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P04129 (MERP_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Mercuric transport protein periplasmic component
Alternative name(s):
Mercury scavenger protein
Periplasmic mercury ion-binding protein
Gene names
Name:merP
Encoded onPlasmid IncFII R100 (NR1)
OrganismShigella flexneri
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length91 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mercury scavenger that specifically binds to one mercury ion and which passes it to the mercuric reductase (merA) via the merT protein.

Subunit structure

Monomer.

Subcellular location

Periplasm Probable.

Sequence similarities

Contains 1 HMA domain.

Ontologies

Keywords
   Biological processMercuric resistance
Transport
   Cellular componentPeriplasm
   DomainSignal
   LigandMercury
Metal-binding
   Technical term3D-structure
Plasmid
Transposable element
Gene Ontology (GO)
   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmercury ion binding

Inferred from electronic annotation. Source: InterPro

mercury ion transmembrane transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Chain20 – 9172Mercuric transport protein periplasmic component
PRO_0000021679

Regions

Domain23 – 8967HMA

Sites

Metal binding331Mercury Potential
Metal binding361Mercury Potential

Experimental info

Sequence conflict511S → T in AAB59076. Ref.2

Secondary structure

.............. 91
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04129 [UniParc].

Last modified November 1, 1986. Version 1.
Checksum: 822183AC323031A5

FASTA919,414
        10         20         30         40         50         60 
MKKLFASLAL AAAVAPVWAA TQTVTLAVPG MTCAACPITV KKALSKVEGV SKVDVGFEKR 

        70         80         90 
EAVVTFDDTK ASVQKLTKAT ADAGYPSSVK Q 

« Hide

References

[1]"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."
Misra T.K., Brown N.L., Fritzinger D.C., Pridmore R.D., Barnes W.M., Haberstroh L., Silver S.
Proc. Natl. Acad. Sci. U.S.A. 81:5975-5979(1984) [PubMed: 6091128] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The DNA sequence of the mercury resistance operon of the IncFII plasmid NR1."
Barrineau P., Gilbert P., Jackson W.J., Jones C.S., Summers A.O., Wisdom S.
J. Mol. Appl. Genet. 2:601-619(1984) [PubMed: 6530603] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Transposon: Tn21.
[3]"Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system."
Steele R.A., Opella S.J.
Biochemistry 36:6885-6895(1997) [PubMed: 9188683] [Abstract]
Cited for: STRUCTURE BY NMR.
[4]"NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein involved in bacterial mercuric ion resistance."
Qian H., Sahlman L., Eriksson P.O., Hambraeus C., Edlund U., Sethson I.
Biochemistry 37:9316-9322(1998) [PubMed: 9649312] [Abstract]
Cited for: STRUCTURE BY NMR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01730 Genomic DNA. Translation: AAA92262.1.
K03089 Genomic DNA. Translation: AAB59076.1.
PIRRGEBHD. A03556.
S09524.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AFINMR-A20-91[»]
1AFJNMR-A20-91[»]
1DVWNMR-A25-42[»]
2HQINMR-A20-91[»]
ProteinModelPortalP04129.
SMRP04129. Positions 20-91.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
IPR001802. HG_scavenger.
IPR011795. MerP.
[Graphical view]
PfamPF00403. HMA. 1 hit.
[Graphical view]
PRINTSPR00946. HGSCAVENGER.
SUPFAMSSF55008. HeavyMe_transpt. 1 hit.
TIGRFAMsTIGR02052. MerP. 1 hit.
PROSITEPS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMERP_SHIFL
AccessionPrimary (citable) accession number: P04129
Secondary accession number(s): P07042
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: May 31, 2011
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families