VPB22_MYCTU
ID VPB22_MYCTU Reviewed; 71 AA.
AC P71622; L0TB01;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Antitoxin VapB22;
GN Name=vapB22; OrderedLocusNames=Rv2830c;
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).
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 VapC22. {ECO:0000269|PubMed:20011113, ECO:0000305|PubMed:15718296}.
CC -!- SIMILARITY: Belongs to the phD/YefM antitoxin family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45631.1; -; Genomic_DNA.
DR PIR; A70693; A70693.
DR RefSeq; NP_217346.1; NC_000962.3.
DR RefSeq; WP_003912003.1; NZ_NVQJ01000006.1.
DR AlphaFoldDB; P71622; -.
DR SMR; P71622; -.
DR STRING; 83332.Rv2830c; -.
DR PaxDb; P71622; -.
DR DNASU; 888537; -.
DR GeneID; 888537; -.
DR KEGG; mtu:Rv2830c; -.
DR TubercuList; Rv2830c; -.
DR eggNOG; COG4118; Bacteria.
DR OMA; FRGVAMT; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0097351; F:toxin sequestering activity; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; IMP:MTBBASE.
DR InterPro; IPR006442; Antitoxin_Phd/YefM.
DR InterPro; IPR036165; YefM-like_sf.
DR Pfam; PF02604; PhdYeFM_antitox; 1.
DR SUPFAM; SSF143120; SSF143120; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..71
FT /note="Antitoxin VapB22"
FT /id="PRO_0000408047"
SQ SEQUENCE 71 AA; 7483 MW; 7F79A4D85601879A CRC64;
MTATEVKAKI LSLLDEVAQG EEIEITKHGR TVARLVAATG PHALKGRFSG VAMAAADDDE
LFTTGVSWNV S