ID   VAPB2_MYCTU             Reviewed;          73 AA.
AC   O07227; L0T336;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Antitoxin VapB2;
GN   Name=vapB2; OrderedLocusNames=Rv0300;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   POSSIBLE FUNCTION.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=15718296; DOI=10.1093/nar/gki201;
RA   Pandey D.P., Gerdes K.;
RT   "Toxin-antitoxin loci are highly abundant in free-living but lost from
RT   host-associated prokaryotes.";
RL   Nucleic Acids Res. 33:966-976(2005).
RN   [3]
RP   EXPRESSION IN M.SMEGMATIS, AND FUNCTION AS AN ANTITOXIN.
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=20011113; DOI=10.1371/journal.pgen.1000767;
RA   Ramage H.R., Connolly L.E., Cox J.S.;
RT   "Comprehensive functional analysis of Mycobacterium tuberculosis toxin-
RT   antitoxin systems: implications for pathogenesis, stress responses, and
RT   evolution.";
RL   PLoS Genet. 5:E1000767-E1000767(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS), POSSIBLE MODE OF ACTION, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=23011806; DOI=10.1002/pro.2161;
RA   Min A.B., Miallau L., Sawaya M.R., Habel J., Cascio D., Eisenberg D.;
RT   "The crystal structure of the Rv0301-Rv0300 VapBC-3 toxin-antitoxin complex
RT   from M. tuberculosis reveals a Mg(2+) ion in the active site and a putative
RT   RNA-binding Site.";
RL   Protein Sci. 21:1754-1767(2012).
CC   -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC       Upon expression in M.smegmatis neutralizes the effect of cognate toxin
CC       VapC2. The C-terminal helix of the antitoxin may obstruct the toxin's
CC       RNA-binding groove, blocking access to the active sites. Additionally,
CC       the C-terminal arginine of the antitoxin may remove Mg(2+) ions from
CC       the toxin active sites. {ECO:0000269|PubMed:20011113,
CC       ECO:0000269|PubMed:23011806, ECO:0000305|PubMed:15718296}.
CC   -!- SUBUNIT: Forms a homodimer, which binds to a toxin homodimer, which
CC       then oligomerizes further to a hetero-octamer. When bound to toxin
CC       VapC2 the toxin activity is inhibited; 1 antitoxin may suffice to
CC       inhibit toxin. {ECO:0000269|PubMed:23011806}.
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DR   EMBL; AL123456; CCP43030.1; -; Genomic_DNA.
DR   PIR; E70523; E70523.
DR   RefSeq; NP_214814.1; NC_000962.3.
DR   RefSeq; WP_003401563.1; NZ_NVQJ01000026.1.
DR   PDB; 3H87; X-ray; 1.49 A; C/D=1-73.
DR   PDBsum; 3H87; -.
DR   AlphaFoldDB; O07227; -.
DR   SMR; O07227; -.
DR   STRING; 83332.Rv0300; -.
DR   PaxDb; O07227; -.
DR   DNASU; 886588; -.
DR   GeneID; 886588; -.
DR   KEGG; mtu:Rv0300; -.
DR   TubercuList; Rv0300; -.
DR   eggNOG; ENOG5033C13; Bacteria.
DR   OMA; RRETHEI; -.
DR   EvolutionaryTrace; O07227; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0060701; P:negative regulation of ribonuclease activity; IDA:MTBBASE.
DR   GO; GO:0045727; P:positive regulation of translation; IMP:MTBBASE.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.1220.10; -; 1.
DR   InterPro; IPR013321; Arc_rbn_hlx_hlx.
DR   InterPro; IPR002145; CopG.
DR   InterPro; IPR010985; Ribbon_hlx_hlx.
DR   Pfam; PF01402; RHH_1; 1.
DR   SUPFAM; SSF47598; SSF47598; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Toxin-antitoxin system.
FT   CHAIN           1..73
FT                   /note="Antitoxin VapB2"
FT                   /id="PRO_0000408052"
FT   HELIX           11..24
FT                   /evidence="ECO:0007829|PDB:3H87"
FT   HELIX           28..40
FT                   /evidence="ECO:0007829|PDB:3H87"
FT   HELIX           49..58
FT                   /evidence="ECO:0007829|PDB:3H87"
FT   HELIX           60..63
FT                   /evidence="ECO:0007829|PDB:3H87"
FT   HELIX           65..71
FT                   /evidence="ECO:0007829|PDB:3H87"
SQ   SEQUENCE   73 AA;  8088 MW;  379D16E6EA7D7979 CRC64;
     MSDVLIRDIP DDVLASLDAI AARLGLSRTE YIRRRLAQDA QTARVTVTAA DLRRLRGAVA
     GLGDPELMRQ AWR