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Protein

Antitoxin RnlB

Gene

rnlB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Antitoxin component of a toxin-antitoxin (TA) module. A labile antitoxin (half-life of 2.1 minutes) that inhibits the endonuclease activity of cognate toxin RnlA but not that of non-cognate toxin LsoA.2 Publications

GO - Biological processi

  • negative regulation of endoribonuclease activity Source: EcoCyc
Complete GO annotation...

Enzyme and pathway databases

BioCyciEcoCyc:G7366-MONOMER.
ECOL316407:JW5418-MONOMER.
MetaCyc:G7366-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Antitoxin RnlB
Gene namesi
Name:rnlB
Synonyms:yfjO
Ordered Locus Names:b2631, JW5418
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13201. rnlB.

Pathology & Biotechi

Disruption phenotypei

Essential, it cannot be deleted unless rnlA is also disrupted.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 123123Antitoxin RnlBPRO_0000169280Add
BLAST

Post-translational modificationi

Probably degraded by CplXP and Lon proteases.

Proteomic databases

PaxDbiP52130.

Expressioni

Inductioni

Not repressed by IscR. rnlA-rnlB forms an operon, the downstream rnlB also has its own promoter.1 Publication

Interactioni

Subunit structurei

Can form a complex with cognate toxin RnlA.

Protein-protein interaction databases

BioGridi4261565. 15 interactions.
STRINGi511145.b2631.

Structurei

3D structure databases

ProteinModelPortaliP52130.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4106BHJ. Bacteria.
ENOG410Y1RN. LUCA.
OMAiCSNGFEW.
OrthoDBiEOG64BQ7W.

Family and domain databases

InterProiIPR031834. RnlB/LsoB_antitoxin.
[Graphical view]
PfamiPF15933. RnlB_antitoxin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52130-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFEITGINVS GALKAVVMAT GFENPLSSVN EIETKLSALL GSETTGEILF
60 70 80 90 100
DLLCANGPEW NRFVTLEMKY GRIMLDTAKI IDEQDVPTHI LSKLTFTLRN
110 120
HPEYLEASVL SPDDVRQVLS MDF
Length:123
Mass (Da):13,665
Last modified:December 1, 2000 - v2
Checksum:i721D9EDE233E8D12
GO

Sequence cautioni

The sequence AAA79800.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36840 Genomic DNA. Translation: AAA79800.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75679.2.
AP009048 Genomic DNA. Translation: BAE76766.1.
PIRiT08643.
RefSeqiNP_417120.2. NC_000913.3.
WP_000461704.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75679; AAC75679; b2631.
BAE76766; BAE76766; BAE76766.
GeneIDi947113.
KEGGiecj:JW5418.
eco:b2631.
PATRICi32120653. VBIEscCol129921_2725.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36840 Genomic DNA. Translation: AAA79800.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75679.2.
AP009048 Genomic DNA. Translation: BAE76766.1.
PIRiT08643.
RefSeqiNP_417120.2. NC_000913.3.
WP_000461704.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP52130.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261565. 15 interactions.
STRINGi511145.b2631.

Proteomic databases

PaxDbiP52130.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75679; AAC75679; b2631.
BAE76766; BAE76766; BAE76766.
GeneIDi947113.
KEGGiecj:JW5418.
eco:b2631.
PATRICi32120653. VBIEscCol129921_2725.

Organism-specific databases

EchoBASEiEB2993.
EcoGeneiEG13201. rnlB.

Phylogenomic databases

eggNOGiENOG4106BHJ. Bacteria.
ENOG410Y1RN. LUCA.
OMAiCSNGFEW.
OrthoDBiEOG64BQ7W.

Enzyme and pathway databases

BioCyciEcoCyc:G7366-MONOMER.
ECOL316407:JW5418-MONOMER.
MetaCyc:G7366-MONOMER.

Miscellaneous databases

PROiP52130.

Family and domain databases

InterProiIPR031834. RnlB/LsoB_antitoxin.
[Graphical view]
PfamiPF15933. RnlB_antitoxin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "IscR regulates RNase LS activity by repressing rnlA transcription."
    Otsuka Y., Miki K., Koga M., Katayama N., Morimoto W., Takahashi Y., Yonesaki T.
    Genetics 185:823-830(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: K12.
  4. "Escherichia coli rnlA and rnlB compose a novel toxin-antitoxin system."
    Koga M., Otsuka Y., Lemire S., Yonesaki T.
    Genetics 187:123-130(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ANTITOXIN, INTERACTION WITH RNLA, PROBABLE CLEAVAGE BY LON AND CPLXP PROTEASES, DISRUPTION PHENOTYPE.
    Strain: K12.
  5. "Dmd of bacteriophage T4 functions as an antitoxin against Escherichia coli LsoA and RnlA toxins."
    Otsuka Y., Yonesaki T.
    Mol. Microbiol. 83:669-681(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ANTITOXIN.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiRNLB_ECOLI
AccessioniPrimary (citable) accession number: P52130
Secondary accession number(s): Q2MAE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 1, 2000
Last modified: January 20, 2016
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.