ID   VAPB_MYCS2              Reviewed;          84 AA.
AC   A0QRY5;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Antitoxin VapB;
GN   Name=vapB; OrderedLocusNames=MSMEG_1283, MSMEI_1245;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   FUNCTION AS A ANTITOXIN, FUNCTION IN TRANSCRIPTION REGULATION, SUBUNIT,
RP   INDUCTION, DNA-BINDING, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=19445953; DOI=10.1016/j.jmb.2009.05.006;
RA   Robson J., McKenzie J.L., Cursons R., Cook G.M., Arcus V.L.;
RT   "The vapBC operon from Mycobacterium smegmatis is an autoregulated toxin-
RT   antitoxin module that controls growth via inhibition of translation.";
RL   J. Mol. Biol. 390:353-367(2009).
RN   [5]
RP   FUNCTION AS AN ANTITOXIN, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=22366418; DOI=10.1128/jb.06790-11;
RA   McKenzie J.L., Robson J., Berney M., Smith T.C., Ruthe A., Gardner P.P.,
RA   Arcus V.L., Cook G.M.;
RT   "A VapBC toxin-antitoxin module is a posttranscriptional regulator of
RT   metabolic flux in mycobacteria.";
RL   J. Bacteriol. 194:2189-2204(2012).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=22199354; DOI=10.1074/jbc.m111.286856;
RA   Frampton R., Aggio R.B., Villas-Boas S.G., Arcus V.L., Cook G.M.;
RT   "Toxin-antitoxin systems of Mycobacterium smegmatis are essential for cell
RT   survival.";
RL   J. Biol. Chem. 287:5340-5356(2012).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=24417293; DOI=10.1111/1574-6968.12380;
RA   Demidenok O.I., Kaprelyants A.S., Goncharenko A.V.;
RT   "Toxin-antitoxin vapBC locus participates in formation of the dormant state
RT   in Mycobacterium smegmatis.";
RL   FEMS Microbiol. Lett. 352:69-77(2014).
CC   -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC       Upon overexpression neutralizes the effect of overexpressed cognate
CC       toxin VapC. Overexpression alone prevents cells from entering a
CC       nonculturable dormant state, probably as it binds endogenous VapC
CC       (PubMed:24417293). The TA system acts as a post-transcriptional
CC       regulator of carbon metabolism; in M.smegmatis 3 TA systems (VapB-VapC,
CC       MazE-MazF and Phd-Doc) may be involved in monitoring the nutritional
CC       supply and physiological state of the cell, linking catabolic with
CC       anabolic reactions. Translation of vapC mRNA requires VapB.
CC       {ECO:0000269|PubMed:19445953, ECO:0000269|PubMed:22366418,
CC       ECO:0000269|PubMed:24417293}.
CC   -!- SUBUNIT: Forms a complex with cognate toxin VapC.
CC       {ECO:0000269|PubMed:19445953, ECO:0000269|PubMed:22366418}.
CC   -!- INDUCTION: Expression is low but constitutive, and repressed by VapB-
CC       VapC. Member of the vapB-vapC operon. {ECO:0000269|PubMed:19445953}.
CC   -!- DISRUPTION PHENOTYPE: The vapB-vapC operon is not essential; cells grow
CC       faster than wild-type on rich and minimal glycerol-containing medium.
CC       The operon deletion mutants die faster than wild-type under potassium-
CC       limiting conditions, which is prevented by overexpression of vapB
CC       (PubMed:24417293). The vapB antitoxin gene can be disrupted without
CC       causing death, however despite elevated vapC transcription, no VapC
CC       protein could be detected, suggesting that RNA processing and
CC       translational coupling are important in VapC expression. A triple TA
CC       mutant (missing vapB-vapC, mazE-mazF and phd-doc TA systems) survives
CC       antibiotic challenge, suggesting the TA systems are not required to
CC       generate drug-resistant cells. However the triple mutant is more
CC       sensitive to oxidative and heat stress, and does not survive long term
CC       starvation during aerobic growth on complex medium. There is a
CC       difference in the level of branched-chain amino acids, which may play a
CC       role in monitoring the nutritional supply and physiological state of
CC       the cell. {ECO:0000269|PubMed:19445953, ECO:0000269|PubMed:22199354,
CC       ECO:0000269|PubMed:22366418, ECO:0000269|PubMed:24417293}.
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DR   EMBL; CP000480; ABK71133.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP37721.1; -; Genomic_DNA.
DR   RefSeq; WP_003892665.1; NZ_SIJM01000042.1.
DR   RefSeq; YP_885673.1; NC_008596.1.
DR   AlphaFoldDB; A0QRY5; -.
DR   SMR; A0QRY5; -.
DR   STRING; 246196.MSMEI_1245; -.
DR   EnsemblBacteria; ABK71133; ABK71133; MSMEG_1283.
DR   EnsemblBacteria; AFP37721; AFP37721; MSMEI_1245.
DR   GeneID; 66732745; -.
DR   KEGG; msg:MSMEI_1245; -.
DR   KEGG; msm:MSMEG_1283; -.
DR   PATRIC; fig|246196.19.peg.1272; -.
DR   eggNOG; COG4423; Bacteria.
DR   OMA; IIGYDEH; -.
DR   OrthoDB; 2005573at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR011660; VapB-like.
DR   Pfam; PF07704; PSK_trans_fac; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Reference proteome; Repressor; Toxin-antitoxin system;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..84
FT                   /note="Antitoxin VapB"
FT                   /id="PRO_0000420849"
SQ   SEQUENCE   84 AA;  9280 MW;  7DCCB9774047B15E CRC64;
     MALSIKHPEA DRLARELAAR TGETLTEAVV MALRERLART VGRTQVVPLR EELAAIRRRC
     AALPVLDDRT AESILGYDDR GLPS