ID   MBCT_MYCBO              Reviewed;         186 AA.
AC   P64908; A0A1R3Y0A4; Q10869; X2BJ76;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=NAD(+) phosphorylase MbcT {ECO:0000250|UniProtKB:P9WLP9};
DE            EC=2.4.2.- {ECO:0000250|UniProtKB:P9WLP9};
DE   AltName: Full=Mycobacterial cidal toxin MbcT {ECO:0000250|UniProtKB:P9WLP9};
GN   Name=mbcT; OrderedLocusNames=BQ2027_MB2011C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system.
CC       Degrades NAD(+) by phosphorolysis. Neutralized by its cognate antitoxin
CC       MbcA. {ECO:0000250|UniProtKB:P9WLP9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + phosphate = ADP-beta-D-ribose 1''-phosphate + H(+) +
CC         nicotinamide; Xref=Rhea:RHEA:20788, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:58753; Evidence={ECO:0000250|UniProtKB:P9WLP9};
CC   -!- SUBUNIT: Forms a heterotetramer with cognate antitoxin MbcA.
CC       {ECO:0000250|UniProtKB:P9WLP9}.
CC   -!- SIMILARITY: Belongs to the MbcT/ParT/Res family. {ECO:0000305}.
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DR   EMBL; LT708304; SIU00617.1; -; Genomic_DNA.
DR   RefSeq; NP_855661.1; NC_002945.3.
DR   RefSeq; WP_003410001.1; NC_002945.4.
DR   AlphaFoldDB; P64908; -.
DR   SMR; P64908; -.
DR   EnsemblBacteria; SIU00617; SIU00617; BQ2027_MB2011C.
DR   PATRIC; fig|233413.5.peg.2209; -.
DR   OMA; DSTRACM; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR014914; RES_dom.
DR   Pfam; PF08808; RES; 1.
DR   SMART; SM00953; RES; 1.
PE   3: Inferred from homology;
KW   NAD; Nucleotidyltransferase; Toxin-antitoxin system; Transferase.
FT   CHAIN           1..186
FT                   /note="NAD(+) phosphorylase MbcT"
FT                   /id="PRO_0000103919"
SQ   SEQUENCE   186 AA;  20281 MW;  8414F65A43BD909D CRC64;
     MSDALDEGLV QRIDARGTIE WSETCYRYTG AHRDALSGEG ARRFGGRWNP PLLFPAIYLA
     DSAQACMVEV ERAAQAASTT AEKMLEAAYR LHTIDVTDLA VLDLTTPQAR EAVGLENDDI
     YGDDWSGCQA VGHAAWFLHM QGVLVPAAGG VGLVVTAYEQ RTRPGQLQLR QSVDLTPALY
     QELRAT