UniProtKB - O31760 (RNJ2_BACSU)
Protein
Ribonuclease J2
Gene
rnjB
Organism
Bacillus subtilis (strain 168)
Status
Functioni
Endonucleolytically cleaves the 5'-leader sequence of certain mRNAs. Endonuclease digestion by the RNase J1/J2 complex occurs at a different site and in some cases more efficiently than J1 or J2 alone. The exonuclease activity of the J1/J2 complex is highly processive on substrates longer than 5 nucleotides, on shorter substrates is distributive. Plays a role in mRNA maturation and stability. Appears to have a limited effect on 16S rRNA maturation, despite its similarity to RNase J1. This subunit alone has very poor 5'-3' exonuclease activity.6 Publications
Miscellaneous
Present in about 3000 monomers per cell in mid-log phase.
Cofactori
Zn2+By similarity2 PublicationsNote: Binds 1 zinc ion per subunit. The inability to bind a second zinc ion may explain its very poor exonuclease activity (PubMed:21893285).By similarity2 Publications
Kineticsi
kcat is 0.58 sec (-1) for J1, 0.13 sec (-1) for J1/J2 and <0.005 sec (-1) for J2.
- KM=5.96 µM for exonuclease on 30 nt RNA hybridized to 17 nt quenching DNA, J2 alone1 Publication
- KM=0.22 µM for exonuclease on 30 nt RNA hybridized to 17 nt quenching DNA, J1/J2 complex1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 74 | Zinc; catalyticUniRule annotation | 1 | |
Metal bindingi | 76 | Zinc; catalyticUniRule annotation | 1 | |
Metal bindingi | 142 | Zinc; catalyticUniRule annotation | 1 | |
Metal bindingi | 164 | Zinc; catalyticUniRule annotation | 1 |
GO - Molecular functioni
- 5'-3' exoribonuclease activity Source: UniProtKB-UniRule
- endoribonuclease activity Source: UniProtKB
- RNA binding Source: UniProtKB-UniRule
- zinc ion binding Source: InterPro
GO - Biological processi
- mRNA processing Source: UniProtKB
- rRNA processing Source: UniProtKB-UniRule
Keywordsi
Molecular function | Endonuclease, Exonuclease, Hydrolase, Nuclease, RNA-binding |
Biological process | rRNA processing |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BioCyci | BSUB:BSU16780-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: Ribonuclease J2UniRule annotation (EC:3.1.-.-UniRule annotation)Short name: RNase J2UniRule annotation |
Gene namesi | Name:rnjBUniRule annotation Synonyms:ymfA Ordered Locus Names:BSU16780 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation1 Publication
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Disruption phenotypei
Not essential. While depletion/deletion of RNase J1 or J2 has no large impact on global gene expression, a double mutant alters the expression of hundreds of genes (PubMed:18713320).3 Publications
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000286833 | 1 – 555 | Ribonuclease J2Add BLAST | 555 |
Proteomic databases
jPOSTi | O31760 |
PaxDbi | O31760 |
PRIDEi | O31760 |
Interactioni
Subunit structurei
Unclear whether it forms homodimers or belongs to a larger complex. According to (PubMed:20025672) probably does not form homodimers, while (PubMed:21893285) shows homodimer formation. Both reports show RNase J1 and J2 interaction, probably as a heterotetramer (PubMed:19193632) shows it is a component of a possible RNA degradosome complex composed of rny, rnjA, rnjB, pnp, pfkA and eno, while (PubMed:20025672) finds no evidence of an RNA degradosome complex.
5 PublicationsBinary interactionsi
O31760
With | #Exp. | IntAct |
---|---|---|
rnjA [Q45493] | 4 | EBI-6415198,EBI-6415229 |
Protein-protein interaction databases
DIPi | DIP-59141N |
IntActi | O31760, 4 interactors |
MINTi | O31760 |
STRINGi | 224308.BSU16780 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 364 – 368 | Substrate bindingUniRule annotation | 5 |
Sequence similaritiesi
Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. Bacterial RNase J subfamily.UniRule annotation
Phylogenomic databases
eggNOGi | COG0595, Bacteria |
InParanoidi | O31760 |
OMAi | DFKMDQF |
PhylomeDBi | O31760 |
Family and domain databases
Gene3Di | 3.40.50.10710, 1 hit 3.60.15.10, 1 hit |
HAMAPi | MF_01491, RNase_J_bact, 1 hit |
InterProi | View protein in InterPro IPR001279, Metallo-B-lactamas IPR036866, RibonucZ/Hydroxyglut_hydro IPR011108, RMMBL IPR004613, RNase_J IPR042173, RNase_J_2 IPR030854, RNase_J_bac IPR041636, RNase_J_C |
Pfami | View protein in Pfam PF00753, Lactamase_B, 1 hit PF07521, RMMBL, 1 hit PF17770, RNase_J_C, 1 hit |
PIRSFi | PIRSF004803, RnjA, 1 hit |
SMARTi | View protein in SMART SM00849, Lactamase_B, 1 hit |
SUPFAMi | SSF56281, SSF56281, 1 hit |
TIGRFAMsi | TIGR00649, MG423, 1 hit |
i Sequence
Sequence statusi: Complete.
O31760-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKKKNTENVR IIALGGVGEI GKNLYVIEID SDIFVVDAGL MHPENEMLGI
60 70 80 90 100
DVVIPDISYL IERADRVKAI FLTHGHDENI GGVFYLLNKL SVPVYGTKLT
110 120 130 140 150
LALLREKLKQ YGHNRKTDLR EIHSKSVITF ESTKVSFFRT IHSIPDSVGV
160 170 180 190 200
SFKTSLGSIV CTGDFKFDQT PALNQTCDIG EIAKIGNSGV LALLSDSANA
210 220 230 240 250
ERPGYTPSEA AVSGEISDAL YNSQNRVIIA VFASNINRIQ QVIHAAAQNG
260 270 280 290 300
RKIAVAGKNL QSVLQLARKL GYIEADDELF ISVQDVKKYP KREVAIITAG
310 320 330 340 350
SQGEPLAALT RMANKAHKQL NIEEGDTVVI ASTPIPGQEL IYSKTVDLLA
360 370 380 390 400
RAGAQVIFAQ KRVHVSGHGS QEELKLMINL LKPKYLIPVN GEYRMQKAHS
410 420 430 440 450
KIAEETGMKR SDIFLIEKGD VVEFRGQNVK IGDKVPYGNI LIDGLGVGDI
460 470 480 490 500
GNIVLRDRRL LSQDGILIVV ITLDKQKKHL VSGPEIITRG FVYVRESEGL
510 520 530 540 550
IVQATELVRS IVTEATETSN VEWSTLKQAM RDALNQFLYE KTKRKPMIIP
IIMEV
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL009126 Genomic DNA Translation: CAB13551.2 |
PIRi | H69884 |
RefSeqi | NP_389560.2, NC_000964.3 WP_003231875.1, NZ_JNCM01000035.1 |
Genome annotation databases
EnsemblBacteriai | CAB13551; CAB13551; BSU_16780 |
GeneIDi | 938463 |
KEGGi | bsu:BSU16780 |
PATRICi | fig|224308.179.peg.1820 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL009126 Genomic DNA Translation: CAB13551.2 |
PIRi | H69884 |
RefSeqi | NP_389560.2, NC_000964.3 WP_003231875.1, NZ_JNCM01000035.1 |
3D structure databases
SMRi | O31760 |
ModBasei | Search... |
Protein-protein interaction databases
DIPi | DIP-59141N |
IntActi | O31760, 4 interactors |
MINTi | O31760 |
STRINGi | 224308.BSU16780 |
Proteomic databases
jPOSTi | O31760 |
PaxDbi | O31760 |
PRIDEi | O31760 |
Genome annotation databases
EnsemblBacteriai | CAB13551; CAB13551; BSU_16780 |
GeneIDi | 938463 |
KEGGi | bsu:BSU16780 |
PATRICi | fig|224308.179.peg.1820 |
Phylogenomic databases
eggNOGi | COG0595, Bacteria |
InParanoidi | O31760 |
OMAi | DFKMDQF |
PhylomeDBi | O31760 |
Enzyme and pathway databases
BioCyci | BSUB:BSU16780-MONOMER |
Family and domain databases
Gene3Di | 3.40.50.10710, 1 hit 3.60.15.10, 1 hit |
HAMAPi | MF_01491, RNase_J_bact, 1 hit |
InterProi | View protein in InterPro IPR001279, Metallo-B-lactamas IPR036866, RibonucZ/Hydroxyglut_hydro IPR011108, RMMBL IPR004613, RNase_J IPR042173, RNase_J_2 IPR030854, RNase_J_bac IPR041636, RNase_J_C |
Pfami | View protein in Pfam PF00753, Lactamase_B, 1 hit PF07521, RMMBL, 1 hit PF17770, RNase_J_C, 1 hit |
PIRSFi | PIRSF004803, RnjA, 1 hit |
SMARTi | View protein in SMART SM00849, Lactamase_B, 1 hit |
SUPFAMi | SSF56281, SSF56281, 1 hit |
TIGRFAMsi | TIGR00649, MG423, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RNJ2_BACSU | |
Accessioni | O31760Primary (citable) accession number: O31760 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 15, 2007 |
Last sequence update: | June 16, 2009 | |
Last modified: | April 7, 2021 | |
This is version 115 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families