RELG_MYCTU
ID RELG_MYCTU Reviewed; 87 AA.
AC O33348; L0TDL2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Toxin RelG;
DE EC=3.1.-.-;
DE AltName: Full=Putative endoribonuclease RelG;
GN Name=relG; Synonyms=relE2; OrderedLocusNames=Rv2866;
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, 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, DISRUPTION PHENOTYPE, AND PUTATIVE
RP FUNCTION IN PERSISTER CELL FORMATION.
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 RELB.
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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-87.
RC STRAIN=ATCC 25618 / H37Rv;
RA Miallau L., Chernishof I., Chiang J., Arbing M., Cascio D., Eisenberg D.;
RT "The crystal structure of the toxin-antitoxin complex RelBE2 (Rv2865-2866)
RT from Mycobacterium tuberculosis.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Has
CC RNase activity and preferentially cleaves at the 3'-end of purine
CC ribonucleotides (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 RelB2 (shown only for M.smegmatis).
CC Overexpression also increases the number of gentamicin-tolerant and
CC levofloxacin-tolerant persister cells. {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 cognate antitoxin RelF represses its own
CC promoter. Has been seen to bind DNA in complex with antitoxin RelF but
CC not alone.
CC -!- SUBUNIT: Interacts with cognate antitoxin RelF, which neutralizes the
CC toxin. Also interacts with non-cognate antitoxin RelB in vitro, in
CC M.smegmatis this neutralizes the toxicity of this toxin.
CC {ECO:0000269|PubMed:20498855}.
CC -!- INDUCTION: Expressed in log phase cells. Induced by treatment with
CC rifampicin and gentamicin as well as by oxidative, nitrosative and
CC nutritional stress. Induced in the lungs of mice infected for 4 weeks.
CC A member of the relFG operon. {ECO:0000269|PubMed:19114484,
CC ECO:0000269|PubMed:20061486}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in culture or upon infection
CC of mice. Significantly fewer persister cells are generated in vitro
CC following exposure to rifampicin and gentamicin, but in infected mice
CC no differences are seen. {ECO:0000269|PubMed:20061486}.
CC -!- SIMILARITY: Belongs to the RelE toxin family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45668.1; -; Genomic_DNA.
DR PIR; D70886; D70886.
DR RefSeq; NP_217382.1; NC_000962.3.
DR RefSeq; WP_003414602.1; NZ_NVQJ01000006.1.
DR PDB; 3G5O; X-ray; 2.00 A; B/C=2-87.
DR PDBsum; 3G5O; -.
DR AlphaFoldDB; O33348; -.
DR SMR; O33348; -.
DR DIP; DIP-60145N; -.
DR IntAct; O33348; 1.
DR STRING; 83332.Rv2866; -.
DR PaxDb; O33348; -.
DR DNASU; 887450; -.
DR GeneID; 45426854; -.
DR GeneID; 887450; -.
DR KEGG; mtu:Rv2866; -.
DR TubercuList; Rv2866; -.
DR eggNOG; COG2026; Bacteria.
DR InParanoid; O33348; -.
DR OMA; EGYWSAR; -.
DR PhylomeDB; O33348; -.
DR EvolutionaryTrace; O33348; -.
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:0045892; P:negative regulation of transcription, DNA-templated; IDA: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 3D-structure; DNA-binding; Hydrolase; Nuclease; Reference proteome;
KW Repressor; Toxin-antitoxin system; Transcription; Transcription regulation.
FT CHAIN 1..87
FT /note="Toxin RelG"
FT /id="PRO_0000406200"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3G5O"
FT HELIX 9..15
FT /evidence="ECO:0007829|PDB:3G5O"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:3G5O"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:3G5O"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:3G5O"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:3G5O"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3G5O"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:3G5O"
FT STRAND 58..67
FT /evidence="ECO:0007829|PDB:3G5O"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:3G5O"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:3G5O"
SQ SEQUENCE 87 AA; 10237 MW; 26A297E3CA6C64F5 CRC64;
MPYTVRFTTT ARRDLHKLPP RILAAVVEFA FGDLSREPLR VGKPLRRELA GTFSARRGTY
RLLYRIDDEH TTVVILRVDH RADIYRR
