Cloned (Comment) | Organism |
---|---|
overexpressed in Escherichia coli BL21(DE3) as full-length, C-terminally His-tagged protein | Providencia stuartii |
overexpressed in Escherichia coli BL21(DE3) as full-length, C-terminally His-tagged protein | Bacillus subtilis |
overexpressed in Escherichia coli BL21(DE3) as full-length, C-terminally His-tagged protein | Escherichia coli K-12 |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Na+ | supplemented with 0.4 M NaCl to enhance cleavage rate | Bacillus subtilis | |
Na+ | supplemented with 0.4 M NaCl to enhance cleavage rate | Escherichia coli K-12 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | P54493 | - |
- |
Escherichia coli K-12 | P09391 | - |
- |
Providencia stuartii | P46116 | - |
- |
Purification (Comment) | Organism |
---|---|
using Ni-NTA agarose | Providencia stuartii |
using Ni-NTA agarose | Bacillus subtilis |
using Ni-NTA agarose | Escherichia coli K-12 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | Comment | Organism |
---|---|---|
Rhomboid protease AarA | - |
Providencia stuartii |
Rhomboid protease glpG | - |
Escherichia coli K-12 |
Rhomboid protease gluP | - |
Bacillus subtilis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Providencia stuartii |
37 | - |
assay at | Bacillus subtilis |
37 | - |
assay at | Escherichia coli K-12 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Providencia stuartii |
7.5 | - |
assay at | Bacillus subtilis |
7.5 | - |
assay at | Escherichia coli K-12 |