Detail of EN44352156


Summary

    Name:B5L7M5_STALU
    FullName:bacteriocin
    Producer Organism:Staphylococcus lugdunensis
    Sequence Length:1278
    Mass:140408
    Calculated Isoelectric Point:10.03
    Target:S. aureus
    Link:B5L7M5
    Function:null

Domains

InterPro

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1278

  1  []:IPR002502,Amidase_domain
  2  []:IPR013338,Lysozyme_dom_subfam2
  3  []:IPR002901,Mano_Glyc_endo_b_GlcNAc

Structures

    No structs found on enzybiotics database

Sequence

MTKKFNLKLPSMLALSLFGATLTAQHAHAAESTTDQSTNKNVIDQQNDVVKANKAKKAVS
NAAQNVSGVQAYHNPSLVKSSDTTSGQTYDAKLDTLTDQTHAQTSQQQNAKNQQQTKTAS
QQQTEQAKQQAATTTARQDAQTYNQNAAQSNKTKQQANANVSTTTKQQATQAANTSLKSQ
NNVETTNQKAVSTQNTAQKQSNSVTTYQGRVGGMGSSATKAQTAKSTSGFTGFRKAVSTY
KATSSLPKYKPQVNSSINDYIRKNNIQAPKIEEDYTSYFPKYGYRNGVGKPEGIVVHDTA
NDNSTIDGEIAFMKRNYNSAFVHAFVDGNRIVETTPTDYLSWGAGPNANNRFINVEIVHT
HDYASFARSMNNYADYAATQLQYYGLKPDSAENDGNGTVWTHYAVSHWLGGTDHTDPHAY
LQSHGYSYAELYDLINEKYLIKTGQVAPWGTSSSTDPSKPSTPTNPGKLKVSTNSGVAQI
KPSNSGLFVTVYDKTGKKTNQVQKTLSVTKQATLGNDKFYLVNDYNTGKTFGWVKQGDVV
YNTAKSPVKVNQSYSVKPGTKFYTVPWGTPSQVAGTVSGSSNQTFKATKSQMISTATYLY
GTVNGKSGWISKAYLSAINNDSSSTKPSTDNSKKLNVSNLTNTLGQVSTDTKGAYTTVYD
KTVKENPLLSGRTFSINKKATLNNKTYYLLADFNGNVTRGWVPADQVTIAQSTPTKVKKQ
YNVKGNANIYYVPWSKDNQVVAKTPKNGGQFNSIDQLTVGKETYLHGSINHQWGWIKQSD
VATPAKSAVRTLAVKTTPTTKVTTASTTQKAASAVQTVNKIGQVKVNNSGIRTSVYDKAG
KNAAKYGNRTFTITKQRTVGNNTYVLLTNHNQNTPIGWYNIKDVNIKNYGTENRVTNQYR
VNSKNQGLYSIPWGTTQQQLEQANSLAQRTFKATKSVTIDGVKYLYGSVNNKLGWIAEKD
LTSLSSNTAYNYTFVINNKDSYFYDDLSLKTKHLLSPYYEQTFIVAKYQVVNGVKWYYGQ
FSDGQFAWINENDLSQELIKYSATGMTLDAAAQLQMSLPYPPQSYVGPSKWRNATLAEVK
SAMDTSKFVNDSVQKYQFLQLDQPQYLSVASLNNLLKGCGVLENQGQAFSQAAKQYGLNE
IYLISHALLETGRGQSQLAKGANIVNGKLSTTTAIKYHNVFGIGAYDSNPVFDGITYAKK
AGWDSVEKAIVGGAQFIGQSYVKAGQNTLYKMRWNPENPGKHQYATGVTWASVNAQNMKN
FYDTIHESGKYFDVPTYK
  BlastP to EnzyBase2

Activity

    No MICs found on enzybiotics database

References

  [1]  Gibert L.,Courtin P.,Biswas R.,Camiade E.,Bourgeois I.,  Characterization of AtlL, a bifunctional autolysin of Staphylococcus lugdunensis with N-acetylglucosaminidase and N-acetylmuramoyl-l-alanine amidase activities.  FEMS Microbiol. Lett.,2009,(290):105-113  [PubMed:19025571]