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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi25 – 27HHH → QQQ: No change in copper resistance. 1 Publication3
Mutagenesisi48D → N: No change in copper resistance. 1 Publication1
Mutagenesisi57 – 58HH → QQ: Slight decrease in copper resistance. 1 Publication2
Mutagenesisi69M → I: Loss of copper resistance and strong decrease in copper binding; when associated with I-71. 1 Publication1
Mutagenesisi71M → I: Loss of copper resistance and strong decrease in copper binding; when associated with I-69. 1 Publication1
Mutagenesisi73F → Y: No change in copper resistance. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 211 PublicationAdd BLAST21
ChainiPRO_000002104622 – 110Cation efflux system protein CusFAdd BLAST89

Proteomic databases

PaxDbiP77214.
PRIDEiP77214.

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 interactors.
DIPiDIP-9350N.
IntActiP77214. 2 interactors.
STRINGi511145.b0573.

Structurei

Secondary structure

1110
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 48Combined sources11
Turni49 – 52Combined sources4
Beta strandi53 – 58Combined sources6
Helixi62 – 64Combined sources3
Beta strandi68 – 74Combined sources7
Beta strandi79 – 81Combined sources3
Beta strandi89 – 97Combined sources9
Beta strandi100 – 108Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

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

Proteomic databases

PaxDbiP77214.
PRIDEiP77214.

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: November 2, 2016
This is version 119 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.