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anti-sigma factor MucA + H2O
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the Prc protease degrades mutants forms of MucA, the enzyme activity does not affect alginate production in strains with wild-type MucA, but MucA22 mutants show the mucoid phenotype, overview
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Cab1R protein precursor + H2O
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Cab2R protein precursor + H2O
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D1 polypeptide of photosystem II + H2O
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D1 protein + H2O
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C-terminal processing of D1 protein
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membrane protein SpoIVFA + H2O
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sequenctial processing by the enzyme together with protease 4B. The 4FA regulatory protein is composed of a globular N-terminal domain, a transmembrane helix (residues 73-90), an unstructured linker region and a compact C-terminal domain (residues 160-255, LytM-like) extending into the intermembrane space. 4B/CtpB-mediated removal of 4FA residues 131-154 induces sK maturation
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NIpI protein + H2O
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processing of wild-type substrate and mutants lacking up to 11 amino acids of the C-terminus in vivo, a mutant NIpI protein lacking 12 C-terminal amino acids is not processed, overview, the enzyme activates the substrate
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pre-D1 protein + H2O
D1 protein + peptide
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catalyzes the conversion of the nascent pre-D1 (pD1) protein into the active form of D1 by cleaving the 9 C-terminal residues in spinach, required to maintain the function of the photosystem II complex
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pre-LHCP protein + H2O
LHCP protein + transit peptide
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pre-RBCS protein + H2O
RBCS protein + transit peptide
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ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit precursor + H2O
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additional information
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D1 polypeptide of photosystem II + H2O
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D1 polypeptide of photosystem II + H2O
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D1 polypeptide of photosystem II + H2O
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D1 polypeptide of photosystem II + H2O
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in vivo proteolytic processing of pre-D1, no other protease can compensate for its loss
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Protein + H2O
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endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
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Protein + H2O
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endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
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Protein + H2O
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Protein + H2O
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endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
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Protein + H2O
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Tsp is a component of the ssrA RNA protein-tagging pathway for the removal of incorrectly synthesized proteins
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Protein + H2O
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endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
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Protein + H2O
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endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
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Protein + H2O
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Protein + H2O
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Protein + H2O
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additional information
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broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
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additional information
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O48870
broad substrate specificity, overview, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview, the enzyme is essential for plant survival, regulation of expression in vivo
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additional information
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the enzyme belongs to the family of endoproteases involved in the maturation of proteins destined for the cell envelope
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additional information
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broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
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additional information
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broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
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additional information
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broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
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additional information
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broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
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additional information
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broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
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additional information
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broad substrate specificity, the stromal processing peptidase has a function in the apicoplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
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additional information
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critical for the viability when cells are grown on complex semi-solid media, not essential when cells are grown in complex liquid media, enzyme function affects the permeability of the cell wall
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additional information
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broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
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