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Q03415

- ENP1_LYSSH

UniProt

Q03415 - ENP1_LYSSH

Protein

Gamma-D-glutamyl-L-diamino acid endopeptidase 1

Gene
N/A
Organism
Lysinibacillus sphaericus (Bacillus sphaericus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    An endopeptidase which hydrolyzes the gamma-D-Glu-(L)meso-diaminopimelic acid bond of L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid and L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid(L)-D-Ala peptides. It is active on spore cortex peptidoglycan.

    Catalytic activityi

    Hydrolysis of gamma-D-glutamyl bonds to the L-terminus (position 7) of meso-diaminopimelic acid (meso-A2pm) in 7-(L-Ala-gamma-D-Glu)-meso-A2pm and 7-(L-Ala-gamma-D-Glu)-7-(D-Ala)-meso-A2pm. It is required that the D-terminal amino and carboxy groups of meso-A2pm are unsubstituted.

    Cofactori

    Zinc.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi162 – 1621ZincBy similarity
    Metal bindingi165 – 1651ZincBy similarity
    Binding sitei255 – 2551SubstrateBy similarity
    Metal bindingi307 – 3071ZincBy similarity
    Active sitei347 – 3471Proton donorBy similarity
    Active sitei366 – 3661NucleophileBy similarity

    GO - Molecular functioni

    1. metallocarboxypeptidase activity Source: InterPro
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Cell wall biogenesis/degradation, Sporulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM14.008.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gamma-D-glutamyl-L-diamino acid endopeptidase 1 (EC:3.4.19.11)
    Alternative name(s):
    Endopeptidase I
    Gamma-D-glutamyl-L-diamino acid endopeptidase I
    Gamma-D-glutamyl-meso-diaminopimelate peptidase I
    OrganismiLysinibacillus sphaericus (Bacillus sphaericus)
    Taxonomic identifieri1421 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 396396Gamma-D-glutamyl-L-diamino acid endopeptidase 1PRO_0000212788Add
    BLAST

    Expressioni

    Developmental stagei

    Produced at stage IV of sporulation in forespore and spore integuments.

    Structurei

    3D structure databases

    ProteinModelPortaliQ03415.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati3 – 4644LysM 1Add
    BLAST
    Repeati53 – 9644LysM 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni101 – 396296CatalyticAdd
    BLAST

    Domaini

    LysM repeats are thought to be involved in peptidoglycan binding.

    Sequence similaritiesi

    Belongs to the peptidase M14 family.Curated
    Contains 2 LysM repeats.Curated

    Keywords - Domaini

    Repeat

    Family and domain databases

    Gene3Di3.10.350.10. 2 hits.
    InterProiIPR018392. LysM_dom.
    IPR000834. Peptidase_M14.
    [Graphical view]
    PfamiPF01476. LysM. 2 hits.
    PF00246. Peptidase_M14. 1 hit.
    [Graphical view]
    SMARTiSM00257. LysM. 2 hits.
    SM00631. Zn_pept. 1 hit.
    [Graphical view]
    SUPFAMiSSF54106. SSF54106. 2 hits.
    PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q03415-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDILIRPGDS LWYFSDLFKI PLQLLLDSNR NINPQLLQVG QRIQIPGYVT    50
    TSYTITQGDS LWQIAQNKNL PLNAILLVNP EIQPSRLHIG QTIQVPQRLT 100
    WRLVNGQQNY DYSMMMNDIK KLQTAYPFLQ GTPIGNSVLA QPIPEILIGN 150
    GSKRIHYKAS FHANEWITTP IIMTFLNDYL LALTNQTTIR GLSMGPLYNQ 200
    TTLSLVPMVN PDGVNLVING PPANEALKNK LIAWNHNSQN FSGWKANING 250
    VDLNDQFPAK WELENARNPQ TPGPRDYGGE APLTQPEAIA MADLTRSRNF 300
    AWVLAFHTQG RVIYWGFENL EPPESQTMVE EFSRVSGYEP IQSANSYAGY 350
    KDWFIQDWRR PGFTVELGSG TNPLPISEFD TIYQEALGIF LAGLYL 396
    Length:396
    Mass (Da):44,724
    Last modified:October 1, 1994 - v1
    Checksum:iD929CEBC92324473
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69507 Genomic DNA. Translation: CAA49259.1.
    PIRiS33310.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69507 Genomic DNA. Translation: CAA49259.1 .
    PIRi S33310.

    3D structure databases

    ProteinModelPortali Q03415.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M14.008.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.10.350.10. 2 hits.
    InterProi IPR018392. LysM_dom.
    IPR000834. Peptidase_M14.
    [Graphical view ]
    Pfami PF01476. LysM. 2 hits.
    PF00246. Peptidase_M14. 1 hit.
    [Graphical view ]
    SMARTi SM00257. LysM. 2 hits.
    SM00631. Zn_pept. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54106. SSF54106. 2 hits.
    PROSITEi PS00132. CARBOXYPEPT_ZN_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the sporulation-related gamma-D-glutamyl-(L)meso-diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC 9602 as a member of the metallo(zinc) carboxypeptidase A family. Modular design of the protein."
      Hourdou M.-L., Guinand M., Vacheron M.J., Michel G., Denoroy L., Duez C.M., Englebert S., Joris B., Weber G., Ghuysen J.-M.
      Biochem. J. 292:563-570(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: DSM 396 / NCTC 9602.
    2. "Purification and partial characterization of the extracellular gamma-D-glutamyl-(L)meso-diaminopimelate endopeptidase I, from Bacillus sphaericus NCTC 9602."
      Garnier M., Vacheron M., Guinard J.-M., Michel G.
      Eur. J. Biochem. 148:539-543(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Strain: DSM 396 / NCTC 9602.

    Entry informationi

    Entry nameiENP1_LYSSH
    AccessioniPrimary (citable) accession number: Q03415
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 81 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

    Direct protein sequencing

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3