Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004175 | molecular_function | endopeptidase activity |
| A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0009279 | cellular_component | cell outer membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0004175 | molecular_function | endopeptidase activity |
| B | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0009279 | cellular_component | cell outer membrane |
| B | 0016787 | molecular_function | hydrolase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00835 |
| Number of Residues | 17 |
| Details | OMPTIN_2 Aspartyl proteases, omptin family signature 2. AGYQESRYSFTArGGSY |
| Chain | Residue | Details |
| A | ALA132-TYR148 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 34 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 184 |
| Details | Transmembrane: {"description":"Beta stranded","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 326 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"11576541","evidenceCode":"ECO:0000305"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 10692590, 11566868, 15315948 |
| Chain | Residue | Details |
| A | HIS212 | |
| A | ASP85 | |
| A | ASP83 | |
| A | ALA99 | |
| A | ASP210 | |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 10692590, 11566868, 15315948 |
| Chain | Residue | Details |
| B | HIS212 | |
| B | ASP85 | |
| B | ASP83 | |
| B | ALA99 | |
| B | ASP210 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 821 |
| Chain | Residue | Details |
| A | ASP83 | electrostatic stabiliser |
| A | ASP85 | proton acceptor, proton donor |
| A | ALA99 | nucleofuge, nucleophile, proton acceptor, proton donor |
| A | ASP210 | electrostatic stabiliser |
| A | HIS212 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 821 |
| Chain | Residue | Details |
| B | ASP83 | electrostatic stabiliser |
| B | ASP85 | proton acceptor, proton donor |
| B | ALA99 | nucleofuge, nucleophile, proton acceptor, proton donor |
| B | ASP210 | electrostatic stabiliser |
| B | HIS212 | proton acceptor, proton donor |
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