ID   PEPO_LACLC              Reviewed;         627 AA.
AC   P0C2B4; Q09145; Q9R4Y4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Neutral endopeptidase;
DE            EC=3.4.24.-;
DE   AltName: Full=Endopeptidase O;
GN   Name=pepO;
OS   Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RC   STRAIN=P8-2-47;
RX   PubMed=8458851; DOI=10.1128/jb.175.7.2087-2096.1993;
RA   Mierau I., Tan P.S.T., Haandrikman A.J., Kok J., Leenhouts K.J.,
RA   Konings W.N., Venema G.;
RT   "Cloning and sequencing of the gene for a lactococcal endopeptidase, an
RT   enzyme with sequence similarity to mammalian enkephalinase.";
RL   J. Bacteriol. 175:2087-2096(1993).
CC   -!- FUNCTION: Endopeptidase with broad substrate specificity for several
CC       oligopeptides. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01233, ECO:0000305}.
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DR   EMBL; L04938; AAA25204.1; -; Genomic_DNA.
DR   PIR; A47098; A47098.
DR   RefSeq; WP_011669109.1; NZ_WJUX01000060.1.
DR   RefSeq; YP_005863095.1; NC_017478.1.
DR   AlphaFoldDB; P0C2B4; -.
DR   SMR; P0C2B4; -.
DR   MEROPS; M13.004; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8458851"
FT   CHAIN           2..627
FT                   /note="Neutral endopeptidase"
FT                   /id="PRO_0000078231"
FT   DOMAIN          1..627
FT                   /note="Peptidase M13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   ACT_SITE        476
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        539
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   BINDING         475
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         479
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         535
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
SQ   SEQUENCE   627 AA;  71528 MW;  916B70C7FE9A68D7 CRC64;
     MTRIQDDLFA TVNAEWLENA EIPADKPRIS AFDELVLKNE KNLAKDLADL SQNLPTDNPE
     LLEAIKFYNK AGDWQAREKA DFSAVKNELA KVETLNTFED FKNNLTQLVF HSQAPLPFSF
     SVEPDMKDAI HYSLGFSGPG LILPDTTYYN DEHPRKKELL DFWAKNTSEI LKTFDVENAE
     EIAKSALKFD ALLVPSANTS EEWAKYAELY HPISTDSFVS KVKNLDLKSL IKDLVKTEPD
     KVIVYEDRFY ESFDSLINEE NWSLIKAWML TKIARGATSF FNEDLRILGG AYGRFLSNVQ
     EARSQEKHQL DLTESYFSQV IGLFYGKKYF GEAGKADVKR MVTAMIKVYQ ARLSKNEWLS
     QETAEKAIEK LDAITPFIGF PDKLPEIYSR LKTTSGSLYE DALKFDEILT ARTFEKFSED
     VDKTSWHMPA HMVNAYYSPD SNTIVFPAAI LQAPFYSLEQ SSSQNYGGIG TVIAHEISHA
     FDNNGAQFDK EGNLNKWWLD EDYEAFEEKQ KEMIALFDGV ETEAGPANGK LIVSENIADQ
     GGITAALTAA KDEKDVDLKA FFSQWAKIWR MKASKEFQQM LLSMDFHAPA KLRANIPPTN
     LEEFYDTFDV KETDKMYRAP ENRLKIW