RELF_MYCTU
ID RELF_MYCTU Reviewed; 93 AA.
AC O33347; L0TDS8;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Antitoxin RelF;
GN Name=relF; Synonyms=relB2; OrderedLocusNames=Rv2865;
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 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 INTERACTION WITH RELE.
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 X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
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: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC Upon expression in M.smegmatis neutralizes the effect of toxin RelE2.
CC -!- FUNCTION: Induces its own promoter, in combination with RelG represses
CC its own promoter. Has been seen to bind DNA in complex with toxin RelG
CC but not alone.
CC -!- SUBUNIT: Interacts with toxin RelG, which neutralizes the toxin. Also
CC interacts with toxins RelE and RelK in vitro, in M.smegmatis
CC coexpression with non-cognate toxins increases the toxicity of RelE but
CC not of RelK. {ECO:0000269|PubMed:20498855}.
CC -!- INDUCTION: Expressed in log phase cells. Also expressed in human
CC macrophages 110 hours after infection. A member of the relFG operon.
CC {ECO:0000269|PubMed:19114484}.
CC -!- SIMILARITY: Belongs to the phD/YefM antitoxin family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45667.1; -; Genomic_DNA.
DR PIR; C70886; C70886.
DR RefSeq; NP_217381.1; NC_000962.3.
DR RefSeq; WP_003414599.1; NZ_NVQJ01000006.1.
DR PDB; 3G5O; X-ray; 2.00 A; A/D=1-93.
DR PDBsum; 3G5O; -.
DR AlphaFoldDB; O33347; -.
DR SMR; O33347; -.
DR DIP; DIP-60144N; -.
DR IntAct; O33347; 1.
DR STRING; 83332.Rv2865; -.
DR PaxDb; O33347; -.
DR DNASU; 887458; -.
DR GeneID; 887458; -.
DR KEGG; mtu:Rv2865; -.
DR TubercuList; Rv2865; -.
DR eggNOG; COG2161; Bacteria.
DR InParanoid; O33347; -.
DR OMA; DEVAGTH; -.
DR PhylomeDB; O33347; -.
DR EvolutionaryTrace; O33347; -.
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 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..93
FT /note="Antitoxin RelF"
FT /id="PRO_0000406202"
FT STRAND 1..5
FT /evidence="ECO:0007829|PDB:3G5O"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:3G5O"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:3G5O"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:3G5O"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:3G5O"
FT HELIX 42..55
FT /evidence="ECO:0007829|PDB:3G5O"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:3G5O"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:3G5O"
SQ SEQUENCE 93 AA; 10183 MW; 07F97E029D3B537A CRC64;
MRILPISTIK GKLNEFVDAV SSTQDQITIT KNGAPAAVLV GADEWESLQE TLYWLAQPGI
RESIAEADAD IASGRTYGED EIRAEFGVPR RPH
