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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

Miscellaneous

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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Cu cationNote: Binds 4 Cu cations per monomer.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi101Copper 1; type 21
Metal bindingi103Copper 2; type 31
Metal bindingi141Copper 2; type 31
Metal bindingi143Copper 3; type 31
Metal bindingi443Copper 4; type 11
Metal bindingi446Copper 1; type 21
Metal bindingi448Copper 3; type 31
Metal bindingi499Copper 3; type 31
Metal bindingi500Copper 4; type 11
Metal bindingi501Copper 2; type 31
Metal bindingi505Copper 4; type 11
Metal bindingi510Copper 4; type 11

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

  • detoxification of copper ion Source: EcoCyc
  • response to copper ion Source: EcoCyc

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
LigandCopper, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG12318-MONOMER
MetaCyc:EG12318-MONOMER

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.B.76.1.8 the copper resistance putative porin (copb) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Blue copper oxidase CueO
Alternative name(s):
Copper efflux oxidase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:cueO
Synonyms:yacK
Ordered Locus Names:b0123, JW0119
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG12318 cueO

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

  • Periplasm
  • Note: It is exported via the Tat pathway.

GO - Cellular componenti

Keywords - Cellular componenti

Periplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi500 – 501CH → SR: Residual activity and loss of resistance to copper. 1 Publication2

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 28Tat-type signalPROSITE-ProRule annotation1 PublicationAdd BLAST28
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000295129 – 516Blue copper oxidase CueOAdd BLAST488

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P36649

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P36649

PRoteomics IDEntifications database

More...
PRIDEi
P36649

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By CueR, at increased levels of cytoplasmic cuprous ions.

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.Curated

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4261957, 17 interactors

Database of interacting proteins

More...
DIPi
DIP-11178N

Protein interaction database and analysis system

More...
IntActi
P36649, 5 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_0103

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1516
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB 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[»]
5B7EX-ray1.42A1-516[»]
5B7FX-ray1.45A29-516[»]
5B7MX-ray1.80A/B/C29-516[»]
5GNOX-ray1.45A29-516[»]
5YS1X-ray1.49A1-516[»]
5YS5X-ray2.20A1-516[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P36649

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P36649

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P36649

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini67 – 163Plastocyanin-like 1Add BLAST97
Domaini164 – 410Plastocyanin-like 2Add BLAST247
Domaini411 – 516Plastocyanin-like 3Add BLAST106

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi355 – 400Met-richAdd BLAST46

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105E3B Bacteria
COG2132 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000096435

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P36649

KEGG Orthology (KO)

More...
KOi
K14588

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P36649

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.420, 3 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001117 Cu-oxidase
IPR011706 Cu-oxidase_2
IPR011707 Cu-oxidase_3
IPR002355 Cu_oxidase_Cu_BS
IPR008972 Cupredoxin
IPR006311 TAT_signal

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00394 Cu-oxidase, 1 hit
PF07731 Cu-oxidase_2, 1 hit
PF07732 Cu-oxidase_3, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49503 SSF49503, 3 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00080 MULTICOPPER_OXIDASE2, 1 hit
PS51318 TAT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i37D96B1C331CF30B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC73234.1
AP009048 Genomic DNA Translation: BAB96698.2

Protein sequence database of the Protein Information Resource

More...
PIRi
C64735

NCBI Reference Sequences

More...
RefSeqi
NP_414665.1, NC_000913.3
WP_001189647.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73234; AAC73234; b0123
BAB96698; BAB96698; BAB96698

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
947736

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0119
eco:b0123

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2159

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
PDB 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[»]
5B7EX-ray1.42A1-516[»]
5B7FX-ray1.45A29-516[»]
5B7MX-ray1.80A/B/C29-516[»]
5GNOX-ray1.45A29-516[»]
5YS1X-ray1.49A1-516[»]
5YS5X-ray2.20A1-516[»]
ProteinModelPortaliP36649
SMRiP36649
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261957, 17 interactors
DIPiDIP-11178N
IntActiP36649, 5 interactors
STRINGi316385.ECDH10B_0103

Protein family/group databases

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

Proteomic databases

jPOSTiP36649
PaxDbiP36649
PRIDEiP36649

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73234; AAC73234; b0123
BAB96698; BAB96698; BAB96698
GeneIDi947736
KEGGiecj:JW0119
eco:b0123
PATRICifig|1411691.4.peg.2159

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB2223
EcoGeneiEG12318 cueO

Phylogenomic databases

eggNOGiENOG4105E3B Bacteria
COG2132 LUCA
HOGENOMiHOG000096435
InParanoidiP36649
KOiK14588
PhylomeDBiP36649

Enzyme and pathway databases

BioCyciEcoCyc:EG12318-MONOMER
MetaCyc:EG12318-MONOMER

Miscellaneous databases

EvolutionaryTraceiP36649

Protein Ontology

More...
PROi
PR:P36649

Family and domain databases

Gene3Di2.60.40.420, 3 hits
InterProiView protein in InterPro
IPR001117 Cu-oxidase
IPR011706 Cu-oxidase_2
IPR011707 Cu-oxidase_3
IPR002355 Cu_oxidase_Cu_BS
IPR008972 Cupredoxin
IPR006311 TAT_signal
PfamiView protein in Pfam
PF00394 Cu-oxidase, 1 hit
PF07731 Cu-oxidase_2, 1 hit
PF07732 Cu-oxidase_3, 1 hit
SUPFAMiSSF49503 SSF49503, 3 hits
PROSITEiView protein in PROSITE
PS00080 MULTICOPPER_OXIDASE2, 1 hit
PS51318 TAT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCUEO_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P36649
Secondary accession number(s): P75655, Q8KMZ0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: January 16, 2019
This is version 159 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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