Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of a deletion mutant DELTAcroP | Citrobacter rodentium |
additional information | generation of a deletion mutant DELTAompT | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Aprotinin | inhibits CroP in a competitive manner | Citrobacter rodentium | |
Aprotinin | inhibits OmpT in a competitive manner | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
human LL-37 + H2O | Escherichia coli | a cathelicidin | ? | - |
? | |
human LL-37 + H2O | Citrobacter rodentium | a cathelicidin | ? | - |
? | |
human LL-37 + H2O | Citrobacter rodentium ATCC 51459 | a cathelicidin | ? | - |
? | |
human LL-37 + H2O | Citrobacter rodentium DBS 100 | a cathelicidin | ? | - |
? | |
human LL-37 + H2O | Escherichia coli EDL933 | a cathelicidin | ? | - |
? | |
murine cathelicidin-related antimicrobial peptide + H2O | Escherichia coli | CRAMP | ? | - |
? | |
murine cathelicidin-related antimicrobial peptide + H2O | Citrobacter rodentium | CRAMP | ? | - |
? | |
murine cathelicidin-related antimicrobial peptide + H2O | Citrobacter rodentium ATCC 51459 | CRAMP | ? | - |
? | |
murine cathelicidin-related antimicrobial peptide + H2O | Citrobacter rodentium DBS 100 | CRAMP | ? | - |
? | |
murine cathelicidin-related antimicrobial peptide + H2O | Escherichia coli EDL933 | CRAMP | ? | - |
? | |
plasminogen + H2O | Escherichia coli | - |
plasmin + ? | - |
? | |
plasminogen + H2O | Escherichia coli EDL933 | - |
plasmin + ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Citrobacter rodentium | - |
- |
- |
Citrobacter rodentium ATCC 51459 | - |
- |
- |
Citrobacter rodentium DBS 100 | - |
- |
- |
Escherichia coli | P58603 | - |
- |
Escherichia coli EDL933 | P58603 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Abz-SLGRKIQIK(Dnp)-NH2 + H2O | - |
Escherichia coli | Abz-SLGR + KIQIK(Dnp)-NH2 | - |
? | |
Abz-SLGRKIQIK(Dnp)-NH2 + H2O | - |
Citrobacter rodentium | Abz-SLGR + KIQIK(Dnp)-NH2 | - |
? | |
Abz-SLGRKIQIK(Dnp)-NH2 + H2O | - |
Citrobacter rodentium ATCC 51459 | Abz-SLGR + KIQIK(Dnp)-NH2 | - |
? | |
Abz-SLGRKIQIK(Dnp)-NH2 + H2O | - |
Citrobacter rodentium DBS 100 | Abz-SLGR + KIQIK(Dnp)-NH2 | - |
? | |
Abz-SLGRKIQIK(Dnp)-NH2 + H2O | - |
Escherichia coli EDL933 | Abz-SLGR + KIQIK(Dnp)-NH2 | - |
? | |
human LL-37 + H2O | a cathelicidin | Escherichia coli | ? | - |
? | |
human LL-37 + H2O | a cathelicidin | Citrobacter rodentium | ? | - |
? | |
human LL-37 + H2O | a cathelicidin | Citrobacter rodentium ATCC 51459 | ? | - |
? | |
human LL-37 + H2O | a cathelicidin | Citrobacter rodentium DBS 100 | ? | - |
? | |
human LL-37 + H2O | a cathelicidin | Escherichia coli EDL933 | ? | - |
? | |
additional information | Citrobacter rodentium CroP cleaves CRAMP more rapidly than LL-37. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions. By altering the alpha-helicity of LL-37 and CRAMP, decreasing LL-37 alpha-helicity increases its rate of cleavage by CroP. Conversely, increasing CRAMP alpha-helicity decreased its cleavage rate. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs) | Citrobacter rodentium | ? | - |
? | |
additional information | EHEC OmpT degrades LL-37 and CRAMP at similar rates. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions | Escherichia coli | ? | - |
? | |
additional information | Citrobacter rodentium CroP cleaves CRAMP more rapidly than LL-37. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions. By altering the alpha-helicity of LL-37 and CRAMP, decreasing LL-37 alpha-helicity increases its rate of cleavage by CroP. Conversely, increasing CRAMP alpha-helicity decreased its cleavage rate. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs) | Citrobacter rodentium ATCC 51459 | ? | - |
? | |
additional information | Citrobacter rodentium CroP cleaves CRAMP more rapidly than LL-37. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions. By altering the alpha-helicity of LL-37 and CRAMP, decreasing LL-37 alpha-helicity increases its rate of cleavage by CroP. Conversely, increasing CRAMP alpha-helicity decreased its cleavage rate. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs) | Citrobacter rodentium DBS 100 | ? | - |
? | |
additional information | EHEC OmpT degrades LL-37 and CRAMP at similar rates. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions | Escherichia coli EDL933 | ? | - |
? | |
murine cathelicidin-related antimicrobial peptide + H2O | CRAMP | Escherichia coli | ? | - |
? | |
murine cathelicidin-related antimicrobial peptide + H2O | CRAMP | Citrobacter rodentium | ? | - |
? | |
murine cathelicidin-related antimicrobial peptide + H2O | CRAMP, rapid, almost complete degradation | Citrobacter rodentium | ? | - |
? | |
murine cathelicidin-related antimicrobial peptide + H2O | CRAMP | Citrobacter rodentium ATCC 51459 | ? | - |
? | |
murine cathelicidin-related antimicrobial peptide + H2O | CRAMP, rapid, almost complete degradation | Citrobacter rodentium ATCC 51459 | ? | - |
? | |
murine cathelicidin-related antimicrobial peptide + H2O | CRAMP | Citrobacter rodentium DBS 100 | ? | - |
? | |
murine cathelicidin-related antimicrobial peptide + H2O | CRAMP, rapid, almost complete degradation | Citrobacter rodentium DBS 100 | ? | - |
? | |
murine cathelicidin-related antimicrobial peptide + H2O | CRAMP | Escherichia coli EDL933 | ? | - |
? | |
plasminogen + H2O | - |
Escherichia coli | plasmin + ? | - |
? | |
plasminogen + H2O | - |
Escherichia coli EDL933 | plasmin + ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CroP | - |
Citrobacter rodentium |
ompT | - |
Escherichia coli |
omptin protease | - |
Escherichia coli |
omptin protease | - |
Citrobacter rodentium |
protease 7 | UniProt | Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at room temperature | Escherichia coli |
22 | - |
assay at room temperature | Citrobacter rodentium |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Escherichia coli |
7.4 | - |
assay at | Citrobacter rodentium |
General Information | Comment | Organism |
---|---|---|
evolution | the difference in CroP and OmpT substrate specificity suggests that omptins evolved in response to the substrates present in their host microenvironments | Escherichia coli |
evolution | the difference in CroP and OmpT substrate specificity suggests that omptins evolved in response to the substrates present in their host microenvironments | Citrobacter rodentium |
physiological function | Citrobacter rodentium inactivates antimicrobial peptides (AMPs) and activates plasminogen into plasmin, respectively. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs) | Citrobacter rodentium |
physiological function | Escherichia coli OmpT inactivates antimicrobial peptides (AMPs) and activates plasminogen into plasmin, respectively | Escherichia coli |