ID   VPB15_MYCTO             Reviewed;          80 AA.
AC   P9WLM6; L0T9X2; Q10848;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Antitoxin VapB15;
GN   Name=vapB15; OrderedLocusNames=MT2064.1;
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: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC       Neutralizes the toxic effect of cognate toxin VapC15.
CC       {ECO:0000250|UniProtKB:P9WLM7}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P9WLM7};
CC       Note=The heterotrimer binds 1 Mg(2+)-Mn(2+) pair while the
CC       heterotetramer binds 2 pairs. Both metals are shared by the toxin-
CC       antitoxin pair. {ECO:0000250|UniProtKB:P9WLM7};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P9WLM7};
CC       Note=The heterotrimer binds 1 Mg(2+)-Mn(2+) pair while the
CC       heterotetramer binds 2 pairs. Both metals are shared by the toxin-
CC       antitoxin pair. {ECO:0000250|UniProtKB:P9WLM7};
CC   -!- SUBUNIT: Forms a VapB15-VapC15(2) heterotrimer and a VapB15(2)-
CC       VapC15(2) heterotetramer; each toxin pair forms a homodimer which
CC       creates a channel in which the antitoxin binds.
CC       {ECO:0000250|UniProtKB:P9WLM7}.
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DR   EMBL; AE000516; AAK46342.1; -; Genomic_DNA.
DR   PIR; G70759; G70759.
DR   RefSeq; WP_003899127.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WLM6; -.
DR   SMR; P9WLM6; -.
DR   EnsemblBacteria; AAK46342; AAK46342; MT2064.1.
DR   KEGG; mtc:MT2064.1; -.
DR   PATRIC; fig|83331.31.peg.2223; -.
DR   HOGENOM; CLU_179376_3_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR019239; VapB_antitoxin.
DR   Pfam; PF09957; VapB_antitoxin; 1.
PE   3: Inferred from homology;
KW   Magnesium; Manganese; Metal-binding; Toxin-antitoxin system.
FT   CHAIN           1..80
FT                   /note="Antitoxin VapB15"
FT                   /id="PRO_0000427452"
FT   REGION          60..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with toxin"
FT                   /evidence="ECO:0000250|UniProtKB:P9WLM7"
FT   BINDING         67
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_note="ligand shared with toxin"
FT                   /evidence="ECO:0000250|UniProtKB:P9WLM7"
SQ   SEQUENCE   80 AA;  8884 MW;  524F4A764E722AEB CRC64;
     MYSGVVSRTN IEIDDELVAA AQRMYRLDSK RSAVDLALRR LVGEPLGRDE ALALQGSGFD
     FSNDEIESFS DTDRKLADES