RELJ_MYCTU
ID RELJ_MYCTU Reviewed; 91 AA.
AC P9WF25; L0TCA7; O50386; P65067;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Antitoxin RelJ;
DE AltName: Full=Antitoxin YefM;
GN Name=relJ; Synonyms=relB3, yefM; OrderedLocusNames=Rv3357;
GN ORFNames=MTV004.14;
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 FUNCTION AS AN ANTITOXIN, FUNCTION AS A TRANSCRIPTIONAL REGULATOR,
RP EXPRESSION IN 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 [3]
RP EXPRESSION IN M.SMEGMATIS, AND LACK OF 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 [4]
RP FUNCTION AS AN ANTITOXIN, SUBUNIT, AND DNA-BINDING.
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 [5]
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 [6]
RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS), SUBUNIT, AND FUNCTION AS AN
RP ANTITOXIN IN E.COLI.
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).
CC -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC A probable antitoxin for the putative mRNA interferase RelK. Upon
CC expression in E.coli but not in M.smegmatis this protein neutralizes
CC E.coli YoeB.
CC -!- FUNCTION: Binds to and represses its own promoter, in combination with
CC RelK repression is somewhat lessened. Several DNA-protein complexes are
CC formed in vitro depending on the RelJ:RelK ratio.
CC -!- SUBUNIT: Homodimer (Probable). May form RelJ(2)-RelK toxin-antitoxin
CC complexes, in which the toxin is probably inactive.
CC {ECO:0000269|PubMed:18793646, ECO:0000269|PubMed:20498855,
CC ECO:0000305}.
CC -!- INTERACTION:
CC P9WF25; P9WF09: relK; NbExp=4; IntAct=EBI-9354099, EBI-10091663;
CC P9WF25; I6Y1Q2: sirR; NbExp=3; IntAct=EBI-9354099, EBI-10091643;
CC -!- INDUCTION: Expressed in log phase cells. A member of the relJK operon.
CC {ECO:0000269|PubMed:19114484}.
CC -!- SIMILARITY: Belongs to the phD/YefM antitoxin family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46178.1; -; Genomic_DNA.
DR PIR; D70970; D70970.
DR RefSeq; NP_217874.1; NC_000962.3.
DR RefSeq; WP_003417757.1; NZ_NVQJ01000052.1.
DR PDB; 3CTO; X-ray; 2.50 A; A/B/C/D/E=1-91.
DR PDB; 3D55; X-ray; 2.13 A; A/B/C/D=1-91.
DR PDB; 3OEI; X-ray; 2.14 A; A/B/E/F/I/J/M/N=1-91.
DR PDBsum; 3CTO; -.
DR PDBsum; 3D55; -.
DR PDBsum; 3OEI; -.
DR AlphaFoldDB; P9WF25; -.
DR SMR; P9WF25; -.
DR IntAct; P9WF25; 2.
DR MINT; P9WF25; -.
DR STRING; 83332.Rv3357; -.
DR PaxDb; P9WF25; -.
DR DNASU; 888135; -.
DR GeneID; 45427356; -.
DR GeneID; 888135; -.
DR KEGG; mtu:Rv3357; -.
DR TubercuList; Rv3357; -.
DR eggNOG; COG2161; Bacteria.
DR OMA; SIMETNY; -.
DR PhylomeDB; P9WF25; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA: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 3D-structure; DNA-binding; Reference proteome; Repressor;
KW Toxin-antitoxin system; Transcription; Transcription regulation.
FT CHAIN 1..91
FT /note="Antitoxin RelJ"
FT /id="PRO_0000213742"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:3D55"
FT HELIX 5..10
FT /evidence="ECO:0007829|PDB:3D55"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:3D55"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:3D55"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3D55"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:3D55"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:3D55"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:3D55"
SQ SEQUENCE 91 AA; 10194 MW; 5A4140972F329F0A CRC64;
MSISASEARQ RLFPLIEQVN TDHQPVRITS RAGDAVLMSA DDYDAWQETV YLLRSPENAR
RLMEAVARDK AGHSAFTKSV DELREMAGGE E
