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Protein

Endoribonuclease EndoA

Gene

ndoA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Toxic component of a type II toxin-antitoxin (TA) module. Specific for 5'-UACAU-3' sequences, cleaving after the first U (PubMed:21763692). Yields cleavage products with 3' phosphate and 5' hydroxyl groups (PubMed:15882409). Cannot digest substrate with a UUdUACAUAA cleavage site (PubMed:24120662). Overexpression is toxic for cell growth (shown in E.coli), probably by inhibiting protein synthesis through the cleavage of single-stranded RNA. The toxicity is reversed by the antitoxin EndoAI. Toxin activity cannot be inhibited by MazE from E.coli. The EndoA-EndoAI complex does not seem to bind its own promoter (PubMed:24120662).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei25Transition state stabilizer1 Publication1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease, Toxin

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciBSUB:BSU04660-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoribonuclease EndoA1 Publication (EC:3.1.27.-1 Publication)
Alternative name(s):
Toxin EndoA
mRNA interferase EndoA
mRNA interferase MazF-bs1 Publication
Short name:
MazF-bs
Gene namesi
Name:ndoA1 Publication
Synonyms:mazF, ydcE
Ordered Locus Names:BSU04660
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi10F → A: Remains toxic in E.coli. 1 Publication1
Mutagenesisi19S → A: Partially toxic in E.coli. 1 Publication1
Mutagenesisi21Q → A: Not toxic in E.coli. 1 Publication1
Mutagenesisi25R → A: Not toxic in E.coli, 50-fold decreased RNA-binding. 1 Publication1
Mutagenesisi32N → A: Not toxic in E.coli. 1 Publication1
Mutagenesisi48T → A: Not toxic in E.coli. 1 Publication1
Mutagenesisi50Q → A: Remains toxic in E.coli. 1 Publication1
Mutagenesisi53K → A: Not toxic in E.coli, 70-fold decreased RNA-binding. 1 Publication1
Mutagenesisi56L → A: Not toxic in E.coli. 1 Publication1
Mutagenesisi59H → A: Not toxic in E.coli. 1 Publication1
Mutagenesisi71R → A: Remains toxic in E.coli. 1 Publication1
Mutagenesisi73S → A: Not toxic in E.coli, 100-fold decreased RNA-binding. 1 Publication1
Mutagenesisi78E → A: Not toxic in E.coli, 625-fold decreased RNA-binding. 1 Publication1
Mutagenesisi79Q → A: Not toxic in E.coli. 1 Publication1
Mutagenesisi90D → A: Remains toxic in E.coli. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002019001 – 116Endoribonuclease EndoAAdd BLAST116

Proteomic databases

PaxDbiP96622.

Interactioni

Subunit structurei

Homodimer (PubMed:14517982, PubMed:24120662). Forms a complex with antitoxin EndoAI in which the toxin activity is inhibited (PubMed:15882409). One dimer binds a ssRNA substrate, forms a heterohexamer composed of alternating toxin and antitoxin homodimers which inhibits the endoribonuclease activity. Antitoxin prevents RNA binding to the endoribonuclease (PubMed:24120662).3 Publications

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100002638.

Structurei

Secondary structure

1116
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 12Combined sources6
Beta strandi23 – 29Combined sources7
Helixi33 – 38Combined sources6
Beta strandi40 – 50Combined sources11
Beta strandi59 – 62Combined sources4
Helixi64 – 67Combined sources4
Beta strandi73 – 84Combined sources12
Helixi85 – 87Combined sources3
Beta strandi88 – 94Combined sources7
Helixi97 – 110Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NE8X-ray2.10A2-116[»]
4MDXX-ray1.50A/B1-116[»]
4ME7X-ray2.92A/B/C/D2-116[»]
ProteinModelPortaliP96622.
SMRiP96622.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP96622.

Family & Domainsi

Sequence similaritiesi

Belongs to the PemK/MazF family.Curated

Phylogenomic databases

eggNOGiENOG4108YZM. Bacteria.
COG2337. LUCA.
HOGENOMiHOG000290184.
InParanoidiP96622.
KOiK07171.
OMAiNDIGNQY.
PhylomeDBiP96622.

Family and domain databases

Gene3Di2.30.30.110. 1 hit.
InterProiIPR003477. PemK-like.
IPR011067. Plasmid_toxin/cell-grow_inhib.
[Graphical view]
PfamiPF02452. PemK_toxin. 1 hit.
[Graphical view]
PIRSFiPIRSF033490. MazF. 1 hit.
SUPFAMiSSF50118. SSF50118. 1 hit.

Sequencei

Sequence statusi: Complete.

P96622-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVKRGDVYF ADLSPVVGSE QGGVRPVLVI QNDIGNRFSP TAIVAAITAQ
60 70 80 90 100
IQKAKLPTHV EIDAKRYGFE RDSVILLEQI RTIDKQRLTD KITHLDDEMM
110
DKVDEALQIS LALIDF
Length:116
Mass (Da):12,978
Last modified:May 1, 1997 - v1
Checksum:iFE89144E62BD2B7C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001488 Genomic DNA. Translation: BAA19303.1.
AL009126 Genomic DNA. Translation: CAB12273.1.
PIRiC69773.
RefSeqiNP_388347.1. NC_000964.3.
WP_003156187.1. NZ_JNCM01000031.1.

Genome annotation databases

EnsemblBacteriaiCAB12273; CAB12273; BSU04660.
GeneIDi939935.
9779343.
KEGGibsu:BSU04660.
PATRICi18972516. VBIBacSub10457_0486.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001488 Genomic DNA. Translation: BAA19303.1.
AL009126 Genomic DNA. Translation: CAB12273.1.
PIRiC69773.
RefSeqiNP_388347.1. NC_000964.3.
WP_003156187.1. NZ_JNCM01000031.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NE8X-ray2.10A2-116[»]
4MDXX-ray1.50A/B1-116[»]
4ME7X-ray2.92A/B/C/D2-116[»]
ProteinModelPortaliP96622.
SMRiP96622.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100002638.

Proteomic databases

PaxDbiP96622.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12273; CAB12273; BSU04660.
GeneIDi939935.
9779343.
KEGGibsu:BSU04660.
PATRICi18972516. VBIBacSub10457_0486.

Phylogenomic databases

eggNOGiENOG4108YZM. Bacteria.
COG2337. LUCA.
HOGENOMiHOG000290184.
InParanoidiP96622.
KOiK07171.
OMAiNDIGNQY.
PhylomeDBiP96622.

Enzyme and pathway databases

BioCyciBSUB:BSU04660-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP96622.

Family and domain databases

Gene3Di2.30.30.110. 1 hit.
InterProiIPR003477. PemK-like.
IPR011067. Plasmid_toxin/cell-grow_inhib.
[Graphical view]
PfamiPF02452. PemK_toxin. 1 hit.
[Graphical view]
PIRSFiPIRSF033490. MazF. 1 hit.
SUPFAMiSSF50118. SSF50118. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiENDOA_BACSU
AccessioniPrimary (citable) accession number: P96622
Secondary accession number(s): Q797K4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2005
Last sequence update: May 1, 1997
Last modified: November 2, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Replacing all Arg residues by canavanine yields an enzyme that recognizes a longer consensus sequence UACAUA, thus altering its substrate specificity. Still cleaves between the first and second nucleotides.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.