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Multicopper oxidase MmcO (EC 1.16.3.1) (Mycobacterium multicopper oxidase)

 MMCO_MYCTU              Reviewed;         504 AA.
I6WZK7;
27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 1.
10-OCT-2018, entry version 45.
RecName: Full=Multicopper oxidase MmcO {ECO:0000305};
EC=1.16.3.1 {ECO:0000269|PubMed:23772064};
AltName: Full=Mycobacterium multicopper oxidase {ECO:0000303|PubMed:23772064};
Flags: Precursor;
Name=mmcO {ECO:0000303|PubMed:23772064};
OrderedLocusNames=Rv0846c {ECO:0000312|EMBL:CCP43594.1},
RVBD_0846c {ECO:0000312|EMBL:AFN48726.1};
ORFNames=LH57_04620 {ECO:0000312|EMBL:AIR13579.1},
P425_00886 {ECO:0000312|EMBL:KBJ39045.1};
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
The Broad Institute Genome Sequencing Platform;
Galagan J., Kreiswirth B., Dobos K., Fortune S., Fitzgerald M.,
Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L.,
Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S.,
Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J.,
McCowan C., Murphy C., Pearson M., Poon T., Priest M., Roberts A.,
Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.;
"The genome sequence of Mycobacterium tuberculosis H37Rv.";
Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
The Broad Institute Genomics Platform;
The Broad Institute Genome Sequencing Center for Infectious Disease;
Earl A.M., Kreiswirth B., Gomez J., Victor T., Desjardins C.,
Abeel T., Young S., Zeng Q., Gargeya S., Abouelleil A., Alvarado L.,
Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S.,
Hansen M., Howarth C., Imamovic A., Larimer J., Murphy C., Naylor J.,
Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
Sykes S., Wortman J., Nusbaum C., Birren B.;
"The genome sequence of Mycobacterium tuberculosis H37Rv.";
Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 27294 / TMC 102 / H37Rv;
Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
Monaco A., King S., Sohrabi A.;
"Phylogenetic analysis of Mycobacterial species using whole genome
sequences.";
Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[6]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION,
DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-35 AND CYS-486.
STRAIN=ATCC 25618 / H37Rv;
PubMed=23772064; DOI=10.1128/JB.00546-13;
Rowland J.L., Niederweis M.;
"A multicopper oxidase is required for copper resistance in
Mycobacterium tuberculosis.";
J. Bacteriol. 195:3724-3733(2013).
[7]
INDUCTION, DISRUPTION PHENOTYPE, AND OVEREXPRESSION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=24549843; DOI=10.1128/mBio.00876-13;
Shi X., Festa R.A., Ioerger T.R., Butler-Wu S., Sacchettini J.C.,
Darwin K.H., Samanovic M.I.;
"The copper-responsive RicR regulon contributes to Mycobacterium
tuberculosis virulence.";
MBio 5:E00876-E00876(2014).
-!- FUNCTION: Required for copper resistance. In vitro, oxidizes
organic substrates and Fe(2+). May act in vivo by oxidation of
toxic periplasmic Cu(+). {ECO:0000269|PubMed:23772064}.
-!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O.
{ECO:0000269|PubMed:23772064}.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Evidence={ECO:0000250|UniProtKB:Q70KY3};
Note=Binds 4 Cu cations per monomer.
{ECO:0000250|UniProtKB:Q70KY3};
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:23772064}; Peripheral membrane protein
{ECO:0000269|PubMed:23772064}; Periplasmic side
{ECO:0000269|PubMed:23772064}. Periplasm
{ECO:0000269|PubMed:23772064}. Note=Could be associated with the
membrane through a lipidation site. {ECO:0000269|PubMed:23772064}.
-!- INDUCTION: Repressed by RicR (PubMed:24549843). Induced by copper
(PubMed:23772064, PubMed:24549843). {ECO:0000269|PubMed:23772064,
ECO:0000269|PubMed:24549843}.
-!- PTM: Predicted to be exported by the Tat system. The position of
the signal peptide cleavage has not been experimentally proven.
{ECO:0000255|PROSITE-ProRule:PRU00648}.
-!- DISRUPTION PHENOTYPE: Mutant is more sensitive to copper
(PubMed:23772064, PubMed:24549843). Deletion does not affect
virulence in mice (PubMed:24549843). {ECO:0000269|PubMed:23772064,
ECO:0000269|PubMed:24549843}.
-!- MISCELLANEOUS: Overexpression results in copper hyperresistance
but not hypervirulence. {ECO:0000269|PubMed:24549843}.
-!- SIMILARITY: Belongs to the multicopper oxidase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AL123456; CCP43594.1; -; Genomic_DNA.
EMBL; CP003248; AFN48726.1; -; Genomic_DNA.
EMBL; JLDD01000008; KBJ39045.1; -; Genomic_DNA.
EMBL; CP009480; AIR13579.1; -; Genomic_DNA.
RefSeq; NP_215361.1; NC_000962.3.
RefSeq; WP_003404392.1; NZ_KK339370.1.
ProteinModelPortal; I6WZK7; -.
SMR; I6WZK7; -.
STRING; 83332.Rv0846c; -.
PaxDb; I6WZK7; -.
EnsemblBacteria; AFN48726; AFN48726; RVBD_0846c.
EnsemblBacteria; AIR13579; AIR13579; LH57_04620.
EnsemblBacteria; CCP43594; CCP43594; Rv0846c.
EnsemblBacteria; KBJ39045; KBJ39045; P425_00886.
GeneID; 885207; -.
KEGG; mtu:Rv0846c; -.
KEGG; mtv:RVBD_0846c; -.
PATRIC; fig|83332.111.peg.938; -.
TubercuList; Rv0846c; -.
eggNOG; ENOG4107R16; Bacteria.
eggNOG; COG2132; LUCA.
KO; K22552; -.
OMA; WNQMRMS; -.
PhylomeDB; I6WZK7; -.
BRENDA; 1.16.3.1; 3445.
Proteomes; UP000001584; Chromosome.
Proteomes; UP000031768; Chromosome.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005507; F:copper ion binding; IEA:InterPro.
GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
CDD; cd13896; CuRO_3_CopA; 1.
Gene3D; 2.60.40.420; -; 3.
InterPro; IPR001117; Cu-oxidase.
InterPro; IPR011706; Cu-oxidase_2.
InterPro; IPR011707; Cu-oxidase_3.
InterPro; IPR033138; Cu_oxidase_CS.
InterPro; IPR002355; Cu_oxidase_Cu_BS.
InterPro; IPR008972; Cupredoxin.
InterPro; IPR034279; CuRO_3_CopA.
InterPro; IPR006311; TAT_signal.
Pfam; PF00394; Cu-oxidase; 1.
Pfam; PF07731; Cu-oxidase_2; 1.
Pfam; PF07732; Cu-oxidase_3; 1.
SUPFAM; SSF49503; SSF49503; 3.
PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PROSITE; PS51318; TAT; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Complete proteome; Copper;
Membrane; Metal-binding; Oxidoreductase; Periplasm;
Reference proteome; Signal.
SIGNAL 1 44 Tat-type signal. {ECO:0000255|PROSITE-
ProRule:PRU00648}.
CHAIN 45 504 Multicopper oxidase MmcO.
{ECO:0000255|PROSITE-ProRule:PRU00648}.
/FTId=PRO_0000433098.
DOMAIN 190 349 Plastocyanin-like. {ECO:0000255}.
METAL 120 120 Copper 1. {ECO:0000250|UniProtKB:Q70KY3}.
METAL 122 122 Copper 2. {ECO:0000250|UniProtKB:Q70KY3}.
METAL 161 161 Copper 2. {ECO:0000250|UniProtKB:Q70KY3}.
METAL 163 163 Copper 3. {ECO:0000250|UniProtKB:Q70KY3}.
METAL 437 437 Copper 4. {ECO:0000250|UniProtKB:Q70KY3}.
METAL 440 440 Copper 1. {ECO:0000250|UniProtKB:Q70KY3}.
METAL 442 442 Copper 3. {ECO:0000250|UniProtKB:Q70KY3}.
METAL 485 485 Copper 3. {ECO:0000250|UniProtKB:Q70KY3}.
METAL 486 486 Copper 4. {ECO:0000250|UniProtKB:Q70KY3}.
METAL 487 487 Copper 2. {ECO:0000250|UniProtKB:Q70KY3}.
METAL 491 491 Copper 4. {ECO:0000250|UniProtKB:Q70KY3}.
MUTAGEN 35 35 C->A: Slight decrease in activity.
{ECO:0000269|PubMed:23772064}.
MUTAGEN 486 486 C->A: Lack of activity.
{ECO:0000269|PubMed:23772064}.
SEQUENCE 504 AA; 53796 MW; 166BC12D4D89E403 CRC64;
MPELATSGNA FDKRRFSRRG FLGAGIASGF ALAACASKPT ASGAAGMTAA IDAAEAARPH
SGRTVTATLT PQPARIDLGG PIVSTLTYGN TIPGPLIRAT VGDEIVVSVT NRLGDPTSVH
WHGIALRNDM DGTEPATANI GPGGDFTYRF SVPDPGTYWA HPHVGLQGDH GLYLPVVVDD
PTEPGHYDAE WIIILDDWTD GIGKSPQQLY GELTDPNKPT MQNTTGMPEG EGVDSNLLGG
DGGDIAYPYY LINGRIPVAA TSFKAKPGQR IRIRIINSAA DTAFRIALAG HSMTVTHTDG
YPVIPTEVDA LLIGMAERYD VMVTAAGGVF PLVALAEGKN ALARALLSTG AGSPPDPQFR
PDELNWRVGT VEMFTAATTA NLGRPEPTHD LPVTLGGTMA KYDWTINGEP YSTTNPLHVR
LGQRPTLMFD NTTMMYHPIH LHGHTFQMIK ADGSPGARKD TVIVLPKQKM RAVLVADNPG
VWVMHCHNNY HQVAGMATRL DYIL


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