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UniProtKB/Swiss-Prot entry P04129


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MERP_SHIFL
Primary accession number P04129
Secondary accession number P07042
Integrated into Swiss-Prot on November 1, 1986
Sequence was last modified on November 1, 1986 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 70)
Name and origin of the protein
Protein name Mercuric transport protein periplasmic component [Precursor]
Synonyms Periplasmic mercury ion-binding protein
Mercury scavenger protein
Gene name
Name: merP
From
Shigella flexneri [TaxID: 623] 
Encoded on Plasmid IncFII R100 (NR1).
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Shigella.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6091128 [NCBI, ExPASy, EBI, Israel, Japan]
Misra T.K., Brown N.L., Fritzinger D.C., Pridmore R.D., Barnes W.M., Haberstroh L., Silver S.;
"Mercuric ion-resistance operons of plasmid R100 and transposon Tn501: the beginning of the operon including the regulatory region and the first two structural genes.";
Proc. Natl. Acad. Sci. U.S.A. 81:5975-5979(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TRANSPOSON=Tn21;
PubMed=6530603 [NCBI, ExPASy, EBI, Israel, Japan]
Barrineau P., Gilbert P., Jackson W.J., Jones C.S., Summers A.O., Wisdom S.;
"The DNA sequence of the mercury resistance operon of the IncFII plasmid NR1.";
J. Mol. Appl. Genet. 2:601-619(1984).
[3]
STRUCTURE BY NMR.
DOI=10.1021/bi9631632; PubMed=9188683 [NCBI, ExPASy, EBI, Israel, Japan]
Steele R.A., Opella S.J.;
"Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system.";
Biochemistry 36:6885-6895(1997).
[4]
STRUCTURE BY NMR.
DOI=10.1021/bi9803628; PubMed=9649312 [NCBI, ExPASy, EBI, Israel, Japan]
Qian H., Sahlman L., Eriksson P.O., Hambraeus C., Edlund U., Sethson I.;
"NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein involved in bacterial mercuric ion resistance.";
Biochemistry 37:9316-9322(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J01730; AAA92262.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K03089; AAB59076.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A03556; RGEBHD.
S09524; S09524.
3D structure databases
PDB
1AFI; NMR; -; A=20-91.[ExPASy / RCSB / EBI]
1AFJ; NMR; -; A=20-91.[ExPASy / RCSB / EBI]
1DVW; NMR; -; A=25-42.[ExPASy / RCSB / EBI]
2HQI; NMR; -; A=20-91.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AFI; -.
1AFJ; -.
1DVW; -.
2HQI; -.
ModBase P04129.
Ontologies
GO
GO:0032196; Biological process: transposition (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001757; ATPase_P.
IPR000428; Cu_bd.
IPR006121; HeavyMe_transpt.
IPR001802; HG_scavenger.
IPR011795; MerP.
Graphical view of domain structure.
PANTHER PTHR11939; ATPase_P; 1.
Pfam PF00403; HMA; 1.
Pfam graphical view of domain structure.
PRINTS PR00944; CUEXPORT.
PR00946; HGSCAVENGER.
TIGRFAMs TIGR02052; MerP; 1.
PROSITE PS01047; HMA_1; 1.
PS50846; HMA_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P04129.
ProtoNet P04129.
Other
LinkHub P04129; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Mercuric resistance; Mercury; Metal-binding; Periplasm; Plasmid; Signal; Transport; Transposable element.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
SIGNAL   1   19  19      
CHAIN   20   91  72     Mercuric transport protein periplasmic component. PRO_0000021679
DOMAIN   23   89  67     HMA. 
METAL   33   33        Mercury (Potential). 
METAL   36   36        Mercury (Potential). 
CONFLICT   51   51        S -> T (in Ref. 2; AAB59076). 
STRAND   22   27  6      
STRAND   33   36  4      
TURN   37   39  3      
STRAND   52   56  5      
TURN   57   60  4      
STRAND   61   66  6      
HELIX   73   81  9      
STRAND   88   90  3      
Sequence information
Length: 91 AA [This is the length of the unprocessed precursor] Molecular weight: 9414 Da [This is the MW of the unprocessed precursor] CRC64: 822183AC323031A5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKKLFASLAL AAAVAPVWAA TQTVTLAVPG MTCAACPITV KKALSKVEGV SKVDVGFEKR 

        70         80         90 
EAVVTFDDTK ASVQKLTKAT ADAGYPSSVK Q 

P04129 in FASTA format

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