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Protein

Cation efflux system protein CusF

Gene

cusF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Part of a cation efflux system that mediates resistance to copper and silver. Binds one copper per polypeptide.1 Publication

GO - Molecular functioni

  • copper chaperone activity Source: EcoCyc
  • copper ion binding Source: EcoCyc
  • metallochaperone activity Source: EcoliWiki
  • transition metal ion binding Source: EcoCyc

GO - Biological processi

  • cellular copper ion homeostasis Source: EcoCyc
  • detoxification of copper ion Source: EcoCyc
  • response to copper ion Source: EcoCyc
  • response to silver ion Source: EcoCyc
  • response to zinc ion Source: EcoCyc
Complete GO annotation...

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:G6321-MONOMER.
ECOL316407:JW0562-MONOMER.
MetaCyc:G6321-MONOMER.

Protein family/group databases

TCDBi2.A.6.1.4. the resistance-nodulation-cell division (rnd) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Cation efflux system protein CusF
Gene namesi
Name:cusF
Synonyms:cusX, ylcC
Ordered Locus Names:b0573, JW0562
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14234. cusF.

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
  • periplasmic space Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi25 – 273HHH → QQQ: No change in copper resistance. 1 Publication
Mutagenesisi48 – 481D → N: No change in copper resistance. 1 Publication
Mutagenesisi57 – 582HH → QQ: Slight decrease in copper resistance. 1 Publication
Mutagenesisi69 – 691M → I: Loss of copper resistance and strong decrease in copper binding; when associated with I-71. 1 Publication
Mutagenesisi71 – 711M → I: Loss of copper resistance and strong decrease in copper binding; when associated with I-69. 1 Publication
Mutagenesisi73 – 731F → Y: No change in copper resistance. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 11089Cation efflux system protein CusFPRO_0000021046Add
BLAST

Proteomic databases

PaxDbiP77214.

Expressioni

Inductioni

Transcriptionally regulated by CusR in response to copper and silver ions.1 Publication

Interactioni

Subunit structurei

The cus efflux system is composed of CusA, CusB, CusC and CusF.

Protein-protein interaction databases

BioGridi4262045. 218 interactions.
DIPiDIP-9350N.
IntActiP77214. 2 interactions.
STRINGi511145.b0573.

Structurei

Secondary structure

1
110
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 4811Combined sources
Turni49 – 524Combined sources
Beta strandi53 – 586Combined sources
Helixi62 – 643Combined sources
Beta strandi68 – 747Combined sources
Beta strandi79 – 813Combined sources
Beta strandi89 – 979Combined sources
Beta strandi100 – 1089Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZEQX-ray1.50X28-110[»]
2QCPX-ray1.00X32-110[»]
2VB2X-ray1.70X23-110[»]
2VB3X-ray2.33X23-110[»]
3E6ZX-ray1.00X32-110[»]
ProteinModelPortaliP77214.
SMRiP77214. Positions 28-110.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77214.

Family & Domainsi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410624V. Bacteria.
COG5569. LUCA.
HOGENOMiHOG000126315.
InParanoidiP77214.
KOiK07810.
OMAiPAWANDH.

Family and domain databases

InterProiIPR021647. CusF_Ec.
[Graphical view]
PfamiPF11604. CusF_Ec. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P77214-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKALQVAMF SLFTVIGFNA QANEHHHETM SEAQPQVISA TGVVKGIDLE
60 70 80 90 100
SKKITIHHDP IAAVNWPEMT MRFTITPQTK MSEIKTGDKV AFNFVQQGNL
110
SLLQDIKVSQ
Length:110
Mass (Da):12,251
Last modified:February 1, 1997 - v1
Checksum:i494011382E05DB59
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82598 Genomic DNA. Translation: AAB40771.1.
U00096 Genomic DNA. Translation: AAC73674.1.
AP009048 Genomic DNA. Translation: BAA35207.1.
PIRiC64790.
RefSeqiNP_415105.1. NC_000913.3.
WP_000709870.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73674; AAC73674; b0573.
BAA35207; BAA35207; BAA35207.
GeneIDi945188.
KEGGiecj:JW0562.
eco:b0573.
PATRICi32116314. VBIEscCol129921_0597.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82598 Genomic DNA. Translation: AAB40771.1.
U00096 Genomic DNA. Translation: AAC73674.1.
AP009048 Genomic DNA. Translation: BAA35207.1.
PIRiC64790.
RefSeqiNP_415105.1. NC_000913.3.
WP_000709870.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZEQX-ray1.50X28-110[»]
2QCPX-ray1.00X32-110[»]
2VB2X-ray1.70X23-110[»]
2VB3X-ray2.33X23-110[»]
3E6ZX-ray1.00X32-110[»]
ProteinModelPortaliP77214.
SMRiP77214. Positions 28-110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262045. 218 interactions.
DIPiDIP-9350N.
IntActiP77214. 2 interactions.
STRINGi511145.b0573.

Protein family/group databases

TCDBi2.A.6.1.4. the resistance-nodulation-cell division (rnd) superfamily.

Proteomic databases

PaxDbiP77214.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73674; AAC73674; b0573.
BAA35207; BAA35207; BAA35207.
GeneIDi945188.
KEGGiecj:JW0562.
eco:b0573.
PATRICi32116314. VBIEscCol129921_0597.

Organism-specific databases

EchoBASEiEB3985.
EcoGeneiEG14234. cusF.

Phylogenomic databases

eggNOGiENOG410624V. Bacteria.
COG5569. LUCA.
HOGENOMiHOG000126315.
InParanoidiP77214.
KOiK07810.
OMAiPAWANDH.

Enzyme and pathway databases

BioCyciEcoCyc:G6321-MONOMER.
ECOL316407:JW0562-MONOMER.
MetaCyc:G6321-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP77214.
PROiP77214.

Family and domain databases

InterProiIPR021647. CusF_Ec.
[Graphical view]
PfamiPF11604. CusF_Ec. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCUSF_ECOLI
AccessioniPrimary (citable) accession number: P77214
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: September 7, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The cus system plays an important role in copper tolerance under anaerobic growth and, under extreme copper stress, in aerobic growth.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.