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O33635

- ATL_STAEP

UniProt

O33635 - ATL_STAEP

Protein

Bifunctional autolysin

Gene

atl

Organism
Staphylococcus epidermidis
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      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. As a bacterial surface-associated protein, mediates attachment to polystyrene surfaces, contributing to biofilm formation. Has also vitronectin-binding activity.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
    Alternative name(s):
    AtlE
    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:atlE
    OrganismiStaphylococcus epidermidis
    Taxonomic identifieri1282 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

    Subcellular locationi

    Secreted 1 Publication
    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 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 13351306Bifunctional autolysinPRO_0000045479Add
    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

    Structurei

    Secondary structure

    1
    1335
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi321 – 3288
    Beta strandi336 – 3383
    Beta strandi358 – 3636
    Helixi371 – 38010
    Turni381 – 3844
    Beta strandi388 – 3914
    Beta strandi396 – 3983
    Beta strandi407 – 4093
    Helixi410 – 4145
    Beta strandi417 – 4226
    Helixi428 – 44821
    Turni457 – 4593
    Beta strandi462 – 4665
    Helixi467 – 4737
    Helixi483 – 4886
    Helixi493 – 50715
    Beta strandi699 – 7035
    Beta strandi706 – 7105
    Beta strandi717 – 7204
    Beta strandi736 – 7449
    Beta strandi747 – 7537
    Turni755 – 7573
    Beta strandi760 – 7656
    Helixi766 – 7683
    Beta strandi769 – 7746
    Beta strandi778 – 7869
    Beta strandi791 – 7955
    Helixi800 – 8023
    Beta strandi803 – 8064
    Beta strandi809 – 8113
    Beta strandi813 – 82311
    Beta strandi826 – 8338
    Beta strandi836 – 8416
    Helixi842 – 8443

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LATX-ray1.70A/B303-515[»]
    4EPCX-ray2.90A516-847[»]
    ProteinModelPortaliO33635.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO33635.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati516 – 6811661Add
    BLAST
    Repeati682 – 8451642Add
    BLAST
    Repeati846 – 10151703Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni303 – 863561N-acetylmuramoyl-L-alanine amidaseAdd
    BLAST
    Regioni864 – 1335472Endo-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

    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.

    O33635-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKKFNYKLP SMVALTLFGT AFTAHQANAA EQPQNQSNHK NVLDDQTALK     50
    QAEKAKSEVT QSTTNVSGTQ TYQDPTQVQP KQDTQSTTYD ASLDEMSTYN 100
    EISSNQKQQS LSTDDANQNQ TNSVTKNQQE ETNDLTQEDK TSTDTNQLQE 150
    TQSVAKENEK DLGANANNEQ QDKKMTASQP SENQAIETQT ASNDNESQQK 200
    SQQVTSEQNE TATPKVSNTN ASGYNFDYDD EDDDSSTDHL EPISLNNVNA 250
    TSKQTTSYKY KEPAQRVTTN TVKKETASNQ ATIDTKQFTP FSATAQPRTV 300
    YSVSSQKTSS LPKYTPKVNS SINNYIRKKN MKAPRIEEDY TSYFPKYGYR 350
    NGVGRPEGIV VHDTANDNST IDGEIAFMKR NYTNAFVHAF VDGNRIIETA 400
    PTDYLSWGAG PYGNQRFINV EIVHTHDYDS FARSMNNYAD YAATQLQYYN 450
    LKPDSAENDG RGTVWTHAAI SNFLGGTDHA DPHQYLRSHN YSYAELYDLI 500
    YEKYLIKTKQ VAPWGTTSTK PSQPSKPSGG TNNKLTVSAN RGVAQIKPTN 550
    NGLYTTVYDS KGHKTDQVQK TLSVTKTATL GNNKFYLVED YNSGKKYGWV 600
    KQGDVVYNTA KAPVKVNQTY NVKAGSTLYT VPWGTPKQVA SKVSGTGNQT 650
    FKATKQQQID KATYLYGTVN GKSGWISKYY LTTASKPSNP TKPSTNNQLT 700
    VTNNSGVAQI NAKNSGLYTT VYDTKGKTTN QIQRTLSVTK AATLGDKKFY 750
    LVGDYNTGTN YGWVKQDEVI YNTAKSPVKI NQTYNVKPGV KLHTVPWGTY 800
    NQVAGTVSGK GDQTFKATKQ QQIDKATYLY GTVNGKSGWI SKYYLTAPSK 850
    VQALSTQSTP APKQVKPSTQ TVNQIAQVKA NNSGIRASVY DKTAKSGTKY 900
    ANRTFLINKQ RTQGNNTYVL LQDGTSNTPL GWVNINDVTT QNIGKQTQSI 950
    GKYSVKPTNN GLYSIAWGTK NQQLLAPNTL ANQAFNASKA VYVGKDLYLY 1000
    GTVNNRTGWI AAKDLIQNST DAQSTPYNYT FVINNSKSYF YMDPTKANRY 1050
    SLKPYYEQTF TVIKQKNING VKWYYGQLLD GKYVWIKSTD LVKEKIKYAY 1100
    TGMTLNNAIN IQSRLKYKPQ VQNEPLKWSN ANYSQIKNAM DTKRLANDSS 1150
    LKYQFLRLDQ PQYLSAQALN KLLKGKGVLE NQGAAFSQAA RKYGLNEIYL 1200
    ISHALVETGN GTSQLAKGGD VSKGKFTTKT GHKYHNVFGI GAFDNNALVD 1250
    GIKYAKNAGW TSVSKAIIGG AKFIGNSYVK AGQNTLYKMR WNPANPGTHQ 1300
    YATDINWANV NAQVLKQFYD KIGEVGKYFE IPTYK 1335
    Length:1,335
    Mass (Da):148,273
    Last modified:January 1, 1998 - v1
    Checksum:i0D8986BCB3DFF0A2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U71377 Genomic DNA. Translation: AAB63571.1.
    PIRiT30211.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U71377 Genomic DNA. Translation: AAB63571.1 .
    PIRi T30211.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3LAT X-ray 1.70 A/B 303-515 [» ]
    4EPC X-ray 2.90 A 516-847 [» ]
    ProteinModelPortali O33635.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH73. Glycoside Hydrolase Family 73.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei O33635.

    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. "Evidence for autolysin-mediated primary attachment of Staphylococcus epidermidis to a polystyrene surface."
      Heilmann C., Hussain M., Peters G., Goetz F.
      Mol. Microbiol. 24:1013-1024(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 303-312, SUBCELLULAR LOCATION, INVOLVEMENT IN BIOFILM FORMATION.
      Strain: O47.

    Entry informationi

    Entry nameiATL_STAEP
    AccessioniPrimary (citable) accession number: O33635
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 62 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, Direct protein sequencing, Multifunctional enzyme

    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