RALR_ECOLI
ID RALR_ECOLI Reviewed; 64 AA.
AC P33229;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Endodeoxyribonuclease toxin RalR {ECO:0000303|PubMed:24748661};
DE Short=DNase RalR {ECO:0000303|PubMed:24748661};
DE EC=3.1.-.-;
DE AltName: Full=Restriction alleviation and modification enhancement protein {ECO:0000303|PubMed:7476171};
DE AltName: Full=Toxin RalR {ECO:0000303|PubMed:24748661};
GN Name=ralR; Synonyms=lar {ECO:0000303|PubMed:7476171}, ral, ydaB;
GN OrderedLocusNames=b1348, JW5208;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8244937; DOI=10.1128/jb.175.23.7673-7682.1993;
RA Clark A.J., Sharma V., Brenowitz S., Chu C.C., Sandler S.J., Satin L.,
RA Templin A., Berger I., Cohen A.;
RT "Genetic and molecular analyses of the C-terminal region of the recE gene
RT from the Rac prophage of Escherichia coli K-12 reveal the recT gene.";
RL J. Bacteriol. 175:7673-7682(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION.
RX PubMed=7476171; DOI=10.1111/j.1365-2958.1995.tb02438.x;
RA King G., Murray N.E.;
RT "Restriction alleviation and modification enhancement by the Rac prophage
RT of Escherichia coli K-12.";
RL Mol. Microbiol. 16:769-777(1995).
RN [6]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, INDUCTION, DISRUPTION PHENOTYPE,
RP ANTIBIOTIC RESISTANCE, AND MUTAGENESIS OF LYS-52 AND 43-GLU--ALA-46.
RC STRAIN=K12 / BW25113;
RX PubMed=24748661; DOI=10.1093/nar/gku279;
RA Guo Y., Quiroga C., Chen Q., McAnulty M.J., Benedik M.J., Wood T.K.,
RA Wang X.;
RT "RalR (a DNase) and RalA (a small RNA) form a type I toxin-antitoxin system
RT in Escherichia coli.";
RL Nucleic Acids Res. 42:6448-6462(2014).
CC -!- FUNCTION: Toxic component of a type I toxin-antitoxin (TA) system. Upon
CC overexpression inhibits growth and reduces colony-forming units in both
CC the presence and absence of the Rac prophage, cells become filamentous.
CC Has deoxyribonuclease activity (probably endonucleolytic), does not
CC digest RNA. Its toxic effects are neutralized by sRNA antitoxin RalA,
CC which is encoded in trans on the opposite DNA strand (PubMed:24748661).
CC Has RAL-like activity (PubMed:7476171). {ECO:0000269|PubMed:24748661,
CC ECO:0000269|PubMed:7476171}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:24748661};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24748661};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:24748661}.
CC -!- INDUCTION: The sRNA antitoxin RalA probably works by inhibiting
CC translation of the RalR mRNA. The ability of RalA to block the toxicity
CC of RalR relies on a 16-nt sequence which is complementary to a section
CC of the RalR coding region; in the presence of RalA sRNA decreased
CC amounts of RalR protein accumulate with no significant changes in the
CC level of RalR RNA. {ECO:0000269|PubMed:24748661}.
CC -!- DISRUPTION PHENOTYPE: The single ralR and double ralR-ralA mutant have
CC increased sensitivity to the antibiotic fosfomycin.
CC {ECO:0000269|PubMed:24748661}.
CC -!- MISCELLANEOUS: This protein is encoded on the Rac prophage.
CC {ECO:0000303|PubMed:8244937}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16180.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L23927; AAA16180.1; ALT_INIT; Unassigned_DNA.
DR EMBL; U00096; AAC74430.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14948.1; -; Genomic_DNA.
DR PIR; G64884; G64884.
DR RefSeq; NP_415864.1; NC_000913.3.
DR RefSeq; WP_001317028.1; NZ_SSUR01000011.1.
DR AlphaFoldDB; P33229; -.
DR SMR; P33229; -.
DR BioGRID; 4261586; 121.
DR STRING; 511145.b1348; -.
DR PaxDb; P33229; -.
DR PRIDE; P33229; -.
DR EnsemblBacteria; AAC74430; AAC74430; b1348.
DR EnsemblBacteria; BAA14948; BAA14948; BAA14948.
DR GeneID; 66674824; -.
DR GeneID; 945914; -.
DR KEGG; ecj:JW5208; -.
DR KEGG; eco:b1348; -.
DR PATRIC; fig|83333.113.peg.1370; -.
DR EchoBASE; EB1845; -.
DR eggNOG; ENOG50349DV; Bacteria.
DR HOGENOM; CLU_207096_0_0_6; -.
DR OMA; KIMRYDN; -.
DR BioCyc; EcoCyc:EG11900-MON; -.
DR BioCyc; MetaCyc:EG11900-MON; -.
DR PRO; PR:P33229; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990238; F:double-stranded DNA endodeoxyribonuclease activity; IDA:EcoCyc.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR019908; Toxin_RalR.
DR TIGRFAMs; TIGR03655; anti_R_Lar; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Calcium; Endonuclease; Hydrolase; Magnesium;
KW Nuclease; Reference proteome; Restriction system; Toxin-antitoxin system.
FT CHAIN 1..64
FT /note="Endodeoxyribonuclease toxin RalR"
FT /id="PRO_0000084360"
FT MUTAGEN 43..46
FT /note="EKEA->AIAE: No longer inhibits growth."
FT /evidence="ECO:0000269|PubMed:24748661"
FT MUTAGEN 52
FT /note="K->E: No longer inhibits growth, has no DNase
FT activity."
FT /evidence="ECO:0000269|PubMed:24748661"
SQ SEQUENCE 64 AA; 7019 MW; 0D84834187B22F59 CRC64;
MRYDNVKPCP FCGCPSVTVK AISGYYRAKC NGCESRTGYG GSEKEALERW NKRTTGNNNG
GVHV
