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P0C2T5

- ACMA_LACLC

UniProt

P0C2T5 - ACMA_LACLC

Protein

Probable N-acetylmuramidase

Gene

acmA

Organism
Lactococcus lactis subsp. cremoris (Streptococcus cremoris)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 37 (01 Oct 2014)
      Sequence version 1 (01 May 2007)
      Previous versions | rss
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    Functioni

    Hydrolyzes the cell wall of L.lactis and M.lysodeikticus. Required for cell separation during growth.

    Catalytic activityi

    Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.

    GO - Molecular functioni

    1. amidase activity Source: InterPro
    2. lysozyme activity Source: UniProtKB-EC

    GO - Biological processi

    1. barrier septum assembly Source: UniProtKB-KW
    2. cell wall macromolecule metabolic process Source: InterPro
    3. cytolysis Source: UniProtKB-KW
    4. defense response to bacterium Source: UniProtKB-KW
    5. peptidoglycan catabolic process Source: InterPro

    Keywords - Molecular functioni

    Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

    Keywords - Biological processi

    Cell cycle, Cell division, Cell wall biogenesis/degradation, Septation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable N-acetylmuramidase (EC:3.2.1.17)
    Alternative name(s):
    Autolysin
    Lysozyme
    Peptidoglycan hydrolase
    Gene namesi
    Name:acmA
    OrganismiLactococcus lactis subsp. cremoris (Streptococcus cremoris)
    Taxonomic identifieri1359 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

    Subcellular locationi

    Secreted 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 – 5757Sequence AnalysisAdd
    BLAST
    Chaini58 – 437380Probable N-acetylmuramidasePRO_0000012113Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP0C2T5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati245 – 28743LysM 1Add
    BLAST
    Repeati321 – 36343LysM 2Add
    BLAST
    Repeati395 – 43743LysM 3Add
    BLAST

    Domaini

    The LysM repeats are thought to be involved in peptidoglycan binding.

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 73 family.Curated
    Contains 3 LysM repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di3.10.350.10. 3 hits.
    InterProiIPR018392. LysM_dom.
    IPR013338. Lysozyme_subfam2_dom.
    IPR002901. MGlyc_endo_b_GlcNAc_like_dom.
    [Graphical view]
    PfamiPF01832. Glucosaminidase. 1 hit.
    PF01476. LysM. 3 hits.
    [Graphical view]
    SMARTiSM00257. LysM. 3 hits.
    SM00047. LYZ2. 1 hit.
    [Graphical view]
    SUPFAMiSSF54106. SSF54106. 3 hits.

    Sequencei

    Sequence statusi: Complete.

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

    P0C2T5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPVSRVKVKN RHLKKKTKKP LAFYKPTTKF VGAVLIAGTL TTTHELLLQQ    50
    TSPMVQAATN SSEAFIESIA ASAKPVADAN GLYPSVMIAQ AILESNWGSS 100
    QLSRAPYYNL FGIQGTYQGK SVVFKTQEYL NGKWVTKDMP FRVYPSFNQS 150
    FQDNTYVLKT TNFGNGPYYA KAWRANAATY QDATAALTGK YATDPSYGAS 200
    LNRIISQYNL TRFDGASSAG NTNSGGSTTT NTNNNSGTNS SSTTYTVKSG 250
    DTLWGISQRY GISVAQIQSA NNLKSTIIYI GQKLLLTGSA SSTNSGGSNN 300
    SASTTPTTSV TPAKPASQTS VKVKSGDTLW ALSVKYKTSI AQLKSWNHLS 350
    SDTIYIGQNL IVSQSAATSN PSTGSGSTAT NNSNSTSSNS NASIHKVVKG 400
    DTLWGLSQKS GSPIASIKAW NHLSSDTILI GQYLRIK 437
    Length:437
    Mass (Da):46,597
    Last modified:May 1, 2007 - v1
    Checksum:i169778AF09E13963
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF036720 Genomic DNA. Translation: AAB93629.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF036720 Genomic DNA. Translation: AAB93629.1 .

    3D structure databases

    ProteinModelPortali P0C2T5.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.10.350.10. 3 hits.
    InterProi IPR018392. LysM_dom.
    IPR013338. Lysozyme_subfam2_dom.
    IPR002901. MGlyc_endo_b_GlcNAc_like_dom.
    [Graphical view ]
    Pfami PF01832. Glucosaminidase. 1 hit.
    PF01476. LysM. 3 hits.
    [Graphical view ]
    SMARTi SM00257. LysM. 3 hits.
    SM00047. LYZ2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54106. SSF54106. 3 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Varying influence of the autolysin, N-acetyl muramidase, and the cell envelope proteinase on the rate of autolysis of six commercial Lactococcus lactis cheese starter bacteria grown in milk."
      Govindasamy-Lucey S., Gopal P.K., Sullivan P.A., Pillidge C.J.
      J. Dairy Res. 67:585-596(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 2250.

    Entry informationi

    Entry nameiACMA_LACLC
    AccessioniPrimary (citable) accession number: P0C2T5
    Secondary accession number(s): O52362, Q48603
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 37 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3