MG1655
W3110
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Gene Report : cueO
PEC Original Annotations
Essentiality
     Class non-essential
     References (PMID)  
     Deletion OCR32 (D)  
Related gene (W3110 PEC)
     Gene Search Search MG1655 PEC by gene name:  cueO
Related strains
     Strains Search Search strains by gene name:  cueO   Search strains by all related name:  cueO b0123 cuiD ECK0122 JW0119 o516 yacK

General information  (Go to Linear View:)
 Gene Name cueO  
 Alternative name b0123,cuiD,ECK0122,JW0119,o516,yacK  
 Location, Length 137,083 - 138,633 (  +  ) ;   2.95 min ; 1551 (bp) ,   516 (aa) Go to Linear View
 Product multicopper oxidase (laccase)  
 Operon Name cueO  
 Note  
 Function  
 Gene Ontology GO:0005507 ; copper ion binding ( cueO )
GO:0016491 ; oxidoreductase activity ( cueO )
GO:0042597 ; periplasmic space ( cueO )
GO:0046872 ; metal ion binding ( cueO )
 PID 1786314  
 EC number
  (KEGG Pathway)
 
 
Verified Protein Starts (data compiled from literature and appropriate citations are available from EcoGene)
     EcoGene cueO ( EG12318 )  
    Number of removed 28 aa cleaved  
SWISS-PROT  ( Show simple )
  botton Entry name(Acc.no) CUEO_ECOLI ( P36649 ; P75655 )
    -  Protein name Blue copper oxidase cueO precursor  
    -  Synonyms Copper efflux oxidase  
    -  Gene name Name=cueO; OrderedLocusNames=b0123;  
    -  Comments
  • FUNCTION:Probably involved in periplasmic detoxification of copper by oxidizing Cu(I) to Cu(II) 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.
  • COFACTOR:This protein belongs to the multicopper oxidases which contain three distinct Cu centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear.
  • SUBUNIT:Monomer (Probable).
  • SUBCELLULAR LOCATION:Periplasmic. It is exported via the Tat pathway.
  • INDUCTION:By cueR, at increased levels of cytoplasmic cuprous ions.
  • DOMAIN:The methionine-rich domain could provide binding sites for exogenous copper ions. This methionine-rich region is probably important for copper tolerance in bacteria.
  • MISCELLANEOUS:This protein is sensitive to oxygen deprivation. It probably plays a significant role in copper efflux under aerobic conditions.
  • SIMILARITY:Belongs to the multicopper oxidase family.
  • SIMILARITY:Contains 3 plastocyanin-like domains.
  • CAUTION:Ref.1 sequence differs from that shown due to a frameshift in position 464.  
  •   botton Entry name(Acc.no) Q8CWE2 ( Q8CWE2 )
        -  Protein name Blue copper oxidase cueO.  
        -  Synonyms  
        -  Gene name Name=yacK; OrderedLocusNames=c0152;  
        -  Comments
  • SUBCELLULAR LOCATION:Integral membrane protein. Outer membrane (By similarity).
  • SIMILARITY:Belongs to the fimbrial export usher family.  
  •   botton Entry name(Acc.no) CUEO_ECO57 ( Q8X947 )
        -  Protein name Blue copper oxidase cueO precursor  
        -  Synonyms Copper efflux oxidase  
        -  Gene name Name=cueO; OrderedLocusNames=z0133, ECs0127;  
        -  Comments
  • FUNCTION:Probably involved in periplasmic detoxification of copper by oxidizing Cu(I) to Cu(II) 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 (By similarity).
  • COFACTOR:This protein belongs to the multicopper oxidases which contain three distinct Cu centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear (By similarity).
  • SUBUNIT:Monomer (Probable).
  • SUBCELLULAR LOCATION:Periplasmic. It is exported via the Tat pathway (By similarity).
  • INDUCTION:By cueR, at increased levels of cytoplasmic cuprous ions (Probable).
  • DOMAIN:The methionine-rich domain could provide binding sites for exogenous copper ions. This methionine-rich region is probably important for copper tolerance in bacteria.
  • SIMILARITY:Belongs to the multicopper oxidase family.
  • SIMILARITY:Contains 3 plastocyanin-like domains.  

  •  Linear View (Whole Mode)
    View Location
       125.0  –  150.0 (KBP)

    Homology Analysis
    BLAST
        Bacteria
             GTOP cueO (  homologous genes of other bacterias  )  
        PDB     (database updated : 2007.02.20 )
             PSI-BLAST Chain A, Crystal Structure Of Cueo, A Multi-Copper Oxidase From E. Coli Involved In Copper Homeostasis  
        SWISS-PROT     (database updated : 2007.02.20 )
             BLAST Blue copper oxidase cueO precursor  
             PSI-BLAST Blue copper oxidase cueO precursor
        nr     (database updated : 2007.02.20 )
             BLAST multicopper oxidase (laccase) [Escherichia coli K12]  
    Pfam 28.0   (database updated : 2015-05 )
        Pfam
    PROSITE
        PROSITE ASN_GLYCOSYLATION    GLYCOSAMINOGLYCAN    CAMP_PHOSPHO_SITE    PKC_PHOSPHO_SITE    MYRISTYL    AMIDATION    MULTICOPPER_OXIDASE2     

    Other Cross-Reference
        COG COG2132Q 
        EcoCyc cueO 

    Sequences
    Amino acid
    FASTA format
    0001 MQRRDFLKYS VALGVASALP LWSRAVFAAE RPTLPIPDLL TTDARNRIQL TIGAGQSTFG GKTATTWGYN 
    0071 GNLLGPAVKL QRGKAVTVDI YNQLTEETTL HWHGLEVPGE VDGGPQGIIP PGGKRSVTLN VDQPAATCWF 
    0141 HPHQHGKTGR QVAMGLAGLV VIEDDEILKL MLPKQWGIDD VPVIVQDKKF SADGQIDYQL DVMTAAVGWF 
    0211 GDTLLTNGAI YPQHAAPRGW LRLRLLNGCN ARSLNFATSD NRPLYVIASD GGLLPEPVKV SELPVLMGER 
    0281 FEVLVEVNDN KPFDLVTLPV SQMGMAIAPF DKPHPVMRIQ PIAISASGAL PDTLSSLPAL PSLEGLTVRK 
    0351 LQLSMDPMLD MMGMQMLMEK YGDQAMAGMD HSQMMGHMGH GNMNHMNHGG KFDFHHANKI NGQAFDMNKP 
    0421 MFAAAKGQYE RWVISGVGDM MLHPFHIHGT QFRILSENGK PPAAHRAGWK DTVKVEGNVS EVLVKFNHDA 
    0491 PKEHAYMAHC HLLEHEDTGM MLGFTV
    
    
    Nucleotide
    FASTA format

    View sequence out neighbor 100bp
    -100                                             TGTCGATTAA ATTGTGTCTG CGGCTTGACC 
    -070 TTCCCGTAAG GGGAAGGACT ATGCTCAACG TTTGATTTTG TTTCGCCTGC TTAAGAATAA GGAAATAACT 
    0001 atgcaacgtc gtgatttctt aaaatattcc gtcgcgctgg gtgtggcttc ggctttgccg ctgtggagcc 
    0071 gcgcagtatt tgcggcagaa cgcccaacgt taccgatccc tgatttgctc acgaccgatg cccgtaatcg 
    0141 cattcagtta actattggcg caggccagtc cacctttggc gggaaaactg caactacctg gggctataac 
    0211 ggcaatctgc tggggccggc ggtgaaatta cagcgcggca aagcggtaac ggttgatatc tacaaccaac 
    0281 tgacggaaga gacaacgttg cactggcacg ggctggaagt accgggtgaa gtcgacggcg gcccgcaggg 
    0351 aattattccg ccaggtggca agcgctcggt gacgttgaac gttgatcaac ctgccgctac ctgctggttc 
    0421 catccgcatc agcacggcaa aaccgggcga caggtggcga tggggctggc tgggctggtg gtgattgaag 
    0491 atgacgagat cctgaaatta atgctgccaa aacagtgggg tatcgatgat gttccggtga tcgttcagga 
    0561 taagaaattt agcgccgacg ggcagattga ttatcaactg gatgtgatga ccgccgccgt gggctggttt 
    0631 ggcgatacgt tgctgaccaa cggtgcaatc tacccgcaac acgctgcccc gcgtggttgg ctgcgcctgc 
    0701 gtttgctcaa tggctgtaat gcccgttcgc tcaatttcgc caccagcgac aatcgcccgc tgtatgtgat 
    0771 tgccagcgac ggtggtctgc tacctgaacc agtgaaggtg agcgaactgc cggtgctgat gggcgagcgt 
    0841 tttgaagtgc tggtggaggt taacgataac aaaccctttg acctggtgac gctgccggtc agccagatgg 
    0911 ggatggcgat tgcgccgttt gataagcctc atccggtaat gcggattcag ccgattgcta ttagtgcctc 
    0981 cggtgctttg ccagacacat taagtagcct gcctgcgtta ccttcgctgg aagggctgac ggtacgcaag 
    1051 ctgcaactct ctatggaccc gatgctcgat atgatgggga tgcagatgct aatggagaaa tatggcgatc 
    1121 aggcgatggc cgggatggat cacagccaga tgatgggcca tatggggcac ggcaatatga atcatatgaa 
    1191 ccacggcggg aagttcgatt tccaccatgc caacaaaatc aacggtcagg cgtttgatat gaacaagccg 
    1261 atgtttgcgg cggcgaaagg gcaatacgaa cgttgggtta tctctggcgt gggcgacatg atgctgcatc 
    1331 cgttccatat ccacggcacg cagttccgta tcttgtcaga aaatggcaaa ccgccagcgg ctcatcgcgc 
    1401 gggctggaaa gataccgtta aggtagaagg taatgtcagc gaagtgctgg tgaagtttaa tcacgatgca 
    1471 ccgaaagaac atgcttatat ggcgcactgc catctgctgg agcatgaaga tacggggatg atgttagggt 
    1541 ttacggtata aAAAGACCGT ATTCGGAAAT ATGCCCGGAT CTCTCCGGGC ATTAAACTGA TGACAAACGC 
    1611 AAATCTGCCT GATGCGCTAC GCTTATCAGG CCTACGCTAG C