| Tag | Content |
|---|
| CPLM ID | CPLM-007106 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Periplasmic pH-dependent serine endoprotease DegQ |
Protein Synonyms/Alias | Protease Do |
Gene Name | degQ |
Gene Synonyms/Alias | hhoA; b3234; JW3203 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 161 | IAIADSDKLRVGDFA | 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 | DegQ could degrade transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for a beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable to be cleaved, thereby preventing non-specific proteolysis of folded proteins. DegQ can substitute for the periplasmic protease DegP. |
Sequence Annotation | DOMAIN 258 349 PDZ 1.
DOMAIN 355 447 PDZ 2.
REGION 212 214 Substrate binding.
REGION 230 234 Substrate binding.
REGION 269 273 Substrate binding.
ACT_SITE 109 109 Charge relay system (Potential).
ACT_SITE 139 139 Charge relay system (Potential).
ACT_SITE 214 214 Charge relay system (Potential).
BINDING 59 59 Substrate (By similarity).
BINDING 109 109 Substrate (By similarity).
BINDING 139 139 Substrate (By similarity).
BINDING 212 212 Substrate; via amide nitrogen. |
Keyword | 3D-structure; Complete proteome; Direct protein sequencing; Hydrolase; Periplasm; Protease; Reference proteome; Repeat; Serine protease; Signal; Stress response. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 455 AA |
Protein Sequence | MKKQTQLLSA LALSVGLTLS ASFQAVASIP GQVADQAPLP SLAPMLEKVL PAVVSVRVEG 60
TASQGQKIPE EFKKFFGDDL PDQPAQPFEG LGSGVIINAS KGYVLTNNHV INQAQKISIQ 120
LNDGREFDAK LIGSDDQSDI ALLQIQNPSK LTQIAIADSD KLRVGDFAVA VGNPFGLGQT 180
ATSGIVSALG RSGLNLEGLE NFIQTDASIN RGNSGGALLN LNGELIGINT AILAPGGGSV 240
GIGFAIPSNM ARTLAQQLID FGEIKRGLLG IKGTEMSADI AKAFNLDVQR GAFVSEVLPG 300
SGSAKAGVKA GDIITSLNGK PLNSFAELRS RIATTEPGTK VKLGLLRNGK PLEVEVTLDT 360
STSSSASAEM ITPALEGATL SDGQLKDGGK GIKIDEVVKG SPAAQAGLQK DDVIIGVNRD 420
RVNSIAEMRK VLAAKPAIIA LQIVRGNESI YLLMR 455 |
Gene Ontology | GO:0071575; C:integral to external side of plasma membrane; ISA:EcoliWiki. GO:0042597; C:periplasmic space; IDA:UniProtKB. GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB. GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:UniProtKB. GO:0006950; P:response to stress; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |