Detail of EN22817871

Summary

    Name:ATL_STAAU
    FullName:Bifunctional autolysin,Atl
    Producer Organism:Staphylococcus aureus
    Sequence Length:1255
    Mass:137535
    Calculated Isoelectric Point:10.09
    Target:S. aureus
    Link:P0C5Z8
    Function:Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Cleaves the peptidoglycan connecting the daughter cells at the end of the cell division cycle, resulting in the separation of the two newly divided cells. Acts as an autolysin in penicillin-induced lysis.

Domains

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

GO term prediction

  1  GO:0008745, the N-acetylmuramoyl-L-alanine amidase activity
  2  GO:0009253, the peptidoglycan catabolic process
  3  GO:0004040, the amidase activity
  4  GO:0016787, the hydrolase activity

Structures

No structs found on enzybiotics database

Sequence

MLGVINRMAKKFNYKLPSMVALTLVGSAVTAHQVQAAETTQDQTTNKNVLDSNKVKATTE
QAKAEVKNPTQNISGTQVYQDPAIVQPKTANNKTGNAQVSQKVDTAQVNGDTRANQSATT
NNTQPVAKSTSTTAPKTNTNVTNAGYSLVDDEDDNSEHQINPELIKSAAKPAALETQYKA
AAPKAKTEATPKVTTFSASAQPRSVAATPKTSLPKYKPQVNSSINDYIRKNNLKAPKIEE
DYTSYFPKYAYRNGVGRPEGIVVHDTANDRSTINGEISYMKNNYQNAFVHAFVDGDRIIE
TAPTDYLSWGVGAVGNPRFINVEIVHTHDYASFARSMNNYADYAATQLQYYGLKPDSAEY
DGNGTVWTHYAVSKYLGGTDHADPHGYLRSHNYSYDQLYDLINEKYLIKMGKVAPWGTQF
TTTPTTPSKPTTPSKPSTGKLTVAANNGVAQIKPTNSGLYTTVYDKTGKATNEVQKTFAV
SKTATLGNQKFYLVQDYNSGNKFGWVKEGDVVYNTAKSPVNVNQSYSIKSGTKLYTVPWG
TSKQVAGSVSGSGNQTFKASKQQQIDKSIYLYGSVNGKSGWVSKAYLVDTAKPTPTPIPK
PSTPTTNNKLTVSSLNGVAQINAKNNGLFTTVYDKTGKPTKEVQKTFAVTKEASLGGNKF
YLVKDYNSPTLIGWVKQGDVIYNNAKSPVNVMQTYTVKPGTKLYSVPWGTYKQEAGAVSG
TGNQTFKATKQQQIDKSIYLFGTVNGKSGWVSKAYLAVPAAPKKAVAQPKTAVKAYTVTK
PQTTQTVSKIAQVKPNNTGIRASVYEKTAKNGAKYADRTFYVTKERAHGNETYVLLNNTS
HNIPLGWFNVKDLNVQNLGKEVKTTQKYTVNKSNNGLSMVPWGTKNQVILTGNNIAQGTF
NATKQVSVGKDVYLYGTINNRTGWVNAKDLTAPTAVKPTTSAAKDYNYTYVIKNGNGYYY
VTPNSDTAKYSLKAFNEQPFAVVKEQVINGQTWYYGKLSNGKLAWIKSTDLAKELIKYNQ
TGMTLNQVAQIQAGLQYKPQVQRVPGKWTDANFNDVKHAMDTKRLAQDPALKYQFLRLDQ
PQNISIDKINQFLKGKGVLENQGAAFNKAAQMYGINEVYLISHALLETGNGTSQLAKGAD
VVNNKVVTNSNTKYHNVFGIAAYDNDPLREGIKYAKQAGWDTVSKAIVGGAKFIGNSYVK
AGQNTLYKMRWNPAHPGTHQYATDVDWANINAKIIKGYYDKIGEVGKYFDIPQYK

BlastP to EnzyBase2

Activity

No MICs found on enzybiotics database

References

  [1]  Daum R.S.,Challapalli M.,Boyle-Vavra S.,  Resistance to autolysis in vancomycin-selected Staphylococcus aureus isolates precedes vancomycin-intermediate resistance.  Antimicrob. Agents Chemother.,2003,(47):2036-2039  [MEDLINE:22645854]
  [2]  Okagaki C.,Yamada M.,Yasojima A.,Oshida T.,Takano M.,  Modification of autolysis by synthetic peptides derived from the presumptive binding domain of Staphylococcus aureus autolysin.  Microbiol. Immunol.,2000,(44):463-472  [PubMed:10941929]
  [3]  Schneewind O.,Baba T.,  Targeting of muralytic enzymes to the cell division site of Gram-positive bacteria: repeat domains direct autolysin to the equatorial surface ring of Staphylococcus aureus.  EMBO J.,1998,(17):4639-4646  [PubMed:9707423]
  [4]  Matsumoto A.,Yamada S.,Nakashima S.,Sugai M.,Komatsuzawa H.,  Subcellular localization of the major autolysin, ATL and its processed proteins in Staphylococcus aureus.  Microbiol. Immunol.,1997,(41):469-479  [PubMed:9251058]
  [5]  Matsumoto A.,Komatsuzawa H.,Nakashima S.,Yamada S.,Sugai M.,  Localized perforation of the cell wall by a major autolysin: atl gene products and the onset of penicillin-induced lysis of Staphylococcus aureus.  J. Bacteriol.,1997,(179):2958-2962  [PubMed:9139914]
  [6]  Oshida T.,Nakashima S.,Komatsuzawa H.,Sugai M.,Yamada S.,  An autolysin ring associated with cell separation of Staphylococcus aureus.  J. Bacteriol.,1996,(178):1565-1571  [PubMed:8626282]
  [7]  Oshida T.,Hong Y.-M.,Akiyama T.,Komatsuzawa H.,Sugai M.,  Identification of endo-beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase as cluster-dispersing enzymes in Staphylococcus aureus.  J. Bacteriol.,1995,(177):1491-1496  [PubMed:7883705]