O34327 · RAPJ_BACSU
- ProteinResponse regulator aspartate phosphatase J
- GenerapJ
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids373 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the regulation of sporulation (Probable). Acts as a phosphatase that specifically dephosphorylates the sporulation initiation phosphotransferase Spo0F and inhibits its activity (PubMed:21346797, PubMed:23526881).
Activity regulation
Inhibited in vitro by the competence and sporulation stimulating factor (CSF), encoded by phrC (PubMed:23526881).
However, CSF has at least three targets (RapB, RapC, and RapJ) and the physiological importance of RapJ inhibition by CSF is unknown (PubMed:23526881).
Interaction with CSF induces a conformational change in RapJ (PubMed:23526881).
However, CSF has at least three targets (RapB, RapC, and RapJ) and the physiological importance of RapJ inhibition by CSF is unknown (PubMed:23526881).
Interaction with CSF induces a conformational change in RapJ (PubMed:23526881).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 147 | L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor | |||
Binding site | 150 | L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor | |||
Binding site | 181 | L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor | |||
Binding site | 192 | L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor | |||
Binding site | 217 | L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor | |||
Binding site | 225 | L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor | |||
Binding site | 228 | L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor | |||
Binding site | 260 | L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor | |||
Binding site | 297 | L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor | |||
Binding site | 300 | L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor | |||
Binding site | 335 | L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | phosphoprotein phosphatase activity | |
Biological Process | sporulation resulting in formation of a cellular spore |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameResponse regulator aspartate phosphatase J
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionO34327
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 87 | Displays a severe phosphatase defect. | |||
Mutagenesis | 105 | Shows wild-type phosphatase activity but is insensitive to PhrC inhibition. | |||
Mutagenesis | 147 | Insensitive to PhrC inhibition. | |||
Mutagenesis | 150 | Insensitive to PhrC inhibition. | |||
Mutagenesis | 161 | Shows wild-type phosphatase activity and sensitivity to PhrC inhibition. | |||
Mutagenesis | 192 | Insensitive to PhrC inhibition. | |||
Mutagenesis | 225 | Insensitive to PhrC inhibition. | |||
Mutagenesis | 250 | Insensitive to PhrC inhibition. | |||
Mutagenesis | 300 | Insensitive to PhrC inhibition. | |||
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000106444 | 1-373 | Response regulator aspartate phosphatase J | ||
Proteomic databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | IntAct | |
---|---|---|---|---|---|
BINARY | O34327 | phrC P94416 | 4 | EBI-5246213, EBI-16042798 | |
BINARY | O34327 | spo0F P06628 | 2 | EBI-5246213, EBI-6418009 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for repeat.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Repeat | 99-135 | TPR 1 | |||
Repeat | 146-179 | TPR 2 | |||
Repeat | 220-253 | TPR 3 | |||
Repeat | 259-292 | TPR 4 | |||
Repeat | 334-367 | TPR 5 | |||
Domain
Contains a small N-terminal 3-helix bundle domain and a large C-terminal TPR domain, connected by a linker region.
Sequence similarities
Belongs to the Rap family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length373
- Mass (Da)44,414
- Last updated1998-01-01 v1
- ChecksumE5EC939CE2B6E1DC
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB000617 EMBL· GenBank· DDBJ | BAA22243.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL009126 EMBL· GenBank· DDBJ | CAB12076.1 EMBL· GenBank· DDBJ | Genomic DNA |