(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Actinobacteria [phylum]: NE > Actinobacteria [class]: NE > Propionibacteriales: NE > Propionibacteriaceae: NE > Cutibacterium: NE > Cutibacterium acnes: NE > Propionibacterium acnes HL110PA4: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Propionibacterium acnes JCM 18920: N, E.
Propionibacterium acnes HL110PA4: N, E.
Molecular evidence
Database
No mutation 3 structures: 6KHK, 6KHL, 6KHM No kinetic
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MALQEIEFTSHNGRDAIQAWAYEPVGTPTAVVQIIHGLGEHSRRYLHMIS ALLDAGFVVIADDHAGHGRTAMQSGVWADAGDNAAEVVISDELTLQQQLA GQFDDLPWVVFGHSWGSMIARAMATRPGTRLDGLALCGIVAQPRGFETTL DHKTLAKAMATAPTDPAPEALVAQMFDGFADRLSEDDGPTGWVARSKEVV ADHGKDKFNNFGAPMSTRFLQGLADIYAMANGDSFYATMPNIPIVLFAGS EDPAGDFGTGVKAVAERLRRDGHNVELHLYDGLRHEVHNEPESRADVESS LVTFVDRVANRRIKRSR
Reference
Title: The grease trap: Uncovering the mechanism of the hydrophobic lid in Cutibacterium acnes lipase Kim HJ, Lee BJ, Kwon AR Ref: J Lipid Res, :, 2020 : PubMed
Acne is one of the most common dermatological conditions, but the details of its pathology are unclear, and current management regimens often have adverse effects. Cutibacterium acnes is known as a major acne-associated bacterium that derives energy from lipase-mediated sebum lipid degradation. C. acnes is commensal, but lipase activity has been observed to differ among C. acnes types. For example, higher populations of the type IA strains are present in acne lesions with higher lipase activity. In the present study, we examined a conserved lipase in type IB and II, but truncated in type IA C. acnes strains. Closed, blocked, and open structures of C. acnes ATCC11828 lipases were elucidated by X-ray crystallography at 1.6-2.4 A. The closed crystal structure, which is the most common form in aqueous solution, revealed that hydrophobic lid domain shields the active site. By comparing closed, blocked, and open structures, we found that the lid domain-opening mechanisms of C. acnes lipases involve the lid-opening residues, Phe- 179 and Phe-211. To the best of our knowledge, this is the first structure-function study of C. acnes lipases, which may help shed light on the mechanisms involved in acne development and may aid in future drug design.
Cutibacterium acnes (Propionibacterium acnes) HL110PA4 Lysophospholipase
