O34327 · RAPJ_BACSU

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).

Features

Showing features for binding site.

137350100150200250300350
TypeIDPosition(s)Description
Binding site147L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor
Binding site150L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor
Binding site181L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor
Binding site192L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor
Binding site217L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor
Binding site225L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor
Binding site228L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor
Binding site260L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor
Binding site297L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor
Binding site300L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor
Binding site335L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine (UniProtKB | ChEBI); allosteric inhibitor

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionphosphoprotein phosphatase activity
Biological Processsporulation resulting in formation of a cellular spore

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Response regulator aspartate phosphatase J
  • EC number

Gene names

    • Name
      rapJ
    • Synonyms
      ycdE
    • Ordered locus names
      BSU02820

Organism names

Accessions

  • Primary accession
    O34327

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis87Displays a severe phosphatase defect.
Mutagenesis105Shows wild-type phosphatase activity but is insensitive to PhrC inhibition.
Mutagenesis147Insensitive to PhrC inhibition.
Mutagenesis150Insensitive to PhrC inhibition.
Mutagenesis161Shows wild-type phosphatase activity and sensitivity to PhrC inhibition.
Mutagenesis192Insensitive to PhrC inhibition.
Mutagenesis225Insensitive to PhrC inhibition.
Mutagenesis250Insensitive to PhrC inhibition.
Mutagenesis300Insensitive to PhrC inhibition.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001064441-373Response regulator aspartate phosphatase J

Proteomic databases

Interaction

Subunit

Monomer in solution (PubMed:23526881).
Homodimer (PubMed:21346797).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY O34327phrC P944164EBI-5246213, EBI-16042798
BINARY O34327spo0F P066282EBI-5246213, EBI-6418009

Protein-protein interaction databases

Family & Domains

Features

Showing features for repeat.

TypeIDPosition(s)Description
Repeat99-135TPR 1
Repeat146-179TPR 2
Repeat220-253TPR 3
Repeat259-292TPR 4
Repeat334-367TPR 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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    373
  • Mass (Da)
    44,414
  • Last updated
    1998-01-01 v1
  • Checksum
    E5EC939CE2B6E1DC
MRAKIPSEEVAVKLNEWYKLIRAFEADQAEALKQEIEYDLEDMEENQDLLLYFSLMEFRHRIMLDKLMPVKDSDTKPPFSDMLNEIESNQQKLTGLLEYYFYYFRGMYEFKQKNFILAIDHYKHAEEKLEYVEDEIEKAEFLFKVAEVYYHIKQTYFSMNYASQALDIYTKYELYGRRRVQCEFIIAGNLTDVYHHEKALTHLCSALEHARQLEEAYMIAAAYYNVGHCKYSLGDYKEAEGYFKTAAAIFEEHNFQQAVQAVFSLTHIYCKEGKYDKAVEAYDRGIKSAAEWEDDMYLTKFRLIHELYLGSGDLNVLTECFDLLESRQLLADAEDLLHDTAERFNQLEHYESAAFFYRRLMNIKKKLAEQRFQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB000617
EMBL· GenBank· DDBJ
BAA22243.1
EMBL· GenBank· DDBJ
Genomic DNA
AL009126
EMBL· GenBank· DDBJ
CAB12076.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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