MBCT_MYCTO
ID MBCT_MYCTO Reviewed; 186 AA.
AC P9WLP8; L0TB64; P64907; Q10869;
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=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=MT2043;
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).
RN [2]
RP INDUCTION IN MOUSE INFECTION MODEL.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=20628579; DOI=10.1371/journal.ppat.1000988;
RA Homolka S., Niemann S., Russell D.G., Rohde K.H.;
RT "Functional genetic diversity among Mycobacterium tuberculosis complex
RT clinical isolates: delineation of conserved core and lineage-specific
RT transcriptomes during intracellular survival.";
RL PLoS Pathog. 6:E1000988-E1000988(2010).
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 -!- INDUCTION: Expression induced in both active and resting C57BL/6 mouse
CC macrophages. {ECO:0000269|PubMed:20628579}.
CC -!- SIMILARITY: Belongs to the MbcT/ParT/Res family. {ECO:0000305}.
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DR EMBL; AE000516; AAK46319.1; -; Genomic_DNA.
DR PIR; C70757; C70757.
DR RefSeq; WP_003410001.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WLP8; -.
DR SMR; P9WLP8; -.
DR EnsemblBacteria; AAK46319; AAK46319; MT2043.
DR KEGG; mtc:MT2043; -.
DR PATRIC; fig|83331.31.peg.2200; -.
DR HOGENOM; CLU_124933_0_0_11; -.
DR Proteomes; UP000001020; 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 2: Evidence at transcript level;
KW NAD; Nucleotidyltransferase; Toxin-antitoxin system; Transferase.
FT CHAIN 1..186
FT /note="NAD(+) phosphorylase MbcT"
FT /id="PRO_0000427441"
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