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Literature summary for 3.4.21.B49 extracted from

  • Campo N.; Rudner D.Z.
    SpoIVB and CtpB are both forespore signals in the activation of the sporulation transcription factor sigmaK in Bacillus subtilis (2007), J. Bacteriol., 189, 6021-6027.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.B49

Cloned(Commentary)

Cloned (Comment) Organism
expressed as His-tag fusion protein Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
A36R not cleavable by SpoIVB Bacillus subtilis
A40R not cleavable by SpoIVB Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information secreted by the forespore into the intermembrane space between the forespore and the mother cell membrane Bacillus subtilis
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bacillus subtilis autoproteolysis as observed for SpoIVB ?
-
 ?
additional information Bacillus subtilis involved in sigmaK signaling, acts in cooperation with SpoIVB ?
-
 ?
additional information Bacillus subtilis PY79 autoproteolysis as observed for SpoIVB ?
-
 ?
additional information Bacillus subtilis PY79 involved in sigmaK signaling, acts in cooperation with SpoIVB ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis PY79
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information autoproteolysis as observed for SpoIVB Bacillus subtilis ?
-
 ?
additional information involved in sigmaK signaling, acts in cooperation with SpoIVB Bacillus subtilis ?
-
 ?
additional information autoproteolysis as observed for SpoIVB Bacillus subtilis PY79 ?
-
 ?
additional information involved in sigmaK signaling, acts in cooperation with SpoIVB Bacillus subtilis PY79 ?
-
 ?

Synonyms

Synonyms Comment Organism
CtpB PDZ-containing serine protease with similar organization as SpoIVB, enzyme activated by autoproteolysis and cleavage by SpoIVB Bacillus subtilis