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P14892

- CWLA_BACSP

UniProt

P14892 - CWLA_BACSP

Protein

N-acetylmuramoyl-L-alanine amidase CwlA

Gene

cwlA

Organism
Bacillus sp.
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation.

    Catalytic activityi

    Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

    GO - Molecular functioni

    1. N-acetylmuramoyl-L-alanine amidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cytolysis Source: UniProtKB-KW
    2. defense response to bacterium Source: UniProtKB-KW
    3. establishment of competence for transformation Source: UniProtKB-KW
    4. peptidoglycan catabolic process Source: InterPro
    5. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antimicrobial, Bacteriolytic enzyme, Hydrolase

    Keywords - Biological processi

    Cell wall biogenesis/degradation, Competence, Sporulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetylmuramoyl-L-alanine amidase CwlA (EC:3.5.1.28)
    Alternative name(s):
    Autolysin
    Cell wall hydrolase
    Gene namesi
    Name:cwlA
    OrganismiBacillus sp.
    Taxonomic identifieri1409 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    Subcellular locationi

    Secreted Curated

    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 – 3737Add
    BLAST
    Chaini38 – 251214N-acetylmuramoyl-L-alanine amidase CwlAPRO_0000006452Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP14892.
    SMRiP14892. Positions 1-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.80.10. 1 hit.
    InterProiIPR021976. Amidase02_C.
    IPR002502. Amidase_domain.
    [Graphical view]
    PfamiPF12123. Amidase02_C. 1 hit.
    PF01510. Amidase_2. 1 hit.
    [Graphical view]
    SMARTiSM00644. Ami_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF55846. SSF55846. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P14892-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEIKQMLVPV SRYSVLCPYE MNPTEITFHN TYNDAPAINE RNNVANNSTG    50
    TSFHIAVDDK EAIQLIPFNR NAWHAGDGTN GRGNRHSIGV EICYSQSGGA 100
    RYRKAELNAV EVIAQLMIQF DIPISKVKTH QERNGKYCPH RMLDEGRVQW 150
    FKNQCANRAS SIKNSNKTQE TGKVEIIVNK FNKVVTYEFG TALVPEMLGM 200
    MDALGYESRI ISYGDKQGLV RFETAYRQGN ELDKATAWLD AKGLKYFYTK 250
    E 251
    Length:251
    Mass (Da):28,473
    Last modified:April 1, 1990 - v1
    Checksum:i1F52F36B20576F0D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13524 Genomic DNA. Translation: CAA31877.1.
    PIRiS08306.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13524 Genomic DNA. Translation: CAA31877.1 .
    PIRi S08306.

    3D structure databases

    ProteinModelPortali P14892.
    SMRi P14892. Positions 1-147.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.80.10. 1 hit.
    InterProi IPR021976. Amidase02_C.
    IPR002502. Amidase_domain.
    [Graphical view ]
    Pfami PF12123. Amidase02_C. 1 hit.
    PF01510. Amidase_2. 1 hit.
    [Graphical view ]
    SMARTi SM00644. Ami_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55846. SSF55846. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing and expression of a Bacillus bacteriolytic enzyme in Escherichia coli."
      Potvin C., Leclerc D., Tremblay G., Asselin A., Bellemare G.
      Mol. Gen. Genet. 214:241-248(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiCWLA_BACSP
    AccessioniPrimary (citable) accession number: P14892
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    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

    Miscellaneous

    Retention of enzymatic activity was limited to the N-terminal fragment (AA 1-196).

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3