HMM Summary Page: TIGR02037

Functionpeptidase Do
Trusted Cutoff416.20
Domain Trusted Cutoff416.20
Noise Cutoff365.80
Domain Noise Cutoff365.80
Isology Typesubfamily
EC Number3.4.21.-
HMM Length434
Mainrole CategoryProtein fate
Subrole CategoryProtein folding and stabilization
Gene Ontology TermGO:0004252: serine-type endopeptidase activity molecular_function
GO:0005515: protein binding molecular_function
GO:0006508: proteolysis biological_process
GO:0006950: response to stress biological_process
GO:0030288: outer membrane-bounded periplasmic space cellular_component
AuthorHaft DH
Entry DateOct 24 2003 10:12AM
Last ModifiedFeb 25 2011 12:36PM
CommentThis family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [2]
ReferencesDR PFAM; PF00089; trypsin DR PFAM; PF00595; PDZ domain RN [1] RM PMID: 11919638 RT Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. RA Krojer T, Garrido-Franco M, Huber R, Ehrmann M, Clausen T. RL Nature. 2002 Mar 28;416(6879):455-9. RN [2] RM PMID: 12458220 RT Crystal structure of the protease domain of a heat-shock protein HtrA from Thermotoga maritima. AU Kim DY, Kim DR, Ha SC, Lokanath NK, Lee CJ, Hwang HY, Kim KK RL J Biol Chem 2003 Feb 21;278(8):6543-51. Epub 2002 Nov 27.
Genome PropertyGenProp0928: OMP chaperone system: SurA-Skp-DegP (HMM)