RNLB_ECOLI
ID RNLB_ECOLI Reviewed; 123 AA.
AC P52130; Q2MAE0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Antitoxin RnlB;
GN Name=rnlB; Synonyms=yfjO; OrderedLocusNames=b2631, JW5418;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=20421606; DOI=10.1534/genetics.110.114462;
RA Otsuka Y., Miki K., Koga M., Katayama N., Morimoto W., Takahashi Y.,
RA Yonesaki T.;
RT "IscR regulates RNase LS activity by repressing rnlA transcription.";
RL Genetics 185:823-830(2010).
RN [4]
RP FUNCTION AS AN ANTITOXIN, INTERACTION WITH RNLA, PROBABLE CLEAVAGE BY LON
RP AND CPLXP PROTEASES, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=20980243; DOI=10.1534/genetics.110.121798;
RA Koga M., Otsuka Y., Lemire S., Yonesaki T.;
RT "Escherichia coli rnlA and rnlB compose a novel toxin-antitoxin system.";
RL Genetics 187:123-130(2011).
RN [5]
RP FUNCTION AS AN ANTITOXIN.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=22403819; DOI=10.1111/j.1365-2958.2012.07975.x;
RA Otsuka Y., Yonesaki T.;
RT "Dmd of bacteriophage T4 functions as an antitoxin against Escherichia coli
RT LsoA and RnlA toxins.";
RL Mol. Microbiol. 83:669-681(2012).
CC -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC A labile antitoxin (half-life of 2.1 minutes) that inhibits the
CC endonuclease activity of cognate toxin RnlA but not that of non-cognate
CC toxin LsoA. {ECO:0000269|PubMed:20980243, ECO:0000269|PubMed:22403819}.
CC -!- SUBUNIT: Can form a complex with cognate toxin RnlA.
CC -!- INTERACTION:
CC P52130; P52129: rnlA; NbExp=2; IntAct=EBI-21183386, EBI-560462;
CC -!- INDUCTION: Not repressed by IscR. rnlA-rnlB forms an operon, the
CC downstream rnlB also has its own promoter.
CC {ECO:0000269|PubMed:20421606}.
CC -!- PTM: Probably degraded by CplXP and Lon proteases.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted unless rnlA is
CC also disrupted. {ECO:0000269|PubMed:20980243}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA79800.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U36840; AAA79800.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75679.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76766.1; -; Genomic_DNA.
DR PIR; T08643; T08643.
DR RefSeq; NP_417120.2; NC_000913.3.
DR RefSeq; WP_000461704.1; NZ_LN832404.1.
DR PDB; 6Y2P; X-ray; 2.64 A; C/D=1-123.
DR PDBsum; 6Y2P; -.
DR AlphaFoldDB; P52130; -.
DR SASBDB; P52130; -.
DR SMR; P52130; -.
DR BioGRID; 4261565; 15.
DR ComplexPortal; CPX-4115; RnlAB toxin-antitoxin complex.
DR IntAct; P52130; 1.
DR STRING; 511145.b2631; -.
DR PaxDb; P52130; -.
DR PRIDE; P52130; -.
DR EnsemblBacteria; AAC75679; AAC75679; b2631.
DR EnsemblBacteria; BAE76766; BAE76766; BAE76766.
DR GeneID; 947113; -.
DR KEGG; ecj:JW5418; -.
DR KEGG; eco:b2631; -.
DR PATRIC; fig|511145.12.peg.2725; -.
DR EchoBASE; EB2993; -.
DR eggNOG; ENOG50331J3; Bacteria.
DR HOGENOM; CLU_163902_1_0_6; -.
DR OMA; CSNGFEW; -.
DR BioCyc; EcoCyc:G7366-MON; -.
DR BioCyc; MetaCyc:G7366-MON; -.
DR PRO; PR:P52130; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0110001; C:toxin-antitoxin complex; IPI:ComplexPortal.
DR GO; GO:0060702; P:negative regulation of endoribonuclease activity; IMP:EcoCyc.
DR GO; GO:0040008; P:regulation of growth; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0044010; P:single-species biofilm formation; IC:ComplexPortal.
DR InterPro; IPR031834; RnlB/LsoB_antitoxin.
DR Pfam; PF15933; RnlB_antitoxin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..123
FT /note="Antitoxin RnlB"
FT /id="PRO_0000169280"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6Y2P"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:6Y2P"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6Y2P"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:6Y2P"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:6Y2P"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:6Y2P"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:6Y2P"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:6Y2P"
FT STRAND 72..81
FT /evidence="ECO:0007829|PDB:6Y2P"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6Y2P"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:6Y2P"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:6Y2P"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:6Y2P"
SQ SEQUENCE 123 AA; 13665 MW; 721D9EDE233E8D12 CRC64;
MFEITGINVS GALKAVVMAT GFENPLSSVN EIETKLSALL GSETTGEILF DLLCANGPEW
NRFVTLEMKY GRIMLDTAKI IDEQDVPTHI LSKLTFTLRN HPEYLEASVL SPDDVRQVLS
MDF
