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Literature summary extracted from

  • Keiler, K.C.; Sauer, R.T.
    Tsp protease (1998), Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press, , 460-461.
No PubMed abstract available

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.102 periplasm
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 Escherichia coli
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Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.102 Protein + H2O Haemophilus influenzae 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. ?
-
 ?
3.4.21.102 Protein + H2O Bacillus subtilis 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. ?
-
 ?
3.4.21.102 Protein + H2O Escherichia coli 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. ?
-
 ?
3.4.21.102 Protein + H2O Neisseria gonorrhoeae 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. ?
-
 ?
3.4.21.102 Protein + H2O Bartonella bacilliformis 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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 ?
3.4.21.102 Protein + H2O Escherichia coli Tsp is a component of the ssrA RNA protein-tagging pathway for the removal of incorrectly synthesized proteins ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.102 Bacillus subtilis
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-
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3.4.21.102 Bartonella bacilliformis
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3.4.21.102 Escherichia coli
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-
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3.4.21.102 Haemophilus influenzae
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-
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3.4.21.102 Neisseria gonorrhoeae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.102 Protein + H2O endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal positions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third postion 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 Haemophilus influenzae ?
-
 ?
3.4.21.102 Protein + H2O endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal positions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third postion 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 Bacillus subtilis ?
-
 ?
3.4.21.102 Protein + H2O endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal positions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third postion 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 Escherichia coli ?
-
 ?
3.4.21.102 Protein + H2O endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal positions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third postion 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 Neisseria gonorrhoeae ?
-
 ?
3.4.21.102 Protein + H2O endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal positions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third postion 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 Bartonella bacilliformis ?
-
 ?
3.4.21.102 Protein + H2O 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. Haemophilus influenzae ?
-
 ?
3.4.21.102 Protein + H2O 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. Bacillus subtilis ?
-
 ?
3.4.21.102 Protein + H2O 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. Escherichia coli ?
-
 ?
3.4.21.102 Protein + H2O 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. Neisseria gonorrhoeae ?
-
 ?
3.4.21.102 Protein + H2O 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. Bartonella bacilliformis ?
-
 ?
3.4.21.102 Protein + H2O Tsp is a component of the ssrA RNA protein-tagging pathway for the removal of incorrectly synthesized proteins Escherichia coli ?
-
 ?