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Literature summary extracted from

  • Strisovsky, K.; Sharpe, H.J.; Freeman, M.
    Sequence-specific intramembrane proteolysis: identification of a recognition motif in rhomboid substrates (2009), Mol. Cell, 36, 1048-1059.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.105 overexpressed in Escherichia coli BL21(DE3) as full-length, C-terminally His-tagged protein Providencia stuartii
3.4.21.105 overexpressed in Escherichia coli BL21(DE3) as full-length, C-terminally His-tagged protein Bacillus subtilis
3.4.21.105 overexpressed in Escherichia coli BL21(DE3) as full-length, C-terminally His-tagged protein Escherichia coli K-12

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.105 Na+ supplemented with 0.4 M NaCl to enhance cleavage rate Bacillus subtilis
3.4.21.105 Na+ supplemented with 0.4 M NaCl to enhance cleavage rate Escherichia coli K-12

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.105 Bacillus subtilis P54493
-
-
3.4.21.105 Escherichia coli K-12 P09391
-
-
3.4.21.105 Providencia stuartii P46116
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.105 using Ni-NTA agarose Providencia stuartii
3.4.21.105 using Ni-NTA agarose Bacillus subtilis
3.4.21.105 using Ni-NTA agarose Escherichia coli K-12

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.105 LacY trans-membrane domain 2 + H2O LacY trans-membrane domain 2 of Escherichia coli is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage Providencia stuartii ?
-
 ?
3.4.21.105 LacY trans-membrane domain 2 + H2O LacY trans-membrane domain 2 of Escherichia coli is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage Bacillus subtilis ?
-
 ?
3.4.21.105 LacY trans-membrane domain 2 + H2O LacY trans-membrane domain 2 of Escherichia coli is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage Escherichia coli K-12 ?
-
 ?
3.4.21.105 additional information based on trans-membrane domain of Providencia stuartii TatA as a model substrate a primary recognition motif is identified by a series of deletion analysis. Three positions are particularly sensitive to mutations: P1, P4 and P2'. Whereas P1 tolerates only amino acids with a small side chain, P4 requires large and hydrophobic residues, and P2' prefers hydrophobic side chains irrespective of their size. All other positions between P5 and P2' can tolerate a variety of amino acids, although tryptophan, proline, and aspartate are deleterious in most of them. This recognition motif is functionally conserved in multiple substrates Providencia stuartii ?
-
 ?
3.4.21.105 additional information based on trans-membrane domain of Providencia stuartii TatA as a model substrate a primary recognition motif is identified by a series of deletion analysis. Three positions are particularly sensitive to mutations: P1, P4 and P2'. Whereas P1 tolerates only amino acids with a small side chain, P4 requires large and hydrophobic residues, and P2' prefers hydrophobic side chains irrespective of their size. All other positions between P5 and P2' can tolerate a variety of amino acids, although tryptophan, proline, and aspartate are deleterious in most of them. This recognition motif is functionally conserved in multiple substrates Bacillus subtilis ?
-
 ?
3.4.21.105 additional information based on trans-membrane domain of Providencia stuartii TatA as a model substrate a primary recognition motif is identified by a series of deletion analysis. Three positions are particularly sensitive to mutations: P1, P4 and P2'. Whereas P1 tolerates only amino acids with a small side chain, P4 requires large and hydrophobic residues, and P2' prefers hydrophobic side chains irrespective of their size. All other positions between P5 and P2' can tolerate a variety of amino acids, although tryptophan, proline, and aspartate are deleterious in most of them. This recognition motif is functionally conserved in multiple substrates Escherichia coli K-12 ?
-
 ?
3.4.21.105 TatA + H2O trans-membrane domain of Providencia stuartii TatA polypeptide segment E2-G98 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage Providencia stuartii ?
-
 ?
3.4.21.105 TatA + H2O trans-membrane domain of Providencia stuartii TatA polypeptide segment E2-G98 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage Bacillus subtilis ?
-
 ?
3.4.21.105 TatA + H2O trans-membrane domain of Providencia stuartii TatA polypeptide segment E2-G98 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage Escherichia coli K-12 ?
-
 ?
3.4.21.105 trans-membrane domain + H2O trans-membrane domain of Drosophila melanogaster Spitz polypeptide segment G114-L161 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage Providencia stuartii ?
-
 ?
3.4.21.105 trans-membrane domain + H2O trans-membrane domain of Drosophila melanogaster Spitz polypeptide segment G114-L161 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage Bacillus subtilis ?
-
 ?
3.4.21.105 trans-membrane domain + H2O trans-membrane domain of Drosophila melanogaster Spitz polypeptide segment G114-L161 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage Escherichia coli K-12 ?
-
 ?
3.4.21.105 trans-membrane domain Gurken + H2O trans-membrane domain of Drosophila melanogaster Gurken polypeptide segment A223-R271 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage Providencia stuartii ?
-
 ?
3.4.21.105 trans-membrane domain Gurken + H2O trans-membrane domain of Drosophila melanogaster Gurken polypeptide segment A223-R271 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage Bacillus subtilis ?
-
 ?
3.4.21.105 trans-membrane domain Gurken + H2O trans-membrane domain of Drosophila melanogaster Gurken polypeptide segment A223-R271 is engineered into a fusion protein backbone that includes a signal peptide and maltose-binding protein N-terminal to the trans-membrane domain, and a thioredoxin domain and His tag at the C terminus. Substrate is cleaved at the same position by different bacterial rhomboids. Insertion into a fusion protein does not affect cleavage Escherichia coli K-12 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.21.105 Rhomboid protease AarA
-
 Providencia stuartii
3.4.21.105 Rhomboid protease glpG
-
 Escherichia coli K-12
3.4.21.105 Rhomboid protease gluP
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.105 37
-
 assay at Providencia stuartii
3.4.21.105 37
-
 assay at Bacillus subtilis
3.4.21.105 37
-
 assay at Escherichia coli K-12

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.105 7.5
-
 assay at Providencia stuartii
3.4.21.105 7.5
-
 assay at Bacillus subtilis
3.4.21.105 7.5
-
 assay at Escherichia coli K-12