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 27-MAR-2024, entry version 106. 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; Bacillota; 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 RT NCTC 9602 as a member of the metallo(zinc) carboxypeptidase A family. RT Modular 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; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU01379}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X69507; CAA49259.1; -; Genomic_DNA. DR PIR; S33310; S33310. DR AlphaFoldDB; Q03415; -. DR SMR; Q03415; -. DR STRING; 1421.A2J09_18500; -. 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; LysM domain; 2. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR InterPro; IPR034274; ENP1_M14_CPD. DR InterPro; IPR018392; LysM_dom. DR InterPro; IPR036779; LysM_dom_sf. DR InterPro; IPR000834; Peptidase_M14. DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1. DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1. 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; LysM domain; 2. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1. DR PROSITE; PS51782; LYSM; 2. DR PROSITE; PS52035; PEPTIDASE_M14; 1. 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 DOMAIN 108..394 FT /note="Peptidase M14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379" FT ACT_SITE 347 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 366 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379" FT BINDING 162 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379" FT BINDING 165 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379" FT BINDING 255 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 307 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379" 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 //