General Information |
MoonProt ID | 198 |
First appeared in release | 1.0 |
Name(s) | DegQ
Periplasmic pH-dependent serine endoprotease DegQ
Protease Do
Gene Name:degQ |
UniProt ID | P39099 (DEGQ_ECOLI), Reviewed |
GO terms | GO:0006508 proteolysis
GO:0006950 response to stress
GO:0051603 proteolysis involved in cellular protein catabolic process
GO:0003824 catalytic activity
GO:0004252 serine-type endopeptidase activity
GO:0008233 peptidase activity
GO:0008236 serine-type peptidase activity
GO:0016787 hydrolase activity
GO:0042597 periplasmic space
GO:0071575 integral component of external side of plasma membrane |
Organisms for which functions have been demonstrated | Escherichia coli (Gram negative bacterium) |
Sequence length | 455 |
FASTA sequence | >sp|P39099|DEGQ_ECOLI Periplasmic pH-dependent serine endoprotease DegQ OS=Escherichia coli (strain K12) GN=degQ PE=1 SV=1
MKKQTQLLSALALSVGLTLSASFQAVASIPGQVADQAPLPSLAPMLEKVLPAVVSVRVEGTASQGQKIPEEFKKFFGDDLPDQPAQPFEGLGSGVIINASKGYVLTNNHVINQAQKISIQLNDGREFDAKLIGSDDQSDIALLQIQNPSKLTQIAIADSDKLRVGDFAVAVGNPFGLGQTATSGIVSALGRSGLNLEGLENFIQTDASINRGNSGGALLNLNGELIGINTAILAPGGGSVGIGFAIPSNMARTLAQQLIDFGEIKRGLLGIKGTEMSADIAKAFNLDVQRGAFVSEVLPGSGSAKAGVKAGDIITSLNGKPLNSFAELRSRIATTEPGTKVKLGLLRNGKPLEVEVTLDTSTSSSASAEMITPALEGATLSDGQLKDGGKGIKIDEVVKGSPAAQAGLQKDDVIIGVNRDRVNSIAEMRKVLAAKPAIIALQIVRGNESIYLLMR
|
Structure Information |
PDB ID | 4A8A,
4A8B,
4A8C,
4A9G,
3STJ |
Quaternary structure | |
SCOP | NA |
CATH | NA |
TM Helix Prediction | (7-29) signal sequence |
DisProt Annotation | Not in DisProt |
Predicted Disorder Regions | 1-10, 29-35, 62-67, 79-88, 360-382 |
Connections to Disease |
OMIM ID | |
Function 1 |
Function description | peptidase, enzyme
|
References for function | Sawa J, Malet H, Krojer T, Canellas F, Ehrmann M, Clausen T. Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope. J Biol Chem. 2011 Sep 2. PMID: 21685389 |
E.C. number | 3.4.21.107 |
Location of functional site(s) | |
Cellular location of function | Periplasm |
Comments | |
Function 2 |
Function description | chaperone, aids in folding of proteins
|
References for function | Malet H, Canellas F, Sawa J, Yan J, Thalassinos K, Ehrmann M, Clausen T, Saibil HR. Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Nat Struct Mol Biol. 2012 Jan 15. PMID: 22245966 |
E.C. number | N/A |
Location of functional site(s) | |
Cellular location of function | Periplasm |
Comments | |