| General Information |
| MoonProt ID | 454 |
| First appeared in release | 3.0 |
| Name(s) | OMPT
Protease 7
Recommended name:
Protease 7 (EC:3.4.23.49)
Alternative name(s):
Omptin
Outer membrane protein 3B
Protease A
Protease VII |
| UniProt ID | P09169 |
| GO terms | GO:0004190 aspartic-type endopeptidase activity
GO:0006508 proteolysis
GO:0009279 cell outer membrane
GO:0004175 endopeptidase activity
GO:0004190 aspartic-type endopeptidase activity
GO:0008233 peptidase activity
GO:0016787 hydrolase activity
GO:0016020 membrane
GO:0016021 integral component of membrane
GO:0004175 endopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0031230 intrinsic component of cell outer membrane |
| Organisms for which functions have been demonstrated | Escherichia coli (Gram negative bacterium) |
| Sequence length | 317 amino acids |
| FASTA sequence | >sp|P09169|OMPT_ECOLI Protease 7 OS=Escherichia coli (strain K12) OX=83333 GN=ompT PE=1 SV=1
MRAKLLGIVLTTPIAISSFASTETLSFTPDNINADISLGTLSGKTKERVYLAEEGGRKVSQLDWKFNNAAIIKGAINWDLMPQISIGAAGWTTLGSRGGNMVDQDWMDSSNPGTWTDESRHPDTQLNYANEFDLNIKGWLLNEPNYRLGLMAGYQESRYSFTARGGSYIYSSEEGFRDDIGSFPNGERAIGYKQRFKMPYIGLTGSYRYEDFELGGTFKYSGWVESSDNDEHYDPGKRITYRSKVKDQNYYSVAVNAGYYVTPNAKVYVEGAWNRVTNKKGNTSLYDHNNNTSDYSKNGAGIENYNFITTAGLKYTF |
| Structure Information |
| PDB ID | 1I78 |
| Quaternary structure | NA |
| SCOP | class 1000001 All beta proteins; |
| CATH | NA |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
moonID_454_uniID_P09169 is 317 residues long, with 0 residues (0.00%) predicted as disordered.The protein has 0 short (< 30 residues) disorder segments and 0 long (>= 30 residues) disorder segments. |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | Protease |
| References for function | Stumpe S, Schmid R, Stephens DL, Georgiou G, Bakker EP. Identification of OmpT as the protease that hydrolyzes the antimicrobial peptide protamine before it enters growing cells of Escherichia coli. J Bacteriol. 1998 Aug;180(15):4002-6. doi: 10.1128/JB.180.15.4002-4006.1998. PMID: 9683502; PMCID: PMC107389.
Sugimura K, Higashi N. A novel outer-membrane-associated protease in Escherichia coli. J Bacteriol. 1988 Aug;170(8):3650-4. doi: 10.1128/jb.170.8.3650-3654.1988. PMID: 3136144; PMCID: PMC211340. |
| E.C. number | 3.4.23.49 |
| Location of functional site(s) | NA |
| Cellular location of function | external surface of the outer membrane |
| Comments | NA |
| Function 2 |
| Function description | Adhesin to human cells |
| References for function | NA |
| E.C. number | NA |
| Location of functional site(s) | Outer membrane |
| Cellular location of function | NA |
| Comments | NA |