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Q6GAG0

- ATL_STAAS

UniProt

Q6GAG0 - ATL_STAAS

Protein

Bifunctional autolysin

Gene

atl

Organism
Staphylococcus aureus (strain MSSA476)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      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 By similarity.By similarity

    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
    Ordered Locus Names:SAS0988
    OrganismiStaphylococcus aureus (strain MSSA476)
    Taxonomic identifieri282459 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000002201: Chromosome

    Subcellular locationi

    Secreted By similarity
    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.By similarity

    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 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 12501221Bifunctional autolysinPRO_0000045477Add
    BLAST

    Post-translational modificationi

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

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi282459.SAS0988.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6GAG0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati425 – 5831591Add
    BLAST
    Repeati590 – 7521632Add
    BLAST
    Repeati764 – 9261633Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni199 – 769571N-acetylmuramoyl-L-alanine amidaseAdd
    BLAST
    Regioni770 – 1250481Endo-beta-N-acetylglucosaminidaseAdd
    BLAST

    Domaini

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

    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.
    HOGENOMiHOG000279968.
    KOiK13714.
    OMAiKSGWISK.
    OrthoDBiEOG6GXTN7.

    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.

    Q6GAG0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKKFNYKLP SMVALTLVGS AVTAHQVQAA ETTQDQTTNK NVLDSNKVKA     50
    TTEQAKAEVK NPTQNISGTQ VYQDPAIVQP KTANNKTGNA QVSQKVDTAQ 100
    VNGDTRANQS ATTNNTQPVA KSTSTTAPKT NTNVTNAGYS LVDDEDDNSE 150
    NQINPELIKS AAKPAALETQ YKAAAPKAAT TSAPKAKTEA TPKVTTFSAS 200
    AQPRSVAATP KTSLPKYKPQ VNSSINDYIR KNNLKAPKIE EDYTSYFPKY 250
    AYRNGVGRPE GIVVHDTAND RSTINGEISY MKNNYQNAFV HAFVDGDRII 300
    ETAPTDYLSW GVGAVGNPRF INVEIVHTHD YASFARSMNN YADYAATQLQ 350
    YYGLKPDSAE YDGNGTVWTH YAVSKYLGGT DHADPHGYLR SHNYSYDQLY 400
    DLINEKYLIK MGKVAPWGTQ STTTPTTPSK PSTGKLTVAA NNGVAQIKPT 450
    NSGLYTTVYD KTGKATNEVQ KTFAVSKTAT LGNQKFYLVQ DYNSGNKFGW 500
    VKEGDVVYNT AKSPVNVNQS YSIKPGTKLY TVPWGTSKQV AGSVSGSGNQ 550
    TFKASKQQQI DKSIYLYGSV NGKSGWVSKA YLVDTAKPTP TPTPKPSTPT 600
    TNNKLTVSSL NGVAQINAKN NGLFTTVYDK TGKPTKEVQK TFAVTKEASL 650
    GGNKFYLVKD YNSPTLIGWV KQGDVIYNNA KSPVNVMQTY TVKPGTKLYS 700
    VPWGTYKQEA GAVSGTGNQT FKATKQQQID KSIYLFGTVN GKSGWVSKAY 750
    LAVPAAPKKA VAQPKTAVKA YTVTKPQTTQ TVSKIAQVKP NNTGIRASVY 800
    EKTAKNGAKY ADRTFYVTKE RAHGNETYVL LNNTSHNIPL GWFNVKDLNV 850
    QNLGKEVKTT QKYTVNKSNN GLSMVPWGTK NQVILTGNNI AQGTFNATKQ 900
    VSVGKDVYLY GTINNRTGWV NAKDLTAPTA VKPTTSAAKD YNYTYVIKNG 950
    NGYYYVTPNS DTAKYSLKAF NEQPFAVVKE QVINEQTWYY GKLSNGKLAW 1000
    IKSTDLAKEL IKYNQTGMTL NQVAQIQAGL QYKPQVQRVP GKWTDANFND 1050
    VKHAMDTKRL AQDPALKYQF LRLDQPQNIS IDKINQFLKG KGVLENQGAA 1100
    FNKAAQMYGI NEVYLISHAL LETGNGTSQL AKGADVVNNK VVTNSNTKYH 1150
    NVFGIAAYDN DPLREGIKYA KQAGWDTVSK AIVGGAKFIG NSYVKAGQNT 1200
    LYKMRWNPAH PGTHQYATDI DWANINAKII KGYYDKIGEV GKYFDIPQYK 1250
    Length:1,250
    Mass (Da):136,868
    Last modified:July 19, 2004 - v1
    Checksum:iD8C43606B9374D96
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX571857 Genomic DNA. Translation: CAG42763.1.
    RefSeqiWP_001074541.1. NC_002953.3.
    YP_043113.1. NC_002953.3.

    Genome annotation databases

    GeneIDi2862752.
    KEGGisas:SAS0988.
    PATRICi19551413. VBIStaAur96780_1024.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX571857 Genomic DNA. Translation: CAG42763.1 .
    RefSeqi WP_001074541.1. NC_002953.3.
    YP_043113.1. NC_002953.3.

    3D structure databases

    ProteinModelPortali Q6GAG0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 282459.SAS0988.

    Protein family/group databases

    CAZyi GH73. Glycoside Hydrolase Family 73.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2862752.
    KEGGi sas:SAS0988.
    PATRICi 19551413. VBIStaAur96780_1024.

    Phylogenomic databases

    eggNOGi COG4193.
    HOGENOMi HOG000279968.
    KOi K13714.
    OMAi KSGWISK.
    OrthoDBi EOG6GXTN7.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MSSA476.

    Entry informationi

    Entry nameiATL_STAAS
    AccessioniPrimary (citable) accession number: Q6GAG0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 66 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

    Complete proteome, Multifunctional enzyme

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3