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P0C5Z8

- ATL_STAAU

UniProt

P0C5Z8 - ATL_STAAU

Protein

Bifunctional autolysin

Gene

atl

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 38 (01 Oct 2014)
      Sequence version 1 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

    Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
    Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -(Man(GlcNAc)2)Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.

    GO - Molecular functioni

    1. amidase activity Source: InterPro
    2. mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity Source: UniProtKB-EC
    3. N-acetylmuramoyl-L-alanine amidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell wall macromolecule metabolic process Source: InterPro
    2. peptidoglycan catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Protein family/group databases

    CAZyiGH73. Glycoside Hydrolase Family 73.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional autolysin
    Including the following 2 domains:
    N-acetylmuramoyl-L-alanine amidase (EC:3.5.1.28)
    Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase (EC:3.2.1.96)
    Gene namesi
    Name:atl
    Synonyms:nag
    OrganismiStaphylococcus aureus
    Taxonomic identifieri1280 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

    Subcellular locationi

    Secreted 3 Publications
    Note: Secreted, and then anchored on the cell surface at the peripheral cell wall above the completed septum (septal region), for the next cell division cycle.

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3636Sequence AnalysisAdd
    BLAST
    Chaini37 – 12551219Bifunctional autolysinPRO_0000012114Add
    BLAST

    Post-translational modificationi

    Undergoes proteolytic processing to generate the two extracellular lytic enzymes, probably at the septal region on the cell surface.

    Proteomic databases

    PRIDEiP0C5Z8.

    Interactioni

    Subunit structurei

    Oligomer; forms a ring structure at the cell surface which is important for efficient partitioning of daughter cells after cell division.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP0C5Z8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati425 – 58916511 PublicationAdd
    BLAST
    Repeati596 – 75816321 PublicationAdd
    BLAST
    Repeati770 – 93216331 PublicationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni199 – 775577N-acetylmuramoyl-L-alanine amidaseAdd
    BLAST
    Regioni776 – 1255480Endo-beta-N-acetylglucosaminidaseAdd
    BLAST

    Domaini

    The repeat domains R1, R2 and R3 are responsible for directing the proteins to the septal region.

    Sequence similaritiesi

    In the N-terminal section; belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.Curated
    In the C-terminal section; belongs to the glycosyl hydrolase 73 family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG4193.

    Family and domain databases

    Gene3Di3.40.80.10. 1 hit.
    InterProiIPR002502. Amidase_domain.
    IPR013338. Lysozyme_subfam2_dom.
    IPR002901. MGlyc_endo_b_GlcNAc_like_dom.
    [Graphical view]
    PfamiPF01510. Amidase_2. 1 hit.
    PF01832. Glucosaminidase. 1 hit.
    [Graphical view]
    SMARTiSM00644. Ami_2. 1 hit.
    SM00047. LYZ2. 1 hit.
    [Graphical view]
    SUPFAMiSSF55846. SSF55846. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0C5Z8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLGVINRMAK KFNYKLPSMV ALTLVGSAVT AHQVQAAETT QDQTTNKNVL     50
    DSNKVKATTE QAKAEVKNPT QNISGTQVYQ DPAIVQPKTA NNKTGNAQVS 100
    QKVDTAQVNG DTRANQSATT NNTQPVAKST STTAPKTNTN VTNAGYSLVD 150
    DEDDNSEHQI NPELIKSAAK PAALETQYKA AAPKAKTEAT PKVTTFSASA 200
    QPRSVAATPK TSLPKYKPQV NSSINDYIRK NNLKAPKIEE DYTSYFPKYA 250
    YRNGVGRPEG IVVHDTANDR STINGEISYM KNNYQNAFVH AFVDGDRIIE 300
    TAPTDYLSWG VGAVGNPRFI NVEIVHTHDY ASFARSMNNY ADYAATQLQY 350
    YGLKPDSAEY DGNGTVWTHY AVSKYLGGTD HADPHGYLRS HNYSYDQLYD 400
    LINEKYLIKM GKVAPWGTQF TTTPTTPSKP TTPSKPSTGK LTVAANNGVA 450
    QIKPTNSGLY TTVYDKTGKA TNEVQKTFAV SKTATLGNQK FYLVQDYNSG 500
    NKFGWVKEGD VVYNTAKSPV NVNQSYSIKS GTKLYTVPWG TSKQVAGSVS 550
    GSGNQTFKAS KQQQIDKSIY LYGSVNGKSG WVSKAYLVDT AKPTPTPIPK 600
    PSTPTTNNKL TVSSLNGVAQ INAKNNGLFT TVYDKTGKPT KEVQKTFAVT 650
    KEASLGGNKF YLVKDYNSPT LIGWVKQGDV IYNNAKSPVN VMQTYTVKPG 700
    TKLYSVPWGT YKQEAGAVSG TGNQTFKATK QQQIDKSIYL FGTVNGKSGW 750
    VSKAYLAVPA APKKAVAQPK TAVKAYTVTK PQTTQTVSKI AQVKPNNTGI 800
    RASVYEKTAK NGAKYADRTF YVTKERAHGN ETYVLLNNTS HNIPLGWFNV 850
    KDLNVQNLGK EVKTTQKYTV NKSNNGLSMV PWGTKNQVIL TGNNIAQGTF 900
    NATKQVSVGK DVYLYGTINN RTGWVNAKDL TAPTAVKPTT SAAKDYNYTY 950
    VIKNGNGYYY VTPNSDTAKY SLKAFNEQPF AVVKEQVING QTWYYGKLSN 1000
    GKLAWIKSTD LAKELIKYNQ TGMTLNQVAQ IQAGLQYKPQ VQRVPGKWTD 1050
    ANFNDVKHAM DTKRLAQDPA LKYQFLRLDQ PQNISIDKIN QFLKGKGVLE 1100
    NQGAAFNKAA QMYGINEVYL ISHALLETGN GTSQLAKGAD VVNNKVVTNS 1150
    NTKYHNVFGI AAYDNDPLRE GIKYAKQAGW DTVSKAIVGG AKFIGNSYVK 1200
    AGQNTLYKMR WNPAHPGTHQ YATDVDWANI NAKIIKGYYD KIGEVGKYFD 1250
    IPQYK 1255
    Length:1,255
    Mass (Da):137,535
    Last modified:January 15, 2008 - v1
    Checksum:i7257DD87168AAE7D
    GO

    Sequence cautioni

    The sequence AAP44166.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti932 – 9321A → R in BAA22600. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF537210 Genomic DNA. Translation: AAP44166.1. Different initiation.
    D42078 Genomic DNA. Translation: BAA22600.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF537210 Genomic DNA. Translation: AAP44166.1 . Different initiation.
    D42078 Genomic DNA. Translation: BAA22600.1 .

    3D structure databases

    ProteinModelPortali P0C5Z8.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH73. Glycoside Hydrolase Family 73.

    Proteomic databases

    PRIDEi P0C5Z8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG4193.

    Family and domain databases

    Gene3Di 3.40.80.10. 1 hit.
    InterProi IPR002502. Amidase_domain.
    IPR013338. Lysozyme_subfam2_dom.
    IPR002901. MGlyc_endo_b_GlcNAc_like_dom.
    [Graphical view ]
    Pfami PF01510. Amidase_2. 1 hit.
    PF01832. Glucosaminidase. 1 hit.
    [Graphical view ]
    SMARTi SM00644. Ami_2. 1 hit.
    SM00047. LYZ2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55846. SSF55846. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Resistance to autolysis in vancomycin-selected Staphylococcus aureus isolates precedes vancomycin-intermediate resistance."
      Boyle-Vavra S., Challapalli M., Daum R.S.
      Antimicrob. Agents Chemother. 47:2036-2039(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: IL-A.
    2. "Novel cytotoxin in a clinical isolate of methicillin-resistant S. aureus: cloning, sequencing and expression."
      Kamitani S., Minamide W., Yutsudo T., Noda M.
      Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 775-1255.
    3. "Identification of endo-beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase as cluster-dispersing enzymes in Staphylococcus aureus."
      Sugai M., Komatsuzawa H., Akiyama T., Hong Y.-M., Oshida T., Miyake Y., Yamaguchi T., Suginaka H.
      J. Bacteriol. 177:1491-1496(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447.
    4. "An autolysin ring associated with cell separation of Staphylococcus aureus."
      Yamada S., Sugai M., Komatsuzawa H., Nakashima S., Oshida T., Matsumoto A., Suginaka H.
      J. Bacteriol. 178:1565-1571(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUBUNIT.
      Strain: ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447.
    5. "Subcellular localization of the major autolysin, ATL and its processed proteins in Staphylococcus aureus."
      Komatsuzawa H., Sugai M., Nakashima S., Yamada S., Matsumoto A., Oshida T., Suginaka H.
      Microbiol. Immunol. 41:469-479(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
      Strain: ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447.
    6. "Localized perforation of the cell wall by a major autolysin: atl gene products and the onset of penicillin-induced lysis of Staphylococcus aureus."
      Sugai M., Yamada S., Nakashima S., Komatsuzawa H., Matsumoto A., Oshida T., Suginaka H.
      J. Bacteriol. 179:2958-2962(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
      Strain: ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447.
    7. "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."
      Baba T., Schneewind O.
      EMBO J. 17:4639-4646(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE OF REPEATS IN LOCALIZATION AT THE SEPTAL REGION.
      Strain: OS2.
    8. "Modification of autolysis by synthetic peptides derived from the presumptive binding domain of Staphylococcus aureus autolysin."
      Takano M., Oshida T., Yasojima A., Yamada M., Okagaki C., Sugai M., Suginaka H., Matsushita T.
      Microbiol. Immunol. 44:463-472(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: BINDING TO THE BACTERIAL CELL WALL.

    Entry informationi

    Entry nameiATL_STAAU
    AccessioniPrimary (citable) accession number: P0C5Z8
    Secondary accession number(s): O32391
    , P0C1R4, P52081, Q7WTC6, Q7WY94, Q7WY95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 38 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Multifunctional enzyme

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3