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Gene_locus Report for: spops-e1vfe0

Sporosarcina psychrophila (Bacillus psychrophilus). Amino acyl peptidase

Relationship
Family|Prolyl_oligopeptidase_S9
Block| X
Position in NCBI Life Tree|Sporosarcina psychrophila
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Bacteria: N E > Terrabacteria group: N E > Firmicutes: N E > Bacilli: N E > Bacillales: N E > Planococcaceae: N E > Sporosarcina: N E > Sporosarcina psychrophila: N E


Molecular evidence
Database
No mutation
1 structure:
5L8S: The crystal structure of a cold-adapted acylaminoacyl peptidase reveals a novel quaternary architecture based on the arm-exchange mechanism
No kinetic





No Substrate
No inhibitor
1 Genbank : FN997580
1 UniProt : E1VFE0
1 Structure : 5L8S
1 UniProt : E1VFE0
1 Interpro : E1VFE0
1 Prodom : E1VFE0
1 Pfam : E1VFE0
1 PIRSF : E1VFE0
1 SUPERFAM : E1VFE0
Sequence
Graphical view for this peptide sequence: spops-e1vfe0
Colored MSA for Prolyl_oligopeptidase_S9 (raw)
MINFPKPTVEQFFRTYTITNFAVSSDEKRLVFNANLNGKMNLWAMDLPDT
YPYLFAHRDESCNFIKFDPENRYVLAGFDKDGDENYQIYAIPNEGGLPHP
LITGDASEKYYFSHLSADGKCVYYETSKENPSFLNTRIRNLETGEDRLLN
VGEVSTTELAAVSENEESFVYLRAFANTYIVGFVKMGEETFNITPDPEKV
HVAMEPVFTDNETIYFATDYDSDEMYLAKFDLTSKEFSKVLAFDGESIQS
VKWDKDNKAFYLITVKGVTDILYRYDVATDKVEECSLPVDIIEQIQVAKS
GNLYILGRSATVPHNVYQSSNGVEWKQLTNNRVLGLSPEDMVEPDIVSYT
SFDGMEIEALLFKAKPENDNGYTIFWPHGGPQSAERKMFRSMFQCFINRG
YTIFAPNFRGSTGYGSAFTKLVELDWGEGPRLDCIAGIEWLFESGFTDRN
KLFLVGGSYGGYMALLLHGRHSDYFRAVVDIFGPSDLFTFINSVPPHWKP
IMERWLGDPERDKERFIKDSPVTYLDGMVKPMLVIQGAKDPRVVKEESDQ
IVAKLKEKGRDVEYLVLEDEGHGFSKKENEIKVYSLMLAFLEKHQA
Legend This 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

MINFPKPTVEQFFRTYTITNFAVSSDEKRLVFNANLNGKMNLWAMDLPDT
YPYLFAHRDESCNFIKFDPENRYVLAGFDKDGDENYQIYAIPNEGGLPHP
LITGDASEKYYFSHLSADGKCVYYETSKENPSFLNTRIRNLETGEDRLLN
VGEVSTTELAAVSENEESFVYLRAFANTYIVGFVKMGEETFNITPDPEKV
HVAMEPVFTDNETIYFATDYDSDEMYLAKFDLTSKEFSKVLAFDGESIQS
VKWDKDNKAFYLITVKGVTDILYRYDVATDKVEECSLPVDIIEQIQVAKS
GNLYILGRSATVPHNVYQSSNGVEWKQLTNNRVLGLSPEDMVEPDIVSYT
SFDGMEIEALLFKAKPENDNGYTIFWPHGGPQSAERKMFRSMFQCFINRG
YTIFAPNFRGSTGYGSAFTKLVELDWGEGPRLDCIAGIEWLFESGFTDRN
KLFLVGGSYGGYMALLLHGRHSDYFRAVVDIFGPSDLFTFINSVPPHWKP
IMERWLGDPERDKERFIKDSPVTYLDGMVKPMLVIQGAKDPRVVKEESDQ
IVAKLKEKGRDVEYLVLEDEGHGFSKKENEIKVYSLMLAFLEKHQA


References
2 more
    Title: Structural investigation of the cold-adapted acylaminoacyl peptidase from Sporosarcina psychrophila by atomistic simulations and biophysical methods
    Papaleo E, Parravicini F, Grandori R, De Gioia L, Brocca S
    Ref: Biochimica & Biophysica Acta, 1844:2203, 2014 : PubMed

            

    Title: Reciprocal influence of protein domains in the cold-adapted acyl aminoacyl peptidase from Sporosarcina psychrophila
    Parravicini F, Natalello A, Papaleo E, De Gioia L, Doglia SM, Lotti M, Brocca S, Lotti Marina
    Ref: PLoS ONE, 8:e56254, 2013 : PubMed

            

    Title: Promiscuity, stability and cold adaptation of a newly isolated acylaminoacyl peptidase
    Brunialti EA, Gatti-Lafranconi P, Lotti Marina, Lotti M
    Ref: Biochimie, 93:1543, 2011 : PubMed

            


Other Papers


Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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