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Protein

mRNA endoribonuclease LS

Gene

rnlA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Toxic component of a toxin-antitoxin (TA) module. A stable (half-life 27.6 minutes) endoribonuclease that in the absence of cognate antitoxin RnlB causes generalized RNA degradation. Degrades late enterobacteria phage T4 mRNAs, protecting the host against T4 reproduction. Activity is inhibited by cognate antitoxin RnlB and by enterobacteria phage T4 protein Dmd. Targets cyaA mRNA.4 Publications

GO - Molecular functioni

  • endoribonuclease activity Source: EcoCyc

GO - Biological processi

  • mRNA catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease, Toxin

Enzyme and pathway databases

BioCyciEcoCyc:G7365-MONOMER.
ECOL316407:JW2611-MONOMER.
MetaCyc:G7365-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA endoribonuclease LS (EC:3.1.-.-)
Alternative name(s):
RNase LS
Toxin LS
Gene namesi
Name:rnlA
Synonyms:std, yfjN
Ordered Locus Names:b2630, JW2611
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13200. rnlA.

Pathology & Biotechi

Disruption phenotypei

Not essential, slightly smaller colonies on minimal agar plates at 30 degrees Celsius. Strongly reduces RNase LS activity, restores growth of an enterobacteria phage T4 dmd mutant. Altered mRNA half-life for some cellular transcripts, including an increased half-life for an internal fragment of 23S rRNA. Allele rnlA2 is due to a premature stop codon at residue 33 (PubMed:15677746). Sensitive to high concentrations of NaCl, sensitivity is eliminated in a crp or cyaA deletion mutant. Increased levels of Crp and thus increased levels of cAMP.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi188 – 1969EKVLIRQED → KKVLIRQEN in rnlA5; strongly reduces RNase LS activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 357357mRNA endoribonuclease LSPRO_0000169279Add
BLAST

Proteomic databases

PaxDbiP52129.

Expressioni

Inductioni

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 antitoxin RnlB and with enterobacteria phage T4 antitoxin Dmd.

Protein-protein interaction databases

BioGridi4259437. 12 interactions.
DIPiDIP-12079N.
IntActiP52129. 2 interactions.
MINTiMINT-1290895.
STRINGi511145.b2630.

Structurei

Secondary structure

1
357
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93Combined sources
Helixi13 – 153Combined sources
Helixi16 – 2611Combined sources
Beta strandi30 – 356Combined sources
Beta strandi43 – 497Combined sources
Beta strandi56 – 627Combined sources
Beta strandi68 – 714Combined sources
Beta strandi73 – 764Combined sources
Helixi78 – 9013Combined sources
Helixi94 – 974Combined sources
Beta strandi100 – 1045Combined sources
Helixi109 – 11911Combined sources
Beta strandi126 – 1327Combined sources
Beta strandi134 – 14310Combined sources
Turni144 – 1474Combined sources
Beta strandi148 – 1558Combined sources
Turni156 – 1594Combined sources
Beta strandi160 – 1656Combined sources
Helixi169 – 17810Combined sources
Helixi179 – 1813Combined sources
Helixi184 – 1929Combined sources
Helixi199 – 2013Combined sources
Helixi204 – 21512Combined sources
Helixi216 – 2216Combined sources
Helixi224 – 23815Combined sources
Helixi247 – 2504Combined sources
Helixi251 – 26616Combined sources
Turni267 – 2693Combined sources
Turni274 – 2763Combined sources
Helixi279 – 2813Combined sources
Beta strandi286 – 2883Combined sources
Helixi293 – 2964Combined sources
Helixi301 – 32222Combined sources
Helixi336 – 35520Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4I8OX-ray2.10A/B1-357[»]
ProteinModelPortaliP52129.
SMRiP52129. Positions 4-356.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4106K8T. Bacteria.
ENOG410YAX4. LUCA.
HOGENOMiHOG000012167.
OMAiCYRAFIF.

Family and domain databases

InterProiIPR031845. RnlA_toxin.
[Graphical view]
PfamiPF15935. RnlA_toxin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52129-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIRSYKNLN LVRANIETES RQFIENKNYS IQSIGPMPGS RAGLRVVFTR
60 70 80 90 100
PGVNLATVDI FYNGDGSTTI QYLTGANRSL GQELADHLFE TINPAEFEQV
110 120 130 140 150
NMVLQGFVET SVLPVLELSA DESHIEFREH SRNAHTVVWK IISTSYQDEL
160 170 180 190 200
TVSLHITTGK LQIQGRPLSC YRVFTFNLAA LLDLQGLEKV LIRQEDGKAN
210 220 230 240 250
IVQQEVARTY LQTVMADAYP HLHVTAEKLL VSGLCVKLAA PDLPDYCMLL
260 270 280 290 300
YPELRTIEGV LKSKMSGLGM PVQQPAGFGT YFDKPAAHYI LKPQFAATLR
310 320 330 340 350
PEQINIISTA YTFFNVERHS LFHMETVVDA SRMISDMARL MGKATRAWGI

IKDLYIV
Length:357
Mass (Da):40,061
Last modified:November 1, 1997 - v2
Checksum:i78FB0506AC9AE45A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36840 Genomic DNA. Translation: AAA79799.1.
U00096 Genomic DNA. Translation: AAC75678.1.
AP009048 Genomic DNA. Translation: BAE76765.1.
PIRiH65041.
RefSeqiNP_417119.1. NC_000913.3.
WP_000155570.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75678; AAC75678; b2630.
BAE76765; BAE76765; BAE76765.
GeneIDi947107.
KEGGiecj:JW2611.
eco:b2630.
PATRICi32120651. VBIEscCol129921_2724.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36840 Genomic DNA. Translation: AAA79799.1.
U00096 Genomic DNA. Translation: AAC75678.1.
AP009048 Genomic DNA. Translation: BAE76765.1.
PIRiH65041.
RefSeqiNP_417119.1. NC_000913.3.
WP_000155570.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4I8OX-ray2.10A/B1-357[»]
ProteinModelPortaliP52129.
SMRiP52129. Positions 4-356.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259437. 12 interactions.
DIPiDIP-12079N.
IntActiP52129. 2 interactions.
MINTiMINT-1290895.
STRINGi511145.b2630.

Proteomic databases

PaxDbiP52129.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75678; AAC75678; b2630.
BAE76765; BAE76765; BAE76765.
GeneIDi947107.
KEGGiecj:JW2611.
eco:b2630.
PATRICi32120651. VBIEscCol129921_2724.

Organism-specific databases

EchoBASEiEB2992.
EcoGeneiEG13200. rnlA.

Phylogenomic databases

eggNOGiENOG4106K8T. Bacteria.
ENOG410YAX4. LUCA.
HOGENOMiHOG000012167.
OMAiCYRAFIF.

Enzyme and pathway databases

BioCyciEcoCyc:G7365-MONOMER.
ECOL316407:JW2611-MONOMER.
MetaCyc:G7365-MONOMER.

Miscellaneous databases

PROiP52129.

Family and domain databases

InterProiIPR031845. RnlA_toxin.
[Graphical view]
PfamiPF15935. RnlA_toxin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRNLA_ECOLI
AccessioniPrimary (citable) accession number: P52129
Secondary accession number(s): P76604, Q2MAE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 101 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.