ID   PEPO_LACHE              Reviewed;         647 AA.
AC   O52071;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Neutral endopeptidase;
DE            EC=3.4.24.-;
DE   AltName: Full=Endopeptidase O;
GN   Name=pepO;
OS   Lactobacillus helveticus (Lactobacillus suntoryeus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CNRZ 32;
RX   PubMed=9726890; DOI=10.1128/aem.64.9.3411-3415.1998;
RA   Chen Y.-S., Steele J.L.;
RT   "Genetic characterization and physiological role of endopeptidase O from
RT   Lactobacillus helveticus CNRZ32.";
RL   Appl. Environ. Microbiol. 64:3411-3415(1998).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01233, ECO:0000305}.
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DR   EMBL; AF019410; AAC35997.1; -; Genomic_DNA.
DR   RefSeq; WP_003629024.1; NZ_QKQX01000018.1.
DR   AlphaFoldDB; O52071; -.
DR   SMR; O52071; -.
DR   MEROPS; M13.010; -.
DR   PRIDE; O52071; -.
DR   eggNOG; COG3590; Bacteria.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd08662; M13; 1.
DR   Gene3D; 1.10.1380.10; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR000718; Peptidase_M13.
DR   InterPro; IPR018497; Peptidase_M13_C.
DR   InterPro; IPR042089; Peptidase_M13_dom_2.
DR   InterPro; IPR008753; Peptidase_M13_N.
DR   PANTHER; PTHR11733; PTHR11733; 1.
DR   Pfam; PF01431; Peptidase_M13; 1.
DR   Pfam; PF05649; Peptidase_M13_N; 1.
DR   PRINTS; PR00786; NEPRILYSIN.
DR   PROSITE; PS51885; NEPRILYSIN; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..647
FT                   /note="Neutral endopeptidase"
FT                   /id="PRO_0000078232"
FT   DOMAIN          1..647
FT                   /note="Peptidase M13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   ACT_SITE        497
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        560
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   BINDING         496
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         500
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         556
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
SQ   SEQUENCE   647 AA;  73537 MW;  EB5153C5E1DDE6FC CRC64;
     MRRYLAVRGG AGDVAEPDLN AKPQDNLYLA VNSEWLSKAE IPADQTSAGV NTELDIKIEK
     RMMKDFADIA SGKEKMPDIR DFDKAIALYK IAKNFDKRDA EKANPIQNDL QKILDLINFD
     KFKDNATELF MGPYALPFVF DVDADMKNTD FNVLHFGGPS TFLPDTTTYK TPEAKKLLDI
     LEKQSINLLE MAGIGKEEAR VYVQNALAFD QKLSKVVKST EEWSDYAAIY NPVSLTEFLA
     KFKSFDMADF LKTILPEKVE RVIVMEPRFL DHADELINPA NFDEIKGWML VKYINSVAKY
     LSQDFRAAAF PFNQAISGTP ELPSQIKQAY RLANGAFDEA VGIFYGKKYF GEEAKHDVED
     MIHNMLKVYE QRINDNNWLS EDTKKKAIIK LRALVLKIGY PEKIEKIYDL LQIDPERSLY
     ENEAQMATVR TKYMLDKLTQ PVDRSVWLMP GNLNNACYDP QRNDLTFPAG ILQAPFYDIH
     QSRGANYGGI GATIGHEVSH AFDNSGAKFD EHGNMNNWWT DEDFAEFNKR VGQMVDIFDG
     LQYGPAKING KQVVGENIAD LAGLACAVQA GKNDNVDLKD LFENYARSWM QKQRPEAIKT
     EVQVDVHAPQ PTRVNIPVQC QDDFYTAFDV KPDDGMWLDP EDRITIW