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    cusF copper/silver export system periplasmic binding protein [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945188, updated on 3-Dec-2024

    Summary

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    Official Symbol
    cusF
    Official Full Name
    copper/silver export system periplasmic binding protein
    Primary source
    ECOCYC:G6321
    Locus tag
    b0573
    See related
    ASAP:ABE-0001967
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    cusX; ECK0565; ylcC
    Summary
    cusF is in the cusCFBA Cu/Ag efflux operon regulated by Cu and Ag. [More information is available at EcoGene: EG14234]. CusF is a periplasmic binding protein involved in the detoxification of copper and silver ions in Escherichia coli as part of the CusCFBA copper/silver efflux system. [More information is available at EcoCyc: G6321].
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    Genomic context

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    Sequence:
    NC_000913.3 (597131..597463)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene sensor histidine kinase CusS Neighboring gene DNA-binding transcriptional activator CusR Neighboring gene copper/silver export system outer membrane channel Neighboring gene copper/silver export system membrane fusion protein Neighboring gene copper/silver export system RND permease

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Expression and purification of recombinant proteins in Escherichia coli tagged with the metal-binding protein CusF. Cantu-Bustos JE, et al. Protein Expr Purif, 2016 May. PMID 26805756
    2. Subcellular targeting of bacterial CusF enhances Cu accumulation and alters root to shoot Cu translocation in arabidopsis. Yu P, et al. Plant Cell Physiol, 2014 Sep. PMID 24951313
    3. Tryptophan Cu(I)-pi interaction fine-tunes the metal binding properties of the bacterial metallochaperone CusF. Loftin IR, et al. J Biol Inorg Chem, 2009 Aug. PMID 19381697, Free PMC Article
    4. Periplasmic oxidized-protein repair during copper stress in E. coli: A focus on the metallochaperone CusF. Vergnes A, et al. PLoS Genet, 2022 Jul. PMID 35816552, Free PMC Article
    5. N-terminal region of CusB is sufficient for metal binding and metal transfer with the metallochaperone CusF. Mealman TD, et al. Biochemistry, 2012 Aug 28. PMID 22812620, Free PMC Article

    See all (39) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Periplasmic oxidized-protein repair during copper stress in E. coli: A focus on the metallochaperone CusF.
      Title: Periplasmic oxidized-protein repair during copper stress in E. coli: A focus on the metallochaperone CusF.
    2. We therefore recommend the use of CusF as a viable alternative to MBP or GST as a fusion protein/affinity tag for the production of soluble recombinant proteins in E. coli.
      Title: Expression and purification of recombinant proteins in Escherichia coli tagged with the metal-binding protein CusF.
    3. Arabidopsis with cell wall-, cytosol- and vacuole-targeted CusF had increased Cu accumulation; in particular, plants expressing CusF in the cytoplasm transport Cu from roots to shoots more efficiently than plants with cell wallor vacuole-targeted CusF.
      Title: Subcellular targeting of bacterial CusF enhances Cu accumulation and alters root to shoot Cu translocation in arabidopsis.
    4. N-terminal region of CusB is sufficient for metal binding and metal transfer with the metallochaperone CusF.
      Title: N-terminal region of CusB is sufficient for metal binding and metal transfer with the metallochaperone CusF.
    5. Data reveal that N-terminal region of CusB interacts with metal-binding face of CusF; these proteins transiently interact in a metal-dependent fashion.
      Title: Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
    6. CusF uses a new metal recognition site wherein Cu(I) is tetragonally displaced from a Met2His ligand plane toward a conserved tryptophan
      Title: Cu(I) recognition via cation-pi and methionine interactions in CusF.
    7. In the CusF-Ag(I) structure, Ag(I) is coordinated by two methionines and a histidine, with a nearby tryptophan capping the metal site. Measurements on the CusF-Cu(I) complex show a similar environment for Cu(I).
      Title: Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy.
    8. N-terminus verified by Edman degradation on mature peptide
      Title: Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli.
    9. Electron paramagnetic resonance (EPR) spectroscopy has been used to structurally characterize the copper-binding site in CusF protein from Escherichia coli
      Title: Characterization of the copper(II) binding site in the pink copper binding protein CusF by electron paramagnetic resonance spectroscopy.
    10. CusF has a topology and metal binding site that are unique among copper proteins and provide insight into its function.
      Title: A novel copper-binding fold for the periplasmic copper resistance protein CusF.
    Submit: New GeneRIF Correction See all GeneRIFs (11)

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables copper chaperone activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables copper ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metallochaperone activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables transition metal ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in copper ion export NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    involved_in copper ion transmembrane transport NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    acts_upstream_of_or_within detoxification of copper ion IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    acts_upstream_of_or_within intracellular copper ion homeostasis IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    acts_upstream_of_or_within response to copper ion IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    acts_upstream_of_or_within response to silver ion IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    acts_upstream_of_or_within response to silver ion IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in response to toxic substance NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    acts_upstream_of_or_within response to zinc ion IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    involved_in silver ion transmembrane transport NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in outer membrane-bounded periplasmic space IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    located_in periplasmic space IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in periplasmic space IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    copper/silver export system periplasmic binding protein

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      597131..597463
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415105.1 copper/silver export system periplasmic binding protein [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415105.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5B9ALV5
      Conserved Domains (1) summary
      PRK09838
      Location:1 → 110
      PRK09838; periplasmic copper-binding protein; Provisional
    Nucleotide Protein
    Heading Accession and Version

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