(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 > Firmicutes: NE > Bacilli: NE > Bacillales: NE > Paenibacillaceae: NE > Paenibacillus: NE > Paenibacillus odorifer: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acid 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.) Paenibacillus sp. VTT E-133280: N, E.
Molecular evidence
Database
No mutation 1 structure: 6TJ2: Structure of alpha/beta-hydrolase from Paenibacillus species homologue to Tobacco Salicylic Acid Binding Protein 2 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 MKSIHIKIVLALCISIFTIMGLQPLNQHSTVAAANHKSSTKQTPLTFVLI HGSWATAGFWDETASELRKLGHTVYTPEYAGHGADKNNNVTHEQITKSVV DYIKQKDLKDFILLGHSFGGSVIQTVSQQVPDRIKRIVFFDAFAPLDGQS VADQFPAESLKSFEQLRDASGNNTITLPFPLFRDTFVNTASLAQAQAFYK QAPPEPATPLFEKLDLKKFYSLQIPKSYLYLTEDTAIPQGPYGFHPTQSS HLGVFRFIEGKGDHMTTVRTEPKMMAELMVKAGRD
Reference
Title: Extracellular alpha/beta-hydrolase from Paenibacillus species shares structural and functional homology to Tobacco Salicylic Acid Binding Protein 2 Wilkinson RC, Rahman Pour R, Jamshidi S, Fulop V, Bugg TDH Ref: J Struct Biol, :107496, 2020 : PubMed
An alpha/ beta hydrolase annotated as a putative salicylate esterase within the genome of a species of Paenibacillus previously identified from differential and selective growth on Kraft lignin was structurally and functionally characterised. Feruloyl esterases are key to the degradation of lignin in several bacterial species and although this activity was investigated, no such activity was observed. The crystal structure of the Paenibacillus esterase, here denoted as PnbE, was determined at 1.32 A resolution, showing high similarity to Nicotiana tabacum salicylic acid binding protein 2 from the protein database. Structural similarities between these two structures across the core domains and key catalytic residues were observed, with superposition of catalytic residues giving an RMSD of 0.5 A across equivalent Calpha atoms. Conversely, the cap domains of PnbE and Nicotiana tabacum SABP2 showed greater divergence with decreased flexibility in the PnbE cap structure. Activity of PnbE as a putative methyl salicylate esterase was supported with binding studies showing affinity for salicylic acid and functional studies showing methyl salicylate esterase activity. We hypothesise that this activity could enrich Paenibacillus sp. within the rhizosphere by increasing salicylic acid concentrations within the soil.
Paenibacillus odorifer; Paenibacillus sp. Alpha/beta hydrolase
