RELK_MYCTU
ID RELK_MYCTU Reviewed; 85 AA.
AC P9WF09; L0TCJ4; O50387; P64528;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Toxin RelK;
DE EC=3.1.-.-;
DE AltName: Full=Endoribonuclease YoeB;
DE AltName: Full=Putative mRNA interferase RelE3;
DE AltName: Full=Putative mRNA interferase YoeB;
DE AltName: Full=Toxin YoeB;
GN Name=relK; Synonyms=relE3, yoeB; OrderedLocusNames=Rv3358;
GN ORFNames=MTV004.15;
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 SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18793646; DOI=10.1016/j.jmb.2008.08.067;
RA Kumar P., Issac B., Dodson E.J., Turkenburg J.P., Mande S.C.;
RT "Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals
RT that it is not an intrinsically unstructured protein.";
RL J. Mol. Biol. 383:482-493(2008).
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).
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 antitoxin RelJ (shown only for M.smegmatis). Overexpression also
CC increases the number of rifampcin-tolerant persister cells.
CC {ECO:0000250, ECO:0000269|PubMed:19114484, ECO:0000269|PubMed:20011113,
CC ECO:0000269|PubMed:20061486, ECO:0000269|PubMed:20498855}.
CC -!- FUNCTION: In combination with RelJ represses its own promoter. Several
CC DNA-protein complexes are formed in vitro depending on the RelJ:RelK
CC ratio.
CC -!- SUBUNIT: Forms a toxin-antitoxin complex with RelJ, perhaps RelJ(2)-
CC RelK, in which the toxin is probably inactive. Also interacts with
CC antitoxins RelB and RelF in vitro, in M.smegmatis coexpression with
CC non-cognate antitoxin RelB increases the toxicity of RelK while little
CC change is seen in the RelFK pair. {ECO:0000269|PubMed:18793646,
CC ECO:0000269|PubMed:20498855}.
CC -!- INTERACTION:
CC P9WF09; P9WF25: relJ; NbExp=4; IntAct=EBI-10091663, EBI-9354099;
CC P9WF09; I6Y1Q2: sirR; NbExp=3; IntAct=EBI-10091663, EBI-10091643;
CC -!- INDUCTION: Expressed in log phase cells. Induced by treatment with
CC rifampicin and gentamicin as well as by nitrosative and oxidative
CC stress. Expressed in human macrophages 110 hours after infection.
CC Induced in the lungs of mice infected for 4 weeks. A member of the
CC relJK 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 following
CC exposure to gentamicin, levofloxacin and isoniazid.
CC {ECO:0000269|PubMed:20061486}.
CC -!- SIMILARITY: Belongs to the YoeB family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46179.1; -; Genomic_DNA.
DR PIR; E70970; E70970.
DR RefSeq; NP_217875.1; NC_000962.3.
DR RefSeq; WP_003417760.1; NZ_NVQJ01000052.1.
DR PDB; 3OEI; X-ray; 2.14 A; C/D/G/H/K/L/O/P=2-85.
DR PDBsum; 3OEI; -.
DR AlphaFoldDB; P9WF09; -.
DR SMR; P9WF09; -.
DR IntAct; P9WF09; 2.
DR MINT; P9WF09; -.
DR STRING; 83332.Rv3358; -.
DR PaxDb; P9WF09; -.
DR DNASU; 888139; -.
DR GeneID; 45427357; -.
DR GeneID; 888139; -.
DR KEGG; mtu:Rv3358; -.
DR TubercuList; Rv3358; -.
DR eggNOG; COG4115; Bacteria.
DR OMA; KCRFHYD; -.
DR PhylomeDB; P9WF09; -.
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:0016892; F:endoribonuclease activity, producing 3'-phosphomonoesters; IBA:GO_Central.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:1903507; P:negative regulation of nucleic acid-templated transcription; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MTBBASE.
DR GO; GO:0045947; P:negative regulation of translational initiation; IBA:GO_Central.
DR GO; GO:0006401; P:RNA catabolic process; IDA:MTBBASE.
DR Gene3D; 3.30.2310.20; -; 1.
DR InterPro; IPR035093; RelE/ParE_toxin_dom_sf.
DR InterPro; IPR009614; YoeB_toxin.
DR PANTHER; PTHR38039; PTHR38039; 1.
DR Pfam; PF06769; YoeB_toxin; 1.
DR SUPFAM; SSF143011; SSF143011; 1.
DR TIGRFAMs; TIGR02116; toxin_Txe_YoeB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW Reference proteome; Repressor; Toxin-antitoxin system; Transcription;
KW Transcription regulation.
FT CHAIN 1..85
FT /note="Toxin RelK"
FT /id="PRO_0000216213"
FT ACT_SITE 47
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 84
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:3OEI"
FT HELIX 8..20
FT /evidence="ECO:0007829|PDB:3OEI"
FT HELIX 22..37
FT /evidence="ECO:0007829|PDB:3OEI"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3OEI"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:3OEI"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:3OEI"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:3OEI"
SQ SEQUENCE 85 AA; 10102 MW; 8663A289B5FD9DAF CRC64;
MRSVNFDPDA WEDFLFWLAA DRKTARRITR LIGEIQRDPF SGIGKPEPLQ GELSGYWSRR
IDDEHRLVYR AGDDEVTMLK ARYHY
