Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cation efflux system protein CusF

Gene

cusF

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

Functioni

Part of a cation efflux system that mediates resistance to copper and silver. Binds one copper per polypeptide (PubMed:11399769, PubMed:24917681).2 Publications

Miscellaneous

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

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

Keywordsi

LigandCopper, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:G6321-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

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi25 – 27HHH → QQQ: No change in copper resistance. 1 Publication3
Mutagenesisi45 – 57KGIDL…KITIH → AGIDLESAAITIA: Wild-type Cu(+) binding, 50% decrease in Cu transfer from CopA; when associated with A-72. 1 PublicationAdd BLAST13
Mutagenesisi48D → N: No change in copper resistance. 1 Publication1
Mutagenesisi57 – 58HH → QQ: Slight decrease in copper resistance. 1 Publication2
Mutagenesisi69 – 71MTM → ITI: Binds Cu(+) very poorly, does not receive Cu(+) from CopA. 1 Publication3
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
Mutagenesisi72R → A: Wild-type Cu(+) binding, 50% decrease in Cu transfer from CopA; when associated with 45-A--A-57. 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. Interacts with copper-exporting P-type ATPase CopA; when this protein is precharged with copper it binds very little CopA (PubMed:24917681).1 Publication

Protein-protein interaction databases

BioGridi4262045, 218 interactors
DIPiDIP-9350N
IntActiP77214, 2 interactors
STRINGi316385.ECDH10B_0639

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
OMAiMHEQPAA

Family and domain databases

InterProiView protein in InterPro
IPR021647 CusF_Ec
PfamiView protein in Pfam
PF11604 CusF_Ec, 1 hit

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
PATRICifig|1411691.4.peg.1701

Similar proteinsi

Entry informationi

Entry nameiCUSF_ECOLI
AccessioniPrimary (citable) accession number: P77214
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: March 28, 2018
This is version 124 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health