ID   ENP1_LYSSH              Reviewed;         396 AA.
AC   Q03415;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Gamma-D-glutamyl-L-diamino acid endopeptidase 1;
DE            EC=3.4.19.11;
DE   AltName: Full=Endopeptidase I;
DE   AltName: Full=Gamma-D-glutamyl-L-diamino acid endopeptidase I;
DE   AltName: Full=Gamma-D-glutamyl-meso-diaminopimelate peptidase I;
OS   Lysinibacillus sphaericus (Bacillus sphaericus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=DSM 396 / NCTC 9602;
RX   PubMed=8503890; DOI=10.1042/bj2920563;
RA   Hourdou M.-L., Guinand M., Vacheron M.J., Michel G., Denoroy L., Duez C.M.,
RA   Englebert S., Joris B., Weber G., Ghuysen J.-M.;
RT   "Characterization of the sporulation-related gamma-D-glutamyl-(L)meso-
RT   diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC
RT   9602 as a member of the metallo(zinc) carboxypeptidase A family. Modular
RT   design of the protein.";
RL   Biochem. J. 292:563-570(1993).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=DSM 396 / NCTC 9602;
RX   PubMed=3922755; DOI=10.1111/j.1432-1033.1985.tb08873.x;
RA   Garnier M., Vacheron M., Guinard J.-M., Michel G.;
RT   "Purification and partial characterization of the extracellular gamma-D-
RT   glutamyl-(L)meso-diaminopimelate endopeptidase I, from Bacillus sphaericus
RT   NCTC 9602.";
RL   Eur. J. Biochem. 148:539-543(1985).
CC   -!- FUNCTION: An endopeptidase which hydrolyzes the gamma-D-Glu-(L)meso-
CC       diaminopimelic acid bond of L-Ala-gamma-D-Glu-(L)meso-diaminopimelic
CC       acid and L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid(L)-D-Ala
CC       peptides. It is active on spore cortex peptidoglycan.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of gamma-D-glutamyl bonds to the L-terminus
CC         (position 7) of meso-diaminopimelic acid (meso-A2pm) in 7-(L-Ala-
CC         gamma-D-Glu)-meso-A2pm and 7-(L-Ala-gamma-D-Glu)-7-(D-Ala)-meso-A2pm.
CC         It is required that the D-terminal amino and carboxy groups of meso-
CC         A2pm are unsubstituted.; EC=3.4.19.11;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC   -!- DEVELOPMENTAL STAGE: Produced at stage IV of sporulation in forespore
CC       and spore integuments.
CC   -!- DOMAIN: LysM domains are thought to be involved in peptidoglycan
CC       binding.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR   EMBL; X69507; CAA49259.1; -; Genomic_DNA.
DR   PIR; S33310; S33310.
DR   AlphaFoldDB; Q03415; -.
DR   SMR; Q03415; -.
DR   MEROPS; M14.008; -.
DR   KEGG; ag:CAA49259; -.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 2.
DR   CDD; cd06229; M14_Endopeptidase_I; 1.
DR   Gene3D; 3.10.350.10; -; 2.
DR   InterPro; IPR034274; ENP1_M14_CPD.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF01476; LysM; 2.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SMART; SM00257; LysM; 2.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF54106; SSF54106; 2.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS51782; LYSM; 2.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Direct protein sequencing; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Repeat; Sporulation; Zinc.
FT   CHAIN           1..396
FT                   /note="Gamma-D-glutamyl-L-diamino acid endopeptidase 1"
FT                   /id="PRO_0000212788"
FT   DOMAIN          1..45
FT                   /note="LysM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          51..95
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   REGION          101..396
FT                   /note="Catalytic"
FT   ACT_SITE        347
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        366
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   396 AA;  44724 MW;  D929CEBC92324473 CRC64;
     MDILIRPGDS LWYFSDLFKI PLQLLLDSNR NINPQLLQVG QRIQIPGYVT TSYTITQGDS
     LWQIAQNKNL PLNAILLVNP EIQPSRLHIG QTIQVPQRLT WRLVNGQQNY DYSMMMNDIK
     KLQTAYPFLQ GTPIGNSVLA QPIPEILIGN GSKRIHYKAS FHANEWITTP IIMTFLNDYL
     LALTNQTTIR GLSMGPLYNQ TTLSLVPMVN PDGVNLVING PPANEALKNK LIAWNHNSQN
     FSGWKANING VDLNDQFPAK WELENARNPQ TPGPRDYGGE APLTQPEAIA MADLTRSRNF
     AWVLAFHTQG RVIYWGFENL EPPESQTMVE EFSRVSGYEP IQSANSYAGY KDWFIQDWRR
     PGFTVELGSG TNPLPISEFD TIYQEALGIF LAGLYL