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Q99V41

- ATL_STAAN

UniProt

Q99V41 - ATL_STAAN

Protein

Bifunctional autolysin

Gene

atl

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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

    BioCyciSAUR158879:GJCB-957-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:SA0905
    OrganismiStaphylococcus aureus (strain N315)
    Taxonomic identifieri158879 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000000751: 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 – 12481219Bifunctional autolysinPRO_0000045475Add
    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

    STRINGi158879.SA0905.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99V41.
    SMRiQ99V41. Positions 204-410, 433-576, 600-745, 935-1006, 1097-1231.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati417 – 5811651Add
    BLAST
    Repeati588 – 7501632Add
    BLAST
    Repeati762 – 9241633Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni191 – 767577N-acetylmuramoyl-L-alanine amidaseAdd
    BLAST
    Regioni768 – 1248481Endo-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.

    Q99V41-1 [UniParc]FASTAAdd to Basket

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    MAKKFNYKLP SMVALTLVGS AVTAHQVQAA ETTQDQTTNK NVLDSNKVKA     50
    TTEQAKAEVK NPTQNISGTQ VYQDPAIVQP KTANNKTGNA QVSQKVDTAQ 100
    VNGDTRANQS ATTNNTQPVA KSTSTTAPKT NTNVTNAGYS LVDDEDDNSE 150
    HQINPELIKS AAKPAALETQ YKAAAPKAKT EATPKVTTFS ASAQPRSVAA 200
    TPKTSLPKYK PQVNSSINDY IRKNNLKAPK IEEDYTSYFP KYAYRNGVGR 250
    PEGIVVHDTA NDRSTINGEI SYMKNNYQNA FVHAFVDGDR IIETAPTDYL 300
    SWGVGAVGNP RFINVEIVHT HDYASFARSM NNYADYAATQ LQYYGLKPDS 350
    AEYDGNGTVW THYAVSKYLG GTDHADPHGY LRSHNYSYDQ LYDLINEKYL 400
    IKMGKVAPWG TQFTTTPTTP SKPTTPSKPS TGKLTVAANN GVAQIKPTNS 450
    GLYTTVYDKT GKATNEVQKT FAVSKTATLG NQKFYLVQDY NSGNKFGWVK 500
    EGDVVYNTAK SPVNVNQSYS IKSGTKLYTV PWGTSKQVAG SVSGSGNQTF 550
    KASKQQQIDK SIYLYGSVNG KSGWVSKAYL VDTAKPTPTP IPKPSTPTTN 600
    NKLTVSSLNG VAQINAKNNG LFTTVYDKTG KPTKEVQKTF AVTKEASLGG 650
    NKFYLVKDYN SPTLIGWVKQ GDVIYNNAKS PVNVMQTYTV KPGTKLYSVP 700
    WGTYKQEAGA VSGTGNQTFK ATKQQQIDKS IYLFGTVNGK SGWVSKAYLA 750
    VPAAPKKAVA QPKTAVKAYT VTKPQTTQTV SKIAQVKPNN TGIRASVYEK 800
    TAKNGAKYAD RTFYVTKERA HGNETYVLLN NTSHNIPLGW FNVKDLNVQN 850
    LGKEVKTTQK YTVNKSNNGL SMVPWGTKNQ VILTGNNIAQ GTFNATKQVS 900
    VGKDVYLYGT INNRTGWVNA KDLTAPTAVK PTTSAAKDYN YTYVIKNGNG 950
    YYYVTPNSDT AKYSLKAFNE QPFAVVKEQV INGQTWYYGK LSNGKLAWIK 1000
    STDLAKELIK YNQTGMTLNQ VAQIQAGLQY KPQVQRVPGK WTDANFNDVK 1050
    HAMDTKRLAQ DPALKYQFLR LDQPQNISID KINQFLKGKG VLENQGAAFN 1100
    KAAQMYGINE VYLISHALLE TGNGTSQLAK GADVVNNKVV TNSNTKYHNV 1150
    FGIAAYDNDP LREGIKYAKQ AGWDTVSKAI VGGAKFIGNS YVKAGQNTLY 1200
    KMRWNPAHPG THQYATDVDW ANINAKIIKG YYDKIGEVGK YFDIPQYK 1248
    Length:1,248
    Mass (Da):136,751
    Last modified:June 1, 2001 - v1
    Checksum:i701B54EE6152275E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000018 Genomic DNA. Translation: BAB42150.1.
    PIRiC89874.
    RefSeqiNP_374172.1. NC_002745.2.

    Genome annotation databases

    EnsemblBacteriaiBAB42150; BAB42150; BAB42150.
    GeneIDi1123728.
    KEGGisau:SA0905.
    PATRICi19573994. VBIStaAur116463_0967.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000018 Genomic DNA. Translation: BAB42150.1 .
    PIRi C89874.
    RefSeqi NP_374172.1. NC_002745.2.

    3D structure databases

    ProteinModelPortali Q99V41.
    SMRi Q99V41. Positions 204-410, 433-576, 600-745, 935-1006, 1097-1231.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 158879.SA0905.

    Protein family/group databases

    CAZyi GH73. Glycoside Hydrolase Family 73.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB42150 ; BAB42150 ; BAB42150 .
    GeneIDi 1123728.
    KEGGi sau:SA0905.
    PATRICi 19573994. VBIStaAur116463_0967.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SAUR158879:GJCB-957-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: N315.
    2. "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
      Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
      Submitted (OCT-2007) to UniProtKB
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: N315.

    Entry informationi

    Entry nameiATL_STAAN
    AccessioniPrimary (citable) accession number: Q99V41
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 80 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