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Protein

Mercuric transport protein periplasmic component

Gene

merP

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi33 – 331MercuryPROSITE-ProRule annotation
Metal bindingi36 – 361MercuryPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Mercuric resistance, Transport

Keywords - Ligandi

Mercury, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mercuric transport protein periplasmic component
Alternative name(s):
Mercury scavenger protein
Periplasmic mercury ion-binding protein
Gene namesi
Name:merP
Encoded oniPlasmid IncFII R100 (NR1)0 Publication
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Chaini20 – 9172Mercuric transport protein periplasmic componentPRO_0000021679Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
91
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 276Combined sources
Turni29 – 324Combined sources
Beta strandi33 – 353Combined sources
Helixi36 – 4510Combined sources
Beta strandi48 – 569Combined sources
Turni57 – 604Combined sources
Beta strandi61 – 666Combined sources
Turni68 – 703Combined sources
Helixi73 – 8311Combined sources
Beta strandi88 – 903Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AFINMR-A20-91[»]
1AFJNMR-A20-91[»]
1DVWNMR-A25-42[»]
2HQINMR-A20-91[»]
ProteinModelPortaliP04129.
SMRiP04129. Positions 20-91.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04129.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 8967HMAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HMA domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR017969. Heavy-metal-associated_CS.
IPR006121. HMA_dom.
IPR011795. MerP.
IPR001802. MerP/CopZ.
[Graphical view]
PfamiPF00403. HMA. 1 hit.
[Graphical view]
PRINTSiPR00946. HGSCAVENGER.
SUPFAMiSSF55008. SSF55008. 1 hit.
TIGRFAMsiTIGR02052. MerP. 1 hit.
PROSITEiPS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04129-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKLFASLAL AAAVAPVWAA TQTVTLAVPG MTCAACPITV KKALSKVEGV
60 70 80 90
SKVDVGFEKR EAVVTFDDTK ASVQKLTKAT ADAGYPSSVK Q
Length:91
Mass (Da):9,414
Last modified:November 1, 1986 - v1
Checksum:i822183AC323031A5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511S → T in AAB59076 (PubMed:6530603).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01730 Genomic DNA. Translation: AAA92262.1.
K03089 Genomic DNA. Translation: AAB59076.1.
PIRiA03556. RGEBHD.
S09524.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01730 Genomic DNA. Translation: AAA92262.1.
K03089 Genomic DNA. Translation: AAB59076.1.
PIRiA03556. RGEBHD.
S09524.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AFINMR-A20-91[»]
1AFJNMR-A20-91[»]
1DVWNMR-A25-42[»]
2HQINMR-A20-91[»]
ProteinModelPortaliP04129.
SMRiP04129. Positions 20-91.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP04129.

Family and domain databases

InterProiIPR017969. Heavy-metal-associated_CS.
IPR006121. HMA_dom.
IPR011795. MerP.
IPR001802. MerP/CopZ.
[Graphical view]
PfamiPF00403. HMA. 1 hit.
[Graphical view]
PRINTSiPR00946. HGSCAVENGER.
SUPFAMiSSF55008. SSF55008. 1 hit.
TIGRFAMsiTIGR02052. MerP. 1 hit.
PROSITEiPS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiMERP_SHIFL
AccessioniPrimary (citable) accession number: P04129
Secondary accession number(s): P07042
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: November 11, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Plasmid, Transposable element

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.