ID   NPRE_BACPU              Reviewed;         300 AA.
AC   P68734; P06142; P25268;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   02-SEP-2026, entry version 66.
DE   RecName: Full=Neutral protease NprE;
DE            EC=3.4.24.28;
DE   AltName: Full=Bacillolysin-like protease;
DE   AltName: Full=Milk-clotting protease from Bacillus mesentericus strain 76;
DE            Short=MCP 76;
GN   Name=nprE;
OS   Bacillus pumilus (Bacillus mesentericus).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=1408;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=76;
RX   PubMed=2302386; DOI=10.1021/bi00454a029;
RA   Stoeva S., Kleinschmidt T., Mesrob B., Braunitzer G.;
RT   "Primary structure of a zinc protease from Bacillus mesentericus strain
RT   76.";
RL   Biochemistry 29:527-534(1990).
CC   -!- FUNCTION: Extracellular zinc metalloprotease.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Similar, but not identical, to that of thermolysin.;
CC         EC=3.4.24.28;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC       Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermolabile.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR   AlphaFoldDB; P68734; -.
DR   SMR; P68734; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd09597; M4_TLP; 1.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR023612; Peptidase_M4.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR001570; Peptidase_M4_C_domain.
DR   InterPro; IPR013856; Peptidase_M4_domain.
DR   InterPro; IPR050728; Zinc_Metalloprotease_M4.
DR   PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR   PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Zinc.
FT   CHAIN           1..300
FT                   /note="Neutral protease NprE"
FT                   /id="PRO_0000078173"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        228
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         139
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         178
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         178
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         181
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         181
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         183
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         186
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         186
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   300 AA;  32674 MW;  6207B816C446385B CRC64;
     AAATGSGTTL KGATVPLNIS YEGGKYVLRD LSKPTGTQII TYDLQNRQSR LPGTLVSSTT
     KTFTSSSQRA AVDAHYNLGK VYDYFYSNFK RNSYDNKGSK IVSSVHYGTQ YNNAAWTGDQ
     MIYGDGDGSF FSPLSGSLDV TAHEMTHGVT QETANLIYEN QPGALNESFS DVFGYFNDTE
     DWDIGEDITV SQPALRSLSN PTKYNQPDNY ANYRNLPNTD EGDYGGVHTN SGIPNKAAYN
     TITKLGVSKS QQIYYRALTT YLTPSSTFKD AKAALIQSAR DLYGSTDAAK VEAAWNAVGL
//