., GILBERT P., JACKSON W.J., JONES C.S., SUMMERS A.O., RA WISDOM S.; RL J. MOL. APPL. GENET. 2:601-619(1984). 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 A COPY OF THE HEAVY-METAL-ASSOCIATED (HMA) CC 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; G151751; -. DR EMBL; K03089; G150394; -. DR PIR; A03556; RGEBHD. DR PROSITE; PS01047; HMA. KW TRANSPORT; MERCURIC RESISTANCE; PERIPLASMIC; METAL-BINDING; SIGNAL; KW TRANSPOSABLE ELEMENT; PLASMID. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 91 MERCURIC TRANSPORT PERIPLASMIC 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; 70C4CF5F CRC32; MKKLFASLAL AAAVAPVWAA TQTVTLAVPG MTCAACPITV KKALSKVEGV SKVDVGFEKR EAVVTFDDTK ASVQKLTKAT ADAGYPSSVK Q //