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Protein

Blue copper oxidase CueO

Gene

cueO

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

Functioni

Probably involved in periplasmic detoxification of copper by oxidizing Cu+ to Cu2+ and thus preventing its uptake into the cytoplasm. Possesses phenoloxidase and ferroxidase activities and might be involved in the production of polyphenolic compounds and the prevention of oxidative damage in the periplasm.

Cofactori

Cu cationNote: Binds 4 Cu cations per monomer.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi101 – 1011Copper 1; type 2
Metal bindingi103 – 1031Copper 2; type 3
Metal bindingi141 – 1411Copper 2; type 3
Metal bindingi143 – 1431Copper 3; type 3
Metal bindingi443 – 4431Copper 4; type 1
Metal bindingi446 – 4461Copper 1; type 2
Metal bindingi448 – 4481Copper 3; type 3
Metal bindingi499 – 4991Copper 3; type 3
Metal bindingi500 – 5001Copper 4; type 1
Metal bindingi501 – 5011Copper 2; type 3
Metal bindingi505 – 5051Copper 4; type 1
Metal bindingi510 – 5101Copper 4; type 1

GO - Molecular functioni

  • copper ion binding Source: EcoliWiki
  • hydroquinone:oxygen oxidoreductase activity Source: GO_Central
  • oxidoreductase activity, oxidizing metal ions Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG12318-MONOMER.
ECOL316407:JW0119-MONOMER.
MetaCyc:EG12318-MONOMER.

Protein family/group databases

TCDBi1.B.76.1.8. the copper resistance putative porin (copb) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Blue copper oxidase CueO
Alternative name(s):
Copper efflux oxidase
Gene namesi
Name:cueO
Synonyms:yacK
Ordered Locus Names:b0123, JW0119
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12318. cueO.

Subcellular locationi

  • Periplasm

  • Note: It is exported via the Tat pathway.

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
Mutagenesisi500 – 5012CH → SR: Residual activity and loss of resistance to copper. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Tat-type signalPROSITE-ProRule annotation1 PublicationAdd
BLAST
Chaini29 – 516488Blue copper oxidase CueOPRO_0000002951Add
BLAST

Post-translational modificationi

Exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. Can also be exported by the Sec system.

Proteomic databases

PaxDbiP36649.
PRIDEiP36649.

Expressioni

Inductioni

By CueR, at increased levels of cytoplasmic cuprous ions.

Interactioni

Subunit structurei

Monomer.Curated

Protein-protein interaction databases

BioGridi4261957. 12 interactions.
DIPiDIP-11178N.
IntActiP36649. 3 interactions.
STRINGi511145.b0123.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi47 – 5913Combined sources
Beta strandi62 – 7413Combined sources
Beta strandi77 – 815Combined sources
Beta strandi85 – 928Combined sources
Beta strandi94 – 963Combined sources
Beta strandi101 – 1033Combined sources
Helixi109 – 1113Combined sources
Beta strandi124 – 1307Combined sources
Beta strandi135 – 1417Combined sources
Turni145 – 1473Combined sources
Helixi148 – 1536Combined sources
Beta strandi158 – 1636Combined sources
Helixi165 – 1695Combined sources
Turni177 – 1793Combined sources
Beta strandi180 – 1889Combined sources
Beta strandi194 – 1963Combined sources
Helixi202 – 2076Combined sources
Beta strandi212 – 2165Combined sources
Beta strandi219 – 2213Combined sources
Beta strandi223 – 23715Combined sources
Beta strandi244 – 2485Combined sources
Beta strandi254 – 2596Combined sources
Beta strandi262 – 27110Combined sources
Beta strandi273 – 2753Combined sources
Beta strandi280 – 2878Combined sources
Beta strandi293 – 2975Combined sources
Turni303 – 3064Combined sources
Turni308 – 3114Combined sources
Beta strandi314 – 32512Combined sources
Beta strandi348 – 3558Combined sources
Helixi357 – 37115Combined sources
Helixi372 – 3765Combined sources
Helixi381 – 3844Combined sources
Helixi400 – 4023Combined sources
Helixi404 – 4063Combined sources
Beta strandi408 – 4103Combined sources
Beta strandi421 – 4244Combined sources
Beta strandi426 – 4283Combined sources
Beta strandi430 – 4356Combined sources
Beta strandi443 – 4475Combined sources
Beta strandi452 – 4576Combined sources
Helixi464 – 4663Combined sources
Beta strandi470 – 48415Combined sources
Helixi492 – 4943Combined sources
Beta strandi496 – 5027Combined sources
Helixi503 – 5075Combined sources
Beta strandi511 – 5166Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KV7X-ray1.40A29-516[»]
1N68X-ray1.70A29-516[»]
1PF3X-ray1.50A29-516[»]
2FQDX-ray2.40A29-516[»]
2FQEX-ray1.92A29-516[»]
2FQFX-ray2.00A29-516[»]
2FQGX-ray2.30A29-516[»]
2YXVX-ray1.81A/B29-516[»]
2YXWX-ray1.50A/B29-516[»]
3NSCX-ray1.50A29-516[»]
3NSDX-ray2.00A29-516[»]
3NSFX-ray2.00A29-516[»]
3NSYX-ray2.10A29-516[»]
3NT0X-ray1.80A29-516[»]
3OD3X-ray1.10A29-516[»]
3PAUX-ray2.00A29-516[»]
3PAVX-ray1.45A29-516[»]
3QQXX-ray1.50A29-516[»]
3UAAX-ray1.70A29-516[»]
3UABX-ray1.30A29-516[»]
3UACX-ray1.30A29-516[»]
3UADX-ray1.10A29-516[»]
3UAEX-ray1.30A29-516[»]
4E9QX-ray1.30A29-516[»]
4E9RX-ray1.30A29-516[»]
4E9SX-ray1.06A29-516[»]
4E9TX-ray1.30A29-516[»]
4EF3X-ray1.90A29-516[»]
4HAKX-ray1.40A29-516[»]
4HALX-ray1.40A29-516[»]
4NERX-ray1.60A29-516[»]
ProteinModelPortaliP36649.
SMRiP36649. Positions 29-516.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36649.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 16397Plastocyanin-like 1Add
BLAST
Domaini164 – 410247Plastocyanin-like 2Add
BLAST
Domaini411 – 516106Plastocyanin-like 3Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi355 – 40046Met-richAdd
BLAST

Domaini

The methionine-rich domain could provide binding sites for exogenous copper ions. This methionine-rich region is probably important for copper tolerance in bacteria.

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 3 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4105E3B. Bacteria.
COG2132. LUCA.
HOGENOMiHOG000096435.
InParanoidiP36649.
KOiK14588.
OMAiFWQFGAG.
PhylomeDBiP36649.

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 4 hits.
PROSITEiPS00080. MULTICOPPER_OXIDASE2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P36649-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRRDFLKYS VALGVASALP LWSRAVFAAE RPTLPIPDLL TTDARNRIQL
60 70 80 90 100
TIGAGQSTFG GKTATTWGYN GNLLGPAVKL QRGKAVTVDI YNQLTEETTL
110 120 130 140 150
HWHGLEVPGE VDGGPQGIIP PGGKRSVTLN VDQPAATCWF HPHQHGKTGR
160 170 180 190 200
QVAMGLAGLV VIEDDEILKL MLPKQWGIDD VPVIVQDKKF SADGQIDYQL
210 220 230 240 250
DVMTAAVGWF GDTLLTNGAI YPQHAAPRGW LRLRLLNGCN ARSLNFATSD
260 270 280 290 300
NRPLYVIASD GGLLPEPVKV SELPVLMGER FEVLVEVNDN KPFDLVTLPV
310 320 330 340 350
SQMGMAIAPF DKPHPVMRIQ PIAISASGAL PDTLSSLPAL PSLEGLTVRK
360 370 380 390 400
LQLSMDPMLD MMGMQMLMEK YGDQAMAGMD HSQMMGHMGH GNMNHMNHGG
410 420 430 440 450
KFDFHHANKI NGQAFDMNKP MFAAAKGQYE RWVISGVGDM MLHPFHIHGT
460 470 480 490 500
QFRILSENGK PPAAHRAGWK DTVKVEGNVS EVLVKFNHDA PKEHAYMAHC
510
HLLEHEDTGM MLGFTV
Length:516
Mass (Da):56,556
Last modified:November 1, 1997 - v2
Checksum:i37D96B1C331CF30B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73234.1.
AP009048 Genomic DNA. Translation: BAB96698.2.
PIRiC64735.
RefSeqiNP_414665.1. NC_000913.3.
WP_001189647.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73234; AAC73234; b0123.
BAB96698; BAB96698; BAB96698.
GeneIDi947736.
KEGGiecj:JW0119.
eco:b0123.
PATRICi32115347. VBIEscCol129921_0125.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73234.1.
AP009048 Genomic DNA. Translation: BAB96698.2.
PIRiC64735.
RefSeqiNP_414665.1. NC_000913.3.
WP_001189647.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KV7X-ray1.40A29-516[»]
1N68X-ray1.70A29-516[»]
1PF3X-ray1.50A29-516[»]
2FQDX-ray2.40A29-516[»]
2FQEX-ray1.92A29-516[»]
2FQFX-ray2.00A29-516[»]
2FQGX-ray2.30A29-516[»]
2YXVX-ray1.81A/B29-516[»]
2YXWX-ray1.50A/B29-516[»]
3NSCX-ray1.50A29-516[»]
3NSDX-ray2.00A29-516[»]
3NSFX-ray2.00A29-516[»]
3NSYX-ray2.10A29-516[»]
3NT0X-ray1.80A29-516[»]
3OD3X-ray1.10A29-516[»]
3PAUX-ray2.00A29-516[»]
3PAVX-ray1.45A29-516[»]
3QQXX-ray1.50A29-516[»]
3UAAX-ray1.70A29-516[»]
3UABX-ray1.30A29-516[»]
3UACX-ray1.30A29-516[»]
3UADX-ray1.10A29-516[»]
3UAEX-ray1.30A29-516[»]
4E9QX-ray1.30A29-516[»]
4E9RX-ray1.30A29-516[»]
4E9SX-ray1.06A29-516[»]
4E9TX-ray1.30A29-516[»]
4EF3X-ray1.90A29-516[»]
4HAKX-ray1.40A29-516[»]
4HALX-ray1.40A29-516[»]
4NERX-ray1.60A29-516[»]
ProteinModelPortaliP36649.
SMRiP36649. Positions 29-516.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261957. 12 interactions.
DIPiDIP-11178N.
IntActiP36649. 3 interactions.
STRINGi511145.b0123.

Protein family/group databases

TCDBi1.B.76.1.8. the copper resistance putative porin (copb) family.

Proteomic databases

PaxDbiP36649.
PRIDEiP36649.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73234; AAC73234; b0123.
BAB96698; BAB96698; BAB96698.
GeneIDi947736.
KEGGiecj:JW0119.
eco:b0123.
PATRICi32115347. VBIEscCol129921_0125.

Organism-specific databases

EchoBASEiEB2223.
EcoGeneiEG12318. cueO.

Phylogenomic databases

eggNOGiENOG4105E3B. Bacteria.
COG2132. LUCA.
HOGENOMiHOG000096435.
InParanoidiP36649.
KOiK14588.
OMAiFWQFGAG.
PhylomeDBiP36649.

Enzyme and pathway databases

BioCyciEcoCyc:EG12318-MONOMER.
ECOL316407:JW0119-MONOMER.
MetaCyc:EG12318-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP36649.
PROiP36649.

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 4 hits.
PROSITEiPS00080. MULTICOPPER_OXIDASE2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCUEO_ECOLI
AccessioniPrimary (citable) accession number: P36649
Secondary accession number(s): P75655, Q8KMZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein is sensitive to oxygen deprivation. It probably plays a significant role in copper efflux under aerobic conditions.

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
  3. SIMILARITY comments
    Index of protein domains and families

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.