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P32762

- ALYS_BPHB3

UniProt

P32762 - ALYS_BPHB3

Protein

Lytic amidase

Gene

HBL

Organism
Streptococcus pneumoniae phage HB-3
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    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. peptidoglycan catabolic process Source: InterPro

    Keywords - Molecular functioni

    Antimicrobial, Bacteriolytic enzyme, Hydrolase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lytic amidase (EC:3.5.1.28)
    Alternative name(s):
    N-acetylmuramoyl-L-alanine amidase
    Gene namesi
    Name:HBL
    OrganismiStreptococcus pneumoniae phage HB-3
    Taxonomic identifieri10728 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridae
    Virus hostiStreptococcus pneumoniae [TaxID: 1313]

    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
    Chaini1 – 318318Lytic amidasePRO_0000164406Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP32762.
    SMRiP32762. Positions 188-318.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati175 – 19420Cell wall-binding 1Add
    BLAST
    Repeati196 – 21520Cell wall-binding 2Add
    BLAST
    Repeati217 – 23721Cell wall-binding 3Add
    BLAST
    Repeati238 – 25720Cell wall-binding 4Add
    BLAST
    Repeati258 – 27720Cell wall-binding 5Add
    BLAST
    Repeati280 – 30122Cell wall-binding 6Add
    BLAST

    Sequence similaritiesi

    Contains 6 cell wall-binding repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Family and domain databases

    InterProiIPR002502. Amidase_domain.
    IPR018337. Cell_wall/Cho-bd_repeat.
    [Graphical view]
    PfamiPF01510. Amidase_2. 1 hit.
    PF01473. CW_binding_1. 5 hits.
    [Graphical view]
    SMARTiSM00644. Ami_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF55846. SSF55846. 1 hit.
    PROSITEiPS51170. CW. 6 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32762-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDIDRNRLRT GLPQVGVQPY RQVHAHSTGN RNSTVQNEAD YHWRKDPELG    50
    FFSHVVGNFR IMQVGPVNNG SWDVGGGWNA ETYAAVELIE SHSTKEEFMA 100
    DYRLYIELLR NLADEAGLPK TLDTDDLAGI KTHEYCTNNQ PNNHSDHVDP 150
    YPYLASWGIS REQFKQDIEN GLSAATGWQK NGTGYWYVHS DGSYSKDKFE 200
    KINGTWYYFD GSGYMLSDRW KKHTDGNWYY FDQSGEMATG WKKIADKWYY 250
    FDVEGAMKTG WVKYKDTWYY LDAKEGAMVS NAFIQSADGT GWYYLKPDGT 300
    LADKPEFTVE PDGLITVK 318
    Length:318
    Mass (Da):36,509
    Last modified:October 1, 1993 - v1
    Checksum:i65B30A9127E58351
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34652 Genomic DNA. Translation: AAA50574.1.
    PIRiS16016.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34652 Genomic DNA. Translation: AAA50574.1 .
    PIRi S16016.

    3D structure databases

    ProteinModelPortali P32762.
    SMRi P32762. Positions 188-318.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR002502. Amidase_domain.
    IPR018337. Cell_wall/Cho-bd_repeat.
    [Graphical view ]
    Pfami PF01510. Amidase_2. 1 hit.
    PF01473. CW_binding_1. 5 hits.
    [Graphical view ]
    SMARTi SM00644. Ami_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55846. SSF55846. 1 hit.
    PROSITEi PS51170. CW. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the Streptococcus pneumoniae bacteriophage HB-3 amidase reveals high homology with the major host autolysin."
      Romero A., Lopez R., Garcia P.
      J. Bacteriol. 172:5064-5070(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Characterization of the pneumococcal bacteriophage HB-3 amidase: cloning and expression in Escherichia coli."
      Romero A., Lopez R., Garcia P.
      J. Virol. 64:137-142(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-21.

    Entry informationi

    Entry nameiALYS_BPHB3
    AccessioniPrimary (citable) accession number: P32762
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    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 programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3