| General Information |
| MoonProt ID | 124 |
| First appeared in release | 1.0 |
| Name(s) | Periplasmic serine endoprotease DegP
Heat shock protein DegP
Protease Do
htrA
ptd
Gene Name: degP
|
| UniProt ID | P0C0V0 (DEGP_ECOLI), Reviewed |
| GO terms | GO:0006457 protein folding
GO:0006508 proteolysis
GO:0006515 misfolded or incompletely synthesized protein catabolic process
GO:0006950 response to stress
GO:0006979 response to oxidative stress
GO:0009266 response to temperature stimulus
GO:0003824 catalytic activity
GO:0004252 serine-type endopeptidase activity
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0008236 serine-type peptidase activity
GO:0016787 hydrolase activity
GO:0042802 identical protein binding
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0030288 outer membrane-bounded periplasmic space |
| Organisms for which functions have been demonstrated | Escherichia coli (strain K12) (Gram negative bacterium) |
| Sequence length | 474 |
| FASTA sequence | >sp|P0C0V0|DEGP_ECOLI Periplasmic serine endoprotease DegP OS=Escherichia coli (strain K12) GN=degP PE=1 SV=1
MKKTTLALSALALSLGLALSPLSATAAETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEGSPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ
|
| Structure Information |
| PDB ID | 3OTP 4A8D 3MH4 3MH5 |
| Quaternary structure | |
| SCOP | NA |
| CATH | 2.40.10.120, 2.30.42.10 |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | 1-9, 63-109, 381-399 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | peptidase at higher temperatures. |
| References for function | Krojer, Tobias et. al. "Crystal Structure of DegP (HtrA) Reveals a New Protease-chaperone Machine." Max-Planck-Institut fur Biochemie, Abteilung Strukturforschung, Germany. Cardiff University, School of Biosciences, Museum Avenue, Cardiff CF10 3US.
PMID: 11919638
|
| E.C. number | 3.4.21.107 |
| Location of functional site(s) | |
| Cellular location of function | |
| Comments | |
| Function 2 |
| Function description | chaperone at low temperatures |
| References for function | Krojer, Tobias et. al. "Crystal Structure of DegP (HtrA) Reveals a New Protease-chaperone Machine." Max-Planck-Institut fur Biochemie, Abteilung Strukturforschung, Germany. Cardiff University, School of Biosciences, Museum Avenue, Cardiff CF10 3US.
PMID: 11919638
|
| E.C. number | N/A |
| Location of functional site(s) | |
| Cellular location of function | |
| Comments | |