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Literature summary for 3.4.21.116 extracted from

  • Dong, T.C.; Cutting, S.M.
    The PDZ domain of the SpoIVB transmembrane signaling protein enables cis-trans interactions involving multiple partners leading to the activation of the pro-sigmaK processing complex in Bacillus subtilis (2004), J. Biol. Chem., 279, 43468-43478.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information N-terminal deletion of residues 1-35, 1-52, 1-62 or 1-74 and additional C-terminal deletion of up to 33 residues. Study on autoactivation process, which involves one trans cleavage by another enzyme protein and two cis cleavages Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
x * 46000, full-length protein, x * 40000, x * 39000, x * 38000, autoactivation products, SDS-PAGE Bacillus subtilis
39000
-
x * 46000, full-length protein, x * 40000, x * 39000, x * 38000, autoactivation products, SDS-PAGE Bacillus subtilis
40000
-
x * 46000, full-length protein, x * 40000, x * 39000, x * 38000, autoactivation products, SDS-PAGE Bacillus subtilis
46000
-
x * 46000, full-length protein, x * 40000, x * 39000, x * 38000, autoactivation products, SDS-PAGE Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bacillus subtilis autoproteolytical activation. PDZ domain of enzyme binds to enzyme N-terminus to maintain its zymogen form. Following secretion across a spore membrane, domain binds in trans to the C-terminus of another enzyme molecule thus facilitating first cleavage event of enzyme near the N-terminus which releases the enzyme from the forespore membrane ?
-
?
SpoIVFA + H2O Bacillus subtilis intrinsic protein substrate ?
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification autoproteolytical activation. PDZ domain of enzyme binds to enzyme N-terminus to maintain its zymogen form. Following secretion across a spore membrane, domain binds in trans to the C-terminus of another enzyme molecule thus facilitating first cleavage event of enzyme near the N-terminus which releases the enzyme from the forespore membrane Bacillus subtilis

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information autoproteolytical activation. PDZ domain of enzyme binds to enzyme N-terminus to maintain its zymogen form. Following secretion across a spore membrane, domain binds in trans to the C-terminus of another enzyme molecule thus facilitating first cleavage event of enzyme near the N-terminus which releases the enzyme from the forespore membrane Bacillus subtilis ?
-
?
SpoIVFA + H2O intrinsic protein substrate Bacillus subtilis ?
-
?

Subunits

Subunits Comment Organism
? x * 46000, full-length protein, x * 40000, x * 39000, x * 38000, autoactivation products, SDS-PAGE Bacillus subtilis
More Enzyme binds specifically to intrinsic protein BofA Bacillus subtilis

Synonyms

Synonyms Comment Organism
SpoIVB
-
Bacillus subtilis