ID   RELE_MYCTU              Reviewed;          97 AA.
AC   O50461; L0T6B0;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Toxin RelE;
DE            EC=3.1.-.-;
DE   AltName: Full=Putative endoribonuclease RelE;
GN   Name=relE; Synonyms=relE1; OrderedLocusNames=Rv1246c;
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   FUNCTION AS A TOXIN, FUNCTION AS A TRANSCRIPTIONAL REGULATOR, EXPRESSION IN
RP   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 A TOXIN.
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 IN M.TUBERCULOSIS, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX   PubMed=20061486; DOI=10.1128/jb.01285-09;
RA   Singh R., Barry C.E. III, Boshoff H.I.;
RT   "The three RelE homologs of Mycobacterium tuberculosis have individual,
RT   drug-specific effects on bacterial antibiotic tolerance.";
RL   J. Bacteriol. 192:1279-1291(2010).
RN   [6]
RP   FUNCTION AS A TOXIN, SUBUNIT, AND INTERACTION WITH RELF.
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   [7]
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: Toxic component of a type II toxin-antitoxin (TA) system. Has
CC       RNase activity (By similarity). Overexpression in M.tuberculosis or
CC       M.smegmatis inhibits colony formation in a bacteriostatic rather than
CC       bacteriocidal fashion. Its toxic effect is neutralized by coexpression
CC       with cognate antitoxin RelB (shown only for M.smegmatis). {ECO:0000250,
CC       ECO:0000269|PubMed:19114484, ECO:0000269|PubMed:20011113,
CC       ECO:0000269|PubMed:20061486, ECO:0000269|PubMed:20498855}.
CC   -!- FUNCTION: In combination with RelB represses its own promoter. Has been
CC       seen to bind DNA in complex with cognate antitoxin RelB but not alone.
CC   -!- SUBUNIT: Interacts with cognate antitoxin RelB, which neutralizes the
CC       toxin. Also interacts with non-cognate antitoxin RelF in vitro, in
CC       M.smegmatis coexpression of these 2 genes increases the toxicity of
CC       RelE. {ECO:0000269|PubMed:19114484, ECO:0000269|PubMed:20498855}.
CC   -!- INDUCTION: Expressed in log phase cells (at protein level). Induced by
CC       rifampicin treatment. Expressed in human macrophages 110 hours after
CC       infection. Induced in the lungs of mice infected for 4 weeks. A member
CC       of the relBE operon. {ECO:0000269|PubMed:19114484,
CC       ECO:0000269|PubMed:20061486}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype in culture or upon infection
CC       of mice. {ECO:0000269|PubMed:20061486}.
CC   -!- SIMILARITY: Belongs to the RelE toxin family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP44002.1; -; Genomic_DNA.
DR   PIR; E70953; E70953.
DR   RefSeq; NP_215762.1; NC_000962.3.
DR   RefSeq; WP_003898789.1; NZ_NVQJ01000049.1.
DR   AlphaFoldDB; O50461; -.
DR   SMR; O50461; -.
DR   STRING; 83332.Rv1246c; -.
DR   PaxDb; O50461; -.
DR   GeneID; 45425216; -.
DR   GeneID; 887099; -.
DR   KEGG; mtu:Rv1246c; -.
DR   TubercuList; Rv1246c; -.
DR   eggNOG; COG2026; Bacteria.
DR   InParanoid; O50461; -.
DR   OMA; GEFRVIY; -.
DR   PhylomeDB; O50461; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IDA:MTBBASE.
DR   GO; GO:0045926; P:negative regulation of growth; IMP:MTBBASE.
DR   GO; GO:0006401; P:RNA catabolic process; IDA:MTBBASE.
DR   Gene3D; 3.30.2310.20; -; 1.
DR   InterPro; IPR007712; RelE/ParE_toxin.
DR   InterPro; IPR035093; RelE/ParE_toxin_dom_sf.
DR   Pfam; PF05016; ParE_toxin; 1.
DR   SUPFAM; SSF143011; SSF143011; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Hydrolase; Nuclease; Reference proteome; Repressor;
KW   Toxin-antitoxin system; Transcription; Transcription regulation.
FT   CHAIN           1..97
FT                   /note="Toxin RelE"
FT                   /id="PRO_0000406199"
SQ   SEQUENCE   97 AA;  11064 MW;  706298CC2CAB3434 CRC64;
     MSDDHPYHVA ITATAARDLQ RLPEKIAAAC VEFVFGPLLN NPHRLGKPLR NDLEGLHSAR
     RGDYRVVYAI DDGHHRVEII HIARRSASYR MNPCRPR