MBCTN_METTR
ID MBCTN_METTR Reviewed; 30 AA.
AC E3YBA4;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Methanobactin mb-OB3b {ECO:0000303|PubMed:15361623, ECO:0000312|EMBL:EFS20503.1};
DE AltName: Full=Copper-binding compound {ECO:0000303|PubMed:15361623};
DE Short=CBC {ECO:0000303|PubMed:15361623};
DE AltName: Full=Hydrogen peroxide reductase {ECO:0000303|PubMed:18372044};
DE EC=1.11.1.- {ECO:0000269|PubMed:18372044};
DE AltName: Full=Superoxide dismutase {ECO:0000303|PubMed:18372044};
DE EC=1.15.1.1 {ECO:0000269|PubMed:18372044};
DE Flags: Precursor;
GN Name=mbnA {ECO:0000312|EMBL:EFS20503.1}; ORFNames=MettrDRAFT_4473;
OS Methylosinus trichosporium.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylocystaceae; Methylosinus.
OX NCBI_TaxID=426;
RN [1] {ECO:0000312|EMBL:EFS20503.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC {ECO:0000312|EMBL:EFS20503.1};
RX PubMed=20952571; DOI=10.1128/jb.01144-10;
RA Stein L.Y., Yoon S., Semrau J.D., Dispirito A.A., Murrell J.C.,
RA Vuilleumier S., Kalyuzhnaya M.G., Op den Camp H.J., Bringel F., Bruce D.,
RA Cheng J.F., Copeland A., Goodwin L., Han S., Hauser L., Jetten M.S.,
RA Lajus A., Land M.L., Lapidus A., Lucas S., Medigue C., Pitluck S.,
RA Woyke T., Zeytun A., Klotz M.G.;
RT "Genome sequence of the obligate methanotroph Methylosinus trichosporium
RT strain OB3b.";
RL J. Bacteriol. 192:6497-6498(2010).
RN [2] {ECO:0000305}
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 20-30 IN COMPLEX
RP WITH COPPER, DISULFIDE BOND, METAL-BINDING, AND CROSS-LINKS.
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC {ECO:0000269|PubMed:15361623};
RX PubMed=15361623; DOI=10.1126/science.1098322;
RA Kim H.J., Graham D.W., DiSpirito A.A., Alterman M.A., Galeva N.,
RA Larive C.K., Asunskis D., Sherwood P.M.;
RT "Methanobactin, a copper-acquisition compound from methane-oxidizing
RT bacteria.";
RL Science 305:1612-1615(2004).
RN [3] {ECO:0000305}
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, AND MASS SPECTROMETRY.
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC {ECO:0000269|PubMed:15794651};
RX PubMed=15794651; DOI=10.1021/bi047367r;
RA Kim H.J., Galeva N., Larive C.K., Alterman M., Graham D.W.;
RT "Purification and physical-chemical properties of methanobactin: a
RT chalkophore from Methylosinus trichosporium OB3b.";
RL Biochemistry 44:5140-5148(2005).
RN [4] {ECO:0000305}
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC {ECO:0000269|PubMed:16332035};
RX PubMed=16332035; DOI=10.1021/ja0558140;
RA Hakemian A.S., Tinberg C.E., Kondapalli K.C., Telser J., Hoffman B.M.,
RA Stemmler T.L., Rosenzweig A.C.;
RT "The copper chelator methanobactin from Methylosinus trichosporium OB3b
RT binds copper(I).";
RL J. Am. Chem. Soc. 127:17142-17143(2005).
RN [5] {ECO:0000305}
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC {ECO:0000269|PubMed:16207923};
RX PubMed=16207923; DOI=10.1099/mic.0.28169-0;
RA Choi D.W., Antholine W.E., Do Y.S., Semrau J.D., Kisting C.J., Kunz R.C.,
RA Campbell D., Rao V., Hartsel S.C., DiSpirito A.A.;
RT "Effect of methanobactin on the activity and electron paramagnetic
RT resonance spectra of the membrane-associated methane monooxygenase in
RT Methylococcus capsulatus Bath.";
RL Microbiology 151:3417-3426(2005).
RN [6] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC {ECO:0000269|PubMed:16445286};
RX PubMed=16445286; DOI=10.1021/bi051815t;
RA Choi D.W., Zea C.J., Do Y.S., Semrau J.D., Antholine W.E., Hargrove M.S.,
RA Pohl N.L., Boyd E.S., Geesey G.G., Hartsel S.C., Shafe P.H.,
RA McEllistrem M.T., Kisting C.J., Campbell D., Rao V., de la Mora A.M.,
RA Dispirito A.A.;
RT "Spectral, kinetic, and thermodynamic properties of Cu(I) and Cu(II)
RT binding by methanobactin from Methylosinus trichosporium OB3b.";
RL Biochemistry 45:1442-1453(2006).
RN [7] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC {ECO:0000269|PubMed:17070918};
RX PubMed=17070918; DOI=10.1016/j.jinorgbio.2006.08.017;
RA Choi D.W., Do Y.S., Zea C.J., McEllistrem M.T., Lee S.W., Semrau J.D.,
RA Pohl N.L., Kisting C.J., Scardino L.L., Hartsel S.C., Boyd E.S.,
RA Geesey G.G., Riedel T.P., Shafe P.H., Kranski K.A., Tritsch J.R.,
RA Antholine W.E., DiSpirito A.A.;
RT "Spectral and thermodynamic properties of Ag(I), Au(III), Cd(II), Co(II),
RT Fe(III), Hg(II), Mn(II), Ni(II), Pb(II), U(IV), and Zn(II) binding by
RT methanobactin from Methylosinus trichosporium OB3b.";
RL J. Inorg. Biochem. 100:2150-2161(2006).
RN [8] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC {ECO:0000269|PubMed:17615240};
RX PubMed=17615240; DOI=10.1073/pnas.0702879104;
RA Knapp C.W., Fowle D.A., Kulczycki E., Roberts J.A., Graham D.W.;
RT "Methane monooxygenase gene expression mediated by methanobactin in the
RT presence of mineral copper sources.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12040-12045(2007).
RN [9] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC {ECO:0000269|PubMed:18372044};
RX PubMed=18372044; DOI=10.1016/j.jinorgbio.2008.02.003;
RA Choi D.W., Semrau J.D., Antholine W.E., Hartsel S.C., Anderson R.C.,
RA Carey J.N., Dreis A.M., Kenseth E.M., Renstrom J.M., Scardino L.L.,
RA Van Gorden G.S., Volkert A.A., Wingad A.D., Yanzer P.J., McEllistrem M.T.,
RA de la Mora A.M., DiSpirito A.A.;
RT "Oxidase, superoxide dismutase, and hydrogen peroxide reductase activities
RT of methanobactin from types I and II methanotrophs.";
RL J. Inorg. Biochem. 102:1571-1580(2008).
RN [10] {ECO:0000305}
RP IDENTIFICATION, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC {ECO:0000269|PubMed:20961038};
RX PubMed=20961038; DOI=10.1021/bi1014375;
RA Krentz B.D., Mulheron H.J., Semrau J.D., Dispirito A.A., Bandow N.L.,
RA Haft D.H., Vuilleumier S., Murrell J.C., McEllistrem M.T., Hartsel S.C.,
RA Gallagher W.H.;
RT "A comparison of methanobactins from Methylosinus trichosporium OB3b and
RT Methylocystis strain Sb2 predicts methanobactins are synthesized from
RT diverse peptide precursors modified to create a common core for binding and
RT reducing copper ions.";
RL Biochemistry 49:10117-10130(2010).
RN [11] {ECO:0000305}
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC {ECO:0000269|PubMed:20817303};
RX PubMed=20817303; DOI=10.1016/j.jinorgbio.2010.08.002;
RA Choi D.W., Bandow N.L., McEllistrem M.T., Semrau J.D., Antholine W.E.,
RA Hartsel S.C., Gallagher W., Zea C.J., Pohl N.L., Zahn J.A., DiSpirito A.A.;
RT "Spectral and thermodynamic properties of methanobactin from gamma-
RT proteobacterial methane oxidizing bacteria: a case for copper competition
RT on a molecular level.";
RL J. Inorg. Biochem. 104:1240-1247(2010).
RN [12] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC {ECO:0000269|PubMed:21299876};
RX PubMed=21299876; DOI=10.1186/1467-4866-12-2;
RA Pesch M.L., Christl I., Barmettler K., Kraemer S.M., Kretzschmar R.;
RT "Isolation and purification of Cu-free methanobactin from Methylosinus
RT trichosporium OB3b.";
RL Geochem. Trans. 12:2-2(2011).
RN [13] {ECO:0007744|PDB:2XJH, ECO:0007744|PDB:2XJI}
RP FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, X-RAY CRYSTALLOGRAPHY
RP (0.9 ANGSTROMS) OF 20-30 IN COMPLEX WITH COPPER, DISULFIDE BOND,
RP METAL-BINDING, AND CROSS-LINKS.
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC {ECO:0000269|PubMed:21254756};
RX PubMed=21254756; DOI=10.1021/ic101965j;
RA El Ghazouani A., Basle A., Firbank S.J., Knapp C.W., Gray J., Graham D.W.,
RA Dennison C.;
RT "Copper-binding properties and structures of methanobactins from
RT Methylosinus trichosporium OB3b.";
RL Inorg. Chem. 50:1378-1391(2011).
RN [14] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC {ECO:0000269|PubMed:21900235};
RX PubMed=21900235; DOI=10.1074/jbc.m111.284984;
RA Balasubramanian R., Kenney G.E., Rosenzweig A.C.;
RT "Dual pathways for copper uptake by methanotrophic bacteria.";
RL J. Biol. Chem. 286:37313-37319(2011).
RN [15] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC {ECO:0000269|PubMed:21242075};
RX PubMed=21242075; DOI=10.1016/j.jtemb.2010.12.002;
RA Summer K.H., Lichtmannegger J., Bandow N., Choi D.W., DiSpirito A.A.,
RA Michalke B.;
RT "The biogenic methanobactin is an effective chelator for copper in a rat
RT model for Wilson disease.";
RL J. Trace Elem. Med. Biol. 25:36-41(2011).
RN [16] {ECO:0000305}
RP STRUCTURE BY NMR OF 20-30 IN COMPLEX WITH COPPER, DISULFIDE BOND,
RP METAL-BINDING, AND CROSS-LINKS.
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b
RC {ECO:0000269|PubMed:18729522};
RX PubMed=18729522; DOI=10.1021/ja804747d;
RA Behling L.A., Hartsel S.C., Lewis D.E., DiSpirito A.A., Choi D.W.,
RA Masterson L.R., Veglia G., Gallagher W.H.;
RT "NMR, mass spectrometry and chemical evidence reveal a different chemical
RT structure for methanobactin that contains oxazolone rings.";
RL J. Am. Chem. Soc. 130:12604-12605(2008).
CC -!- FUNCTION: Chalkophore involved in scavenging, uptake and suppression of
CC toxicity of copper. Each apo-methanobactin (apo-mb) complexes 1 Cu(2+)
CC or Cu(1+) ion to form Cu(1+)-mb (Cu-mb) which is then taken up by the
CC cell. Enhances growth rate in the presence of copper and reduces growth
CC lag upon exposition to elevated levels of copper. Cu-mb contributes to
CC the switchover from soluble methane monooxygenase (sMMO) to the
CC membrane-bound particulate MMO (pMMO) by inducing transcription of pMMO
CC subunit A. It also stimulates the enzymatic activity of pMMO. In the
CC absence of copper, binds other metal ions, like Zn(2+), Ag(1+), Au(3+),
CC Co(2+), Cd(2+), Fe(3+), Hg(2+), Mn(2+), Ni(2+), Pb(2+) or U(6+), but
CC not Ba(2+), Ca(2+), La(2+), Mg(2+) or Sr(2+). Uptake is an active
CC process, which may involve TonB-dependent transporters, and as such
CC does not involve porins. Cu-Mb can be taken up by other methanotrophic
CC bacteria but not by E.coli. Has Cu-dependent superoxide dismutase-like
CC activity. Shows reductant-dependent oxidase and hydrogen peroxide
CC reductase activities. Reduces copper-levels in liver in a rat model of
CC Wilson disease. {ECO:0000269|PubMed:15361623,
CC ECO:0000269|PubMed:15794651, ECO:0000269|PubMed:16207923,
CC ECO:0000269|PubMed:16332035, ECO:0000269|PubMed:16445286,
CC ECO:0000269|PubMed:17070918, ECO:0000269|PubMed:17615240,
CC ECO:0000269|PubMed:18372044, ECO:0000269|PubMed:20817303,
CC ECO:0000269|PubMed:20961038, ECO:0000269|PubMed:21242075,
CC ECO:0000269|PubMed:21254756, ECO:0000269|PubMed:21900235}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1;
CC Evidence={ECO:0000269|PubMed:18372044};
CC -!- SUBUNIT: Monomer. In the absence of copper, may exist as a dimer or an
CC oligomer. {ECO:0000269|PubMed:15361623, ECO:0000269|PubMed:15794651,
CC ECO:0000269|PubMed:16207923, ECO:0000269|PubMed:16332035,
CC ECO:0000269|PubMed:18729522, ECO:0000269|PubMed:21254756}.
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasm. Note=Secreted as apo-mb,
CC uptake into the cytoplasm in complex with copper as Cu-mb. In the
CC cytoplasm, Cu-mb is associated with the cell membrane.
CC -!- INDUCTION: By low copper concentrations. {ECO:0000269|PubMed:15794651,
CC ECO:0000269|PubMed:20817303}.
CC -!- MASS SPECTROMETRY: Mass=1217; Method=MALDI; Note=In complex with
CC copper.; Evidence={ECO:0000269|PubMed:15361623,
CC ECO:0000269|PubMed:15794651, ECO:0000269|PubMed:16332035,
CC ECO:0000269|PubMed:18729522, ECO:0000269|PubMed:21254756,
CC ECO:0000269|PubMed:21299876, ECO:0000269|PubMed:21900235};
CC -!- MASS SPECTROMETRY: Mass=1217.46; Method=MALDI; Note=In complex with
CC copper.; Evidence={ECO:0000269|PubMed:15361623,
CC ECO:0000269|PubMed:15794651, ECO:0000269|PubMed:16332035,
CC ECO:0000269|PubMed:18729522, ECO:0000269|PubMed:21254756,
CC ECO:0000269|PubMed:21299876, ECO:0000269|PubMed:21900235};
CC -!- MASS SPECTROMETRY: Mass=1217.20; Method=MALDI; Note=In complex with
CC copper.; Evidence={ECO:0000269|PubMed:15361623,
CC ECO:0000269|PubMed:15794651, ECO:0000269|PubMed:16332035,
CC ECO:0000269|PubMed:18729522, ECO:0000269|PubMed:21254756,
CC ECO:0000269|PubMed:21299876, ECO:0000269|PubMed:21900235};
CC -!- MASS SPECTROMETRY: Mass=1217; Method=Electrospray; Note=In complex with
CC copper.; Evidence={ECO:0000269|PubMed:15361623,
CC ECO:0000269|PubMed:15794651, ECO:0000269|PubMed:16332035,
CC ECO:0000269|PubMed:18729522, ECO:0000269|PubMed:21254756,
CC ECO:0000269|PubMed:21299876, ECO:0000269|PubMed:21900235};
CC -!- MASS SPECTROMETRY: Mass=1217.18; Method=Electrospray; Note=In complex
CC with copper.; Evidence={ECO:0000269|PubMed:15361623,
CC ECO:0000269|PubMed:15794651, ECO:0000269|PubMed:16332035,
CC ECO:0000269|PubMed:18729522, ECO:0000269|PubMed:21254756,
CC ECO:0000269|PubMed:21299876, ECO:0000269|PubMed:21900235};
CC -!- MASS SPECTROMETRY: Mass=1154; Method=Electrospray; Note=Without
CC copper.; Evidence={ECO:0000269|PubMed:15361623,
CC ECO:0000269|PubMed:15794651, ECO:0000269|PubMed:16332035,
CC ECO:0000269|PubMed:21254756};
CC -!- MASS SPECTROMETRY: Mass=1154.46; Method=MALDI; Note=Without copper.;
CC Evidence={ECO:0000269|PubMed:15361623, ECO:0000269|PubMed:15794651,
CC ECO:0000269|PubMed:16332035, ECO:0000269|PubMed:21254756};
CC -!- MASS SPECTROMETRY: Mass=1154; Method=MALDI; Note=Without copper.;
CC Evidence={ECO:0000269|PubMed:15361623, ECO:0000269|PubMed:15794651,
CC ECO:0000269|PubMed:16332035, ECO:0000269|PubMed:21254756};
CC -!- MASS SPECTROMETRY: Mass=1154.24; Method=Electrospray; Note=Without
CC copper.; Evidence={ECO:0000269|PubMed:15361623,
CC ECO:0000269|PubMed:15794651, ECO:0000269|PubMed:16332035,
CC ECO:0000269|PubMed:21254756};
CC -!- CAUTION: The rearrangement modifications of the Cys residues involved
CC in the cross-links has not been described and the structure may be
CC subject to revision. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADVE01000073; EFS20503.1; -; Genomic_DNA.
DR PDB; 2XJH; X-ray; 0.92 A; A/B=21-30.
DR PDB; 2XJI; X-ray; 1.00 A; A/B/C/D/E/F=21-30.
DR PDBsum; 2XJH; -.
DR PDBsum; 2XJI; -.
DR AlphaFoldDB; E3YBA4; -.
DR SMR; E3YBA4; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR023963; Methanobactin_OB3b.
DR TIGRFAMs; TIGR04071; methanobac_OB3b; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Copper transport; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Ion transport; Metal-binding;
KW Oxidoreductase; Peroxidase; Secreted; Transport.
FT PROPEP 1..19
FT /evidence="ECO:0000269|PubMed:20961038"
FT /id="PRO_0000415151"
FT PEPTIDE 20..30
FT /note="Methanobactin mb-OB3b"
FT /evidence="ECO:0000269|PubMed:20961038"
FT /id="PRO_0000415152"
FT BINDING 21
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /evidence="ECO:0000269|PubMed:15361623,
FT ECO:0000269|PubMed:18729522, ECO:0000269|PubMed:21254756,
FT ECO:0007744|PDB:2XJH, ECO:0007744|PDB:2XJI"
FT BINDING 27
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /evidence="ECO:0000269|PubMed:15361623,
FT ECO:0000269|PubMed:18729522, ECO:0000269|PubMed:21254756,
FT ECO:0007744|PDB:2XJH, ECO:0007744|PDB:2XJI"
FT DISULFID 24..29
FT /evidence="ECO:0000269|PubMed:15361623,
FT ECO:0000269|PubMed:18729522, ECO:0000269|PubMed:21254756"
FT CROSSLNK 20..21
FT /note="2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic
FT acid (Leu-Cys)"
FT /evidence="ECO:0000269|PubMed:15361623,
FT ECO:0000269|PubMed:18729522, ECO:0000269|PubMed:21254756"
FT CROSSLNK 26..27
FT /note="Proline 5-hydroxy-oxazole-4-carbothionic acid (Pro-
FT Cys)"
SQ SEQUENCE 30 AA; 3143 MW; 80ACD598389EECE5 CRC64;
MTVKIAQKKV LPVIGRAAAL CGSCYPCSCM
