ID   MYMT_MYCTO              Reviewed;          53 AA.
AC   P9WK08; P0CI28; Q8VKQ2;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Metallothionein;
DE            Short=MT;
DE   AltName: Full=Copper-binding metallothionein;
DE            Short=Cu(I)-binding metallothionein;
DE   AltName: Full=Mycobacterial metallothionein;
DE   Flags: Precursor;
GN   Name=mymT; OrderedLocusNames=MT0196;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Metallothioneins are small proteins that have a high content
CC       of cysteine residues wich allow them to bind heavy metal ions through
CC       clusters of thiolate bonds. MymT binds up to seven ions of Cu(+), with
CC       a preference for four to six Cu(+) ions, in a solvent-shielded core.
CC       MymT protects M.tuberculosis from copper toxicity (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the metallothionein superfamily. {ECO:0000305}.
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DR   EMBL; AE000516; AAK44416.1; -; Genomic_DNA.
DR   RefSeq; WP_010886068.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WK08; -.
DR   EnsemblBacteria; AAK44416; AAK44416; MT0196.
DR   GeneID; 45424157; -.
DR   KEGG; mtc:MT0196; -.
DR   PATRIC; fig|83331.31.peg.213; -.
DR   HOGENOM; CLU_3137876_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Copper; Metal-binding; Metal-thiolate cluster.
FT   PROPEP          1..6
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000427736"
FT   CHAIN           7..53
FT                   /note="Metallothionein"
FT                   /id="PRO_0000427737"
FT   BINDING         17
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         17
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         19
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         22
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         24
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         24
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000305"
FT   BINDING         32
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         32
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000305"
FT   BINDING         33
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000305"
FT   BINDING         34
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         43
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         45
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         45
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   53 AA;  5719 MW;  B64C8B485F1668D7 CRC64;
     MRVIRMTNYE AGTLLTCSHE GCGCRVRIEV PCHCAGAGDA YRCTCGDELA PVK