Gene_Locus Report

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Gene_locus Report for: fratt-q5ni32

Francisella tularensis (subsp. tularensis)(and subsp. holarctica (strain LVS)) carboxylesterase/phospholipase family protein (EC 3.1.1.-)

Relationship
Family|LYsophospholipase_carboxylesterase
Block| X
Position in NCBI Life Tree|Francisella tularensis
(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 > Proteobacteria: N E > Gammaproteobacteria: N E > Thiotrichales: N E > Francisellaceae: N E > Francisella: N E > Francisella tularensis: N E
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


Molecular evidence
Database
No mutation
1 structure:
4F21: Crystal structure of carboxylesterase/phospholipase family protein from Francisella tularensis
No kinetic





No Substrate
1 inhbitor:
2-allyl-4-oxocyclobutyl-4-methylbenzenesulfonamide
2 Genbank : AJ749949, AM233362
1 UniProt : Q5NI32
1 Structure : 4F21
1 UniProt : Q5NI32
1 Interpro : Q5NI32
1 Pfam : Q5NI32
1 PIRSF : Q5NI32
1 SUPERFAM : Q5NI32
Sequence
Graphical view for this peptide sequence: fratt-q5ni32
Colored MSA for LYsophospholipase_carboxylesterase (raw)
MNYELMEPAKQARFCVIWLHGLGADGHDFVDIVNYFDVSLDEIRFIFPHA
DIIPVTINMGMQMRAWYDIKSLDANSLNRVVDVEGINSSIAKVNKLIDSQ
VNQGIASENIILAGFSQGGIIATYTAITSQRKLGGIMALSTYLPAWDNFK
GKITSINKGLPILVCHGTDDQVLPEVLGHDLSDKLKVSGFANEYKHYVGM
QHSVCMEEIKDISNFIAKTFKI
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

MNYELMEPAKQARFCVIWLHGLGADGHDFVDIVNYFDVSLDEIRFIFPHA
DIIPVTINMGMQMRAWYDIKSLDANSLNRVVDVEGINSSIAKVNKLIDSQ
VNQGIASENIILAGFSQGGIIATYTAITSQRKLGGIMALSTYLPAWDNFK
GKITSINKGLPILVCHGTDDQVLPEVLGHDLSDKLKVSGFANEYKHYVGM
QHSVCMEEIKDISNFIAKTFKI


References
    Title: A dynamic loop provides dual control over the catalytic and membrane binding activity of a bacterial serine hydrolase
    Smith MA, Phillips WK, Rabin PL, Johnson RJ
    Ref: Biochimica & Biophysica Acta, 1866:925, 2018 : PubMed

            

    Title: Large-scale structural rearrangement of a serine hydrolase from Francisella tularensis facilitates catalysis
    Filippova EV, Weston LA, Kuhn ML, Geissler B, Gehring AM, Armoush N, Adkins CT, Minasov G, Dubrovska I and Johnson RJ <6 more author(s)>
    Ref: Journal of Biological Chemistry, 288:10522, 2013 : PubMed

            

    Title: The complete genome sequence of Francisella tularensis, the causative agent of tularemia
    Larsson P, Oyston PC, Chain P, Chu MC, Duffield M, Fuxelius HH, Garcia E, Halltorp G, Johansson D and Titball RW <17 more author(s)>
    Ref: Nat Genet, 37:153, 2005 : 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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