MCO_STAAU
ID MCO_STAAU Reviewed; 447 AA.
AC Q69HT9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Multicopper oxidase mco;
DE EC=1.-.-.-;
GN Name=mco;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A MULTICOPPER OXIDASE,
RP COFACTOR, AND INDUCTION BY COPPER.
RC STRAIN=ATCC 12600 / DSM 20231 / IAM 12544 / NCDO 949 / NCTC 8532;
RX PubMed=16151171; DOI=10.1128/aem.71.9.5650-5653.2005;
RA Sitthisak S., Howieson K., Amezola C., Jayaswal R.K.;
RT "Characterization of a multicopper oxidase gene from Staphylococcus
RT aureus.";
RL Appl. Environ. Microbiol. 71:5650-5653(2005).
CC -!- FUNCTION: May be involved in copper homeostasis and oxidative stress
CC response. Oxidizes the substrate 3,3'-dimethoxybenzidine in vitro. Also
CC possesses low levels of phenoloxidase and ferroxidase activities.
CC {ECO:0000269|PubMed:16151171}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by copper. {ECO:0000269|PubMed:16151171}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ17236.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY259130; AAQ17236.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q69HT9; -.
DR SMR; Q69HT9; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW Copper; Cytoplasm; Metal-binding; Oxidoreductase.
FT CHAIN 1..447
FT /note="Multicopper oxidase mco"
FT /id="PRO_0000336995"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 428
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 429
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
SQ SEQUENCE 447 AA; 50840 MW; 52E0AE6AA6606E0C CRC64;
MMDMKENDQK RNDMMDMKSH DERKNLNSSQ GKNEITFPKV LDPKKDNNGY KSYTLKAQKG
KTEFYKGNFS NTLGYNGNLL GPTLKLKKGD KVKIKLVNNL DENTTFHWHG LEIDGKVDGG
PSQVIKPGKE KTIKFEVKQE AATLWYHPHP SPNTAKQVYN GLSGLLYIED DKKNNYPSNY
GKNDLPIIIQ DKTFVSKKLN YTKTKDEDGT QGDTVLVNGK VDPKLTTKEG KIRLRLLNGS
NARDLNLKLS NNQSFEYIAS EGGHLEKTKK LKEINLAPSA RKEIVIDLSK MKEDKVNLVD
NDETVILPII NKEKSTNKDT TPKVDKKIKL EGMDDNVTIN GKKFDPNRID FTQKVNRKET
WEIENVKDKM SGMKHPFHIH GTQFKVLSVD GKKPSEDMRG KKDVISLEPG QKAKIEVVFK
NTGTYMFHCH ILEHEDNGMM GQIKVTK
