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Q2FZK7

- ATL_STAA8

UniProt

Q2FZK7 - ATL_STAA8

Protein

Bifunctional autolysin

Gene

atl

Organism
Staphylococcus aureus (strain NCTC 8325)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (21 Mar 2006)
      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

    Enzyme and pathway databases

    BioCyciSAUR93061:GIWJ-959-MONOMER.

    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:SAOUHSC_00994
    OrganismiStaphylococcus aureus (strain NCTC 8325)
    Taxonomic identifieri93061 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000008816: 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 – 12561227Bifunctional autolysinPRO_0000247668Add
    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

    STRINGi93061.SAOUHSC_00994.

    Structurei

    Secondary structure

    1
    1256
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi224 – 2318
    Beta strandi239 – 2413
    Beta strandi261 – 2666
    Helixi274 – 28411
    Turni285 – 2873
    Beta strandi291 – 2944
    Beta strandi299 – 3013
    Beta strandi310 – 3123
    Helixi313 – 3164
    Turni317 – 3193
    Beta strandi320 – 3256
    Helixi331 – 35222
    Turni360 – 3623
    Beta strandi365 – 3695
    Helixi370 – 3767
    Helixi386 – 3916
    Helixi396 – 41015

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4KNKX-ray1.12A/B198-421[»]
    4KNLX-ray1.55A/B/C/D198-421[»]
    ProteinModelPortaliQ2FZK7.
    SMRiQ2FZK7. Positions 213-420, 441-584, 608-753.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati425 – 5891651Add
    BLAST
    Repeati596 – 7581632Add
    BLAST
    Repeati770 – 9321633Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni199 – 775577N-acetylmuramoyl-L-alanine amidaseAdd
    BLAST
    Regioni776 – 1256481Endo-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.

    Q2FZK7-1 [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 YKTAAPKAAT TSAPKAKTEA TPKVTTFSAS 200
    AQPRSVAATP KTSLPKYKPQ VNSSINDYIC KNNLKAPKIE EDYTSYFPKY 250
    AYRNGVGRPE GIVVHDTAND RSTINGEISY MKNNYQNAFV HAFVDGDRII 300
    ETAPTDYLSW GVGAVGNPRF INVEIVHTHD YASFARSMNN YADYAATQLQ 350
    YYGLKPDSAE YDGNGTVWTH YAVSKYLGGT DHADPHGYLR SHNYSYDQLY 400
    DLINEKYLIK MGKVAPWGTQ STTTPTTPSK PTTPSKPSTG KLTVAANNGV 450
    AQIKPTNSGL YTTVYDKTGK ATNEVQKTFA VSKTATLGNQ KFYLVQDYNS 500
    GNKFGWVKEG DVVYNTAKSP VNVNQSYSIK PGTKLYTVPW GTSKQVAGSV 550
    SGSGNQTFKA SKQQQIDKSI YLYGSVNGKS GWVSKAYLVD TAKPTPTPTP 600
    KPSTPTTNNK LTVSSLNGVA QINAKNNGLF TTVYDKTGKP TKEVQKTFAV 650
    TKEASLGGNK FYLVKDYNSP TLIGWVKQGD VIYNNAKSPV NVMQTYTVKP 700
    GTKLYSVPWG TYKQEAGAVS GTGNQTFKAT KQQQIDKSIY LFGTVNGKSG 750
    WVSKAYLAVP AAPKKAVAQP KTAVKAYTVT KPQTTQTVSK IAQVKPNNTG 800
    IRASVYEKTA KNGAKYADRT FYVTKERAHG NETYVLLNNT SHNIPLGWFN 850
    VKDLNVQNLG KEVKTTQKYT VNKSNNGLSM VPWGTKNQVI LTGNNIAQGT 900
    FNATKQVSVG KDVYLYGTIN NRTGWVNAKD LTAPTAVKPT TSAAKDYNYT 950
    YVIKNGNGYY YVTPNSDTAK YSLKAFNEQP FAVVKEQVIN GQTWYYGKLS 1000
    NGKLAWIKST DLAKELIKYN QTGMTLNQVA QIQAGLQYKP QVQRVPGKWT 1050
    DAKFNDVKHA MDTKRLAQDP ALKYQFLRLD QPQNISIDKI NQFLKGKGVL 1100
    ENQGAAFNKA AQMYGINEVY LISHALLETG NGTSQLAKGA DVVNNKVVTN 1150
    SNTKYHNVFG IAAYDNDPLR EGIKYAKQAG WDTVSKAIVG GAKFIGNSYV 1200
    KAGQNTLYKM RWNPAHPGTH QYATDVDWAN INAKIIKGYY DKIGEVGKYF 1250
    DIPQYK 1256
    Length:1,256
    Mass (Da):137,384
    Last modified:March 21, 2006 - v1
    Checksum:i2BB76CAA292FDD20
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D17366 Genomic DNA. Translation: BAA04185.1.
    L41499 Genomic DNA. Translation: AAA99982.1.
    CP000253 Genomic DNA. Translation: ABD30118.1.
    RefSeqiWP_001074547.1. NC_007795.1.
    YP_499546.1. NC_007795.1.

    Genome annotation databases

    EnsemblBacteriaiABD30118; ABD30118; SAOUHSC_00994.
    GeneIDi3920394.
    KEGGisao:SAOUHSC_00994.
    PATRICi19579507. VBIStaAur99865_0912.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D17366 Genomic DNA. Translation: BAA04185.1 .
    L41499 Genomic DNA. Translation: AAA99982.1 .
    CP000253 Genomic DNA. Translation: ABD30118.1 .
    RefSeqi WP_001074547.1. NC_007795.1.
    YP_499546.1. NC_007795.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4KNK X-ray 1.12 A/B 198-421 [» ]
    4KNL X-ray 1.55 A/B/C/D 198-421 [» ]
    ProteinModelPortali Q2FZK7.
    SMRi Q2FZK7. Positions 213-420, 441-584, 608-753.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 93061.SAOUHSC_00994.

    Protein family/group databases

    CAZyi GH73. Glycoside Hydrolase Family 73.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABD30118 ; ABD30118 ; SAOUHSC_00994 .
    GeneIDi 3920394.
    KEGGi sao:SAOUHSC_00994.
    PATRICi 19579507. VBIStaAur99865_0912.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SAUR93061:GIWJ-959-MONOMER.

    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. "A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-beta-N-acetylglucosaminidase domain: cloning, sequence analysis, and characterization."
      Oshida T., Sugai M., Komatsuzawa H., Hong Y.-M., Suginaka H., Tomasz A.
      Proc. Natl. Acad. Sci. U.S.A. 92:285-289(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 205-214 AND 776-792.
    2. Foster S.J.
      Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The Staphylococcus aureus NCTC 8325 genome."
      Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
      (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.); Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C. (2006)
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NCTC 8325.

    Entry informationi

    Entry nameiATL_STAA8
    AccessioniPrimary (citable) accession number: Q2FZK7
    Secondary accession number(s): O32391
    , P52081, Q7WTC6, Q7WY94, Q7WY95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: March 21, 2006
    Last modified: October 1, 2014
    This is version 61 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

    3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3