UniProt Accession

 DEGP_ECOLI; P0C0V0; P09376; P15724 

Genbank Protein ID

 M36536; X12457; U70214; U00096; AP009048; M29955; M31772 

Genbank Nucleotide ID

 AAA23994.1; CAA30997.1; AAB08591.1; AAC73272.1; BAB96738.1; AAA23717.1; AAA23680.1 

Protein Name

 Periplasmic serine endoprotease DegP 

Protein Synonyms/Alias

 Heat shock protein DegP; Protease Do 

Gene Name

 degP 

Gene Synonyms/Alias

 htrA; ptd; b0161; JW0157 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
287	MVEYGQVKRGELGIM	acetylation	[1]
304	ELNSELAKAMKVDAQ	acetylation	[1]
342	VITSLNGKPISSFAA	acetylation	[1]
454	LRKVLDSKPSVLALN	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 

Functional Description

 DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile- Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non- specific proteolysis of folded proteins. Its proteolytic activity is essential for the survival of cells at elevated temperatures. It can degrade IciA, ada, casein, globin and PapA. DegP shares specificity with DegQ. DegP is also involved in the biogenesis of partially folded outer-membrane proteins (OMP). 

Sequence Annotation

 DOMAIN 280 371 PDZ 1.
 DOMAIN 377 466 PDZ 2.
 REGION 234 236 Substrate binding.
 REGION 252 256 Substrate binding.
 REGION 291 295 Substrate binding.
 ACT_SITE 131 131 Charge relay system.
 ACT_SITE 161 161 Charge relay system (Potential).
 ACT_SITE 236 236 Charge relay system.
 BINDING 58 58 Substrate.
 BINDING 131 131 Substrate.
 BINDING 161 161 Substrate.
 DISULFID 83 95  

Keyword

 3D-structure; Cell inner membrane; Cell membrane; Complete proteome; Direct protein sequencing; Disulfide bond; Hydrolase; Membrane; Protease; Reference proteome; Repeat; Serine protease; Signal; Stress response. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 474 AA 

Protein Sequence

Gene Ontology

 GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoliWiki.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0004252; F:serine-type endopeptidase activity; IDA:EcoliWiki.
 GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IMP:EcoliWiki.
 GO:0006457; P:protein folding; IMP:EcoliWiki.
 GO:0006979; P:response to oxidative stress; IEP:EcoliWiki.
 GO:0009266; P:response to temperature stimulus; IEP:EcoliWiki. 

Interpro

 IPR001478; PDZ.
 IPR011782; Pept_S1C_Do.
 IPR001940; Peptidase_S1C.
 IPR009003; Trypsin-like_Pept_dom. 

Pfam

 PF00595; PDZ 

SMART

 SM00228; PDZ 

PROSITE

 PS50106; PDZ 

PRINTS

 PR00834; PROTEASES2C.