RELB_MYCTU
ID RELB_MYCTU Reviewed; 89 AA.
AC O50462; L0T930;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Antitoxin RelB;
GN Name=relB; Synonyms=relB1; OrderedLocusNames=Rv1247c;
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 IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP FUNCTION AS AN ANTITOXIN, FUNCTION AS A TRANSCRIPTIONAL REGULATOR,
RP EXPRESSION IN M.SMEGMATIS, SUBUNIT, INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19114484; DOI=10.1128/jb.01318-08;
RA Korch S.B., Contreras H., Clark-Curtiss J.E.;
RT "Three Mycobacterium tuberculosis Rel toxin-antitoxin modules inhibit
RT mycobacterial growth and are expressed in infected human macrophages.";
RL J. Bacteriol. 191:1618-1630(2009).
RN [4]
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 [5]
RP FUNCTION AS AN ANTITOXIN, SUBUNIT, AND INTERACTION WITH RELG.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20498855; DOI=10.1371/journal.pone.0010672;
RA Yang M., Gao C., Wang Y., Zhang H., He Z.G.;
RT "Characterization of the interaction and cross-regulation of three
RT Mycobacterium tuberculosis RelBE modules.";
RL PLoS ONE 5:E10672-E10672(2010).
RN [6]
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).
CC -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC Upon expression in M.smegmatis neutralizes the effect of toxin RelE.
CC {ECO:0000269|PubMed:20498855}.
CC -!- FUNCTION: Induces its own promoter, in combination with RelE represses
CC its own promoter. Binds DNA in complex with toxin RelE but not alone.
CC {ECO:0000269|PubMed:19114484}.
CC -!- SUBUNIT: Interacts with toxin RelE, which neutralizes its toxicity.
CC Also interacts with toxins RelG and RelK in vitro, in M.smegmatis
CC coexpression with non-cognate toxins neutralizes the toxicity of RelG
CC while increasing the toxicity of RelK. {ECO:0000269|PubMed:19114484,
CC ECO:0000269|PubMed:20498855}.
CC -!- INDUCTION: Expressed in log phase cells. A member of the relBE operon.
CC {ECO:0000269|PubMed:19114484}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the phD/YefM antitoxin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP44003.1; -; Genomic_DNA.
DR PIR; F70953; F70953.
DR RefSeq; NP_215763.1; NC_000962.3.
DR RefSeq; WP_003406322.1; NZ_NVQJ01000049.1.
DR AlphaFoldDB; O50462; -.
DR SMR; O50462; -.
DR STRING; 83332.Rv1247c; -.
DR PaxDb; O50462; -.
DR DNASU; 887086; -.
DR GeneID; 45425217; -.
DR GeneID; 887086; -.
DR KEGG; mtu:Rv1247c; -.
DR TubercuList; Rv1247c; -.
DR eggNOG; COG2161; Bacteria.
DR InParanoid; O50462; -.
DR OMA; VTTHERF; -.
DR PhylomeDB; O50462; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0097351; F:toxin sequestering activity; IPI:MTBBASE.
DR GO; GO:0045927; P:positive regulation of growth; 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 DNA-binding; Reference proteome; Repressor; Toxin-antitoxin system;
KW Transcription; Transcription regulation.
FT CHAIN 1..89
FT /note="Antitoxin RelB"
FT /id="PRO_0000406201"
SQ SEQUENCE 89 AA; 9767 MW; 579ABC9A1A59045B CRC64;
MAVVPLGEVR NRLSEYVAEV ELTHERITIT RHGHPAAVLI SADDLASIEE TLEVLRTPGA
SEAIREGLAD VAAGRFVSND EIRNRYTAR
