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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi188 – 196EKVLIRQED → KKVLIRQEN in rnlA5; strongly reduces RNase LS activity. 1 Publication9

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001692791 – 357mRNA endoribonuclease LSAdd BLAST357

Proteomic databases

PaxDbiP52129.
PRIDEiP52129.

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 interactors.
DIPiDIP-12079N.
IntActiP52129. 2 interactors.
MINTiMINT-1290895.
STRINGi511145.b2630.

Structurei

Secondary structure

1357
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 9Combined sources3
Helixi13 – 15Combined sources3
Helixi16 – 26Combined sources11
Beta strandi30 – 35Combined sources6
Beta strandi43 – 49Combined sources7
Beta strandi56 – 62Combined sources7
Beta strandi68 – 71Combined sources4
Beta strandi73 – 76Combined sources4
Helixi78 – 90Combined sources13
Helixi94 – 97Combined sources4
Beta strandi100 – 104Combined sources5
Helixi109 – 119Combined sources11
Beta strandi126 – 132Combined sources7
Beta strandi134 – 143Combined sources10
Turni144 – 147Combined sources4
Beta strandi148 – 155Combined sources8
Turni156 – 159Combined sources4
Beta strandi160 – 165Combined sources6
Helixi169 – 178Combined sources10
Helixi179 – 181Combined sources3
Helixi184 – 192Combined sources9
Helixi199 – 201Combined sources3
Helixi204 – 215Combined sources12
Helixi216 – 221Combined sources6
Helixi224 – 238Combined sources15
Helixi247 – 250Combined sources4
Helixi251 – 266Combined sources16
Turni267 – 269Combined sources3
Turni274 – 276Combined sources3
Helixi279 – 281Combined sources3
Beta strandi286 – 288Combined sources3
Helixi293 – 296Combined sources4
Helixi301 – 322Combined sources22
Helixi336 – 355Combined sources20

3D structure databases

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

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP52129.
PRIDEiP52129.

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: November 2, 2016
This is version 103 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.