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Sequence of ATL_STAAU

EC Number:3.2.1.96

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
P0C5Z8
Staphylococcus aureus
1255
137535
Reaction
(Man)3(GlcNAc)2Asn + H2O = (Man)3GlcNAc + GlcNAc-Asn
Other sequences found for EC No. 3.2.1.96

General information:

Sequence
show sequence in normal format
>P0C5Z8|mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase|EC 3.2.1.96|Staphylococcus aureus|Swiss-Prot
MLGVINRMAKKFNYKLPSMVALTLVGSAVTAHQVQAAETTQDQTTNKNVLDSNKVKATTE
QAKAEVKNPTQNISGTQVYQDPAIVQPKTANNKTGNAQVSQKVDTAQVNGDTRANQSATT
NNTQPVAKSTSTTAPKTNTNVTNAGYSLVDDEDDNSEHQINPELIKSAAKPAALETQYKA
AAPKAKTEATPKVTTFSASAQPRSVAATPKTSLPKYKPQVNSSINDYIRKNNLKAPKIEE
DYTSYFPKYAYRNGVGRPEGIVVHDTANDRSTINGEISYMKNNYQNAFVHAFVDGDRIIE
TAPTDYLSWGVGAVGNPRFINVEIVHTHDYASFARSMNNYADYAATQLQYYGLKPDSAEY
DGNGTVWTHYAVSKYLGGTDHADPHGYLRSHNYSYDQLYDLINEKYLIKMGKVAPWGTQF
TTTPTTPSKPTTPSKPSTGKLTVAANNGVAQIKPTNSGLYTTVYDKTGKATNEVQKTFAV
SKTATLGNQKFYLVQDYNSGNKFGWVKEGDVVYNTAKSPVNVNQSYSIKSGTKLYTVPWG
TSKQVAGSVSGSGNQTFKASKQQQIDKSIYLYGSVNGKSGWVSKAYLVDTAKPTPTPIPK
PSTPTTNNKLTVSSLNGVAQINAKNNGLFTTVYDKTGKPTKEVQKTFAVTKEASLGGNKF
YLVKDYNSPTLIGWVKQGDVIYNNAKSPVNVMQTYTVKPGTKLYSVPWGTYKQEAGAVSG
TGNQTFKATKQQQIDKSIYLFGTVNGKSGWVSKAYLAVPAAPKKAVAQPKTAVKAYTVTK
PQTTQTVSKIAQVKPNNTGIRASVYEKTAKNGAKYADRTFYVTKERAHGNETYVLLNNTS
HNIPLGWFNVKDLNVQNLGKEVKTTQKYTVNKSNNGLSMVPWGTKNQVILTGNNIAQGTF
NATKQVSVGKDVYLYGTINNRTGWVNAKDLTAPTAVKPTTSAAKDYNYTYVIKNGNGYYY
VTPNSDTAKYSLKAFNEQPFAVVKEQVINGQTWYYGKLSNGKLAWIKSTDLAKELIKYNQ
TGMTLNQVAQIQAGLQYKPQVQRVPGKWTDANFNDVKHAMDTKRLAQDPALKYQFLRLDQ
PQNISIDKINQFLKGKGVLENQGAAFNKAAQMYGINEVYLISHALLETGNGTSQLAKGAD
VVNNKVVTNSNTKYHNVFGIAAYDNDPLREGIKYAKQAGWDTVSKAIVGGAKFIGNSYVK
AGQNTLYKMRWNPAHPGTHQYATDVDWANINAKIIKGYYDKIGEVGKYFDIPQYK
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
646206
Boyle-Vavra S.,Challapalli M.,Daum R.S.
Resistance to autolysis in vancomycin-selected Staphylococcus aureus isolates precedes vancomycin-intermediate resistance.
Antimicrob. Agents Chemother.
47
2036-2039
2003
646208
Sugai M.,Komatsuzawa H.,Akiyama T.,Hong Y.-M.,Oshida T.,Miyake Y.,Yamaguchi T.,Suginaka H.
Identification of endo-beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase as cluster-dispersing enzymes in Staphylococcus aureus.
J. Bacteriol.
177
1491-1496
1995
646209
Yamada S.,Sugai M.,Komatsuzawa H.,Nakashima S.,Oshida T.,Matsumoto A.,Suginaka H.
An autolysin ring associated with cell separation of Staphylococcus aureus.
J. Bacteriol.
178
1565-1571
1996
646210
Komatsuzawa H.,Sugai M.,Nakashima S.,Yamada S.,Matsumoto A.,Oshida T.,Suginaka H.
Subcellular localization of the major autolysin, ATL and its processed proteins in Staphylococcus aureus.
Microbiol. Immunol.
41
469-479
1997
646211
Sugai M.,Yamada S.,Nakashima S.,Komatsuzawa H.,Matsumoto A.,Oshida T.,Suginaka H.
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.
179
2958-2962
1997
646212
Baba T.,Schneewind O.
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.
17
4639-4646
1998
646213
Takano M.,Oshida T.,Yasojima A.,Yamada M.,Okagaki C.,Sugai M.,Suginaka H.,Matsushita T.
Modification of autolysis by synthetic peptides derived from the presumptive binding domain of Staphylococcus aureus autolysin.
Microbiol. Immunol.
44
463-472
2000