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

Summary

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Gene symbol: cusF
Gene description: copper/silver export system periplasmic binding protein
Primary source: ASAP:ABE-0001967
Locus tag: b0573
See related: ECOCYC:G6321
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_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
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.
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.
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.
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.
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.
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.
N-terminus verified by Edman degradation on mature peptide
Title: Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli.
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.
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.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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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

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Reference assembly

Genomic

NC_000913.3 Reference assembly

Range

597131..597463

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

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