ID   NPRM_PRIM2              Reviewed;         562 AA.
AC   P0CH29; Q00891;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-MAY-2023, entry version 46.
DE   RecName: Full=Bacillolysin;
DE            EC=3.4.24.28;
DE   AltName: Full=Calcium-dependent exoproteinase {ECO:0000303|PubMed:8450307};
DE   AltName: Full=Neutral protease {ECO:0000303|PubMed:8450307};
DE   Flags: Precursor;
GN   Name=nprM {ECO:0000303|PubMed:8450307};
OS   Priestia megaterium (strain ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 /
OS   NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19)
OS   (Bacillus megaterium).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=1348623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   COFACTOR, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB
RC   9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19;
RX   PubMed=8450307; DOI=10.1099/00221287-139-1-39;
RA   Kuhn S., Fortnagel P.;
RT   "Molecular cloning and nucleotide sequence of the gene encoding a calcium-
RT   dependent exoproteinase from Bacillus megaterium ATCC 14581.";
RL   J. Gen. Microbiol. 139:39-47(1993).
CC   -!- FUNCTION: Extracellular zinc metalloprotease.
CC       {ECO:0000269|PubMed:8450307}.
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;
CC         Evidence={ECO:0000269|PubMed:8450307};
CC       Note=Binds 4 Ca(2+) ions per subunit. {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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is between 6.4 and 7.2. {ECO:0000269|PubMed:8450307};
CC       Temperature dependence:
CC         Optimum temperature is 58 degrees Celsius.
CC         {ECO:0000269|PubMed:8450307};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8450307}.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR   EMBL; X61380; CAA43654.1; -; Genomic_DNA.
DR   PIR; A47710; A47710.
DR   AlphaFoldDB; P0CH29; -.
DR   SMR; P0CH29; -.
DR   MEROPS; M04.001; -.
DR   GO; GO:0005576; C:extracellular region; 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; cd09597; M4_TLP; 1.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 3.10.450.40; -; 1.
DR   Gene3D; 3.10.450.490; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR025711; PepSY.
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   PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR   PANTHER; PTHR33794:SF3; NEUTRAL PROTEASE B; 1.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF03413; PepSY; 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; Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted;
KW   Signal; Zinc; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000305|PubMed:8450307"
FT   PROPEP          25..245
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000305|PubMed:8450307"
FT                   /id="PRO_0000028610"
FT   CHAIN           246..562
FT                   /note="Bacillolysin"
FT                   /id="PRO_0000028611"
FT   ACT_SITE        389
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   ACT_SITE        477
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         303
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         305
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         384
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         388
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         392
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         412
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         423
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         423
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         429
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         431
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         431
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         433
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         436
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         436
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         439
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         440
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
FT   BINDING         446
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:P05806"
SQ   SEQUENCE   562 AA;  60949 MW;  17203441C7F6AAB7 CRC64;
     MKKKKQALKV LLSVGILSSS FAFAHTSSAA PNNVLSTEKY NKEIKSPEFI SGKLSGPSSQ
     KAQDVVFHYM NTNKDKYKLG NESAQNSFKV TEVVKDPVEQ ATVVRLQQVY NNIPVWGSTQ
     LAHVAKDGTL KVVSGTVAPD LDKKEKLKGQ KQVDSKKAIQ AAEKDLGFKP TYEKSPSSEL
     YVYQNASDTT YAYVVNLNFL SPEPGNYYYF VDAISGKVLD KYNTIDSVAG PKADVKQAAK
     PAAKPVTGTN TIGSGKGVLG DTKSLKTTLS SSTYYLQDNT RGATIYTYDA KNRTSLPGTL
     WADTDNTYNA TRDAAAVDAH YYAGVTYDYY KNKFNRNSYD NAGRPLKSTV HYSSGYNNAF
     WNGSQMVYGD GDGTTFVPLS GGLDVIGHEL THALTERSSN LIYQYESGAL NEAISDIFGT
     LVEYYDNRNP DWEIGEDIYT PGTSGDALRS MSNPAKYGDP DHYSKRYTGS SDNGGVHTNS
     GIINKAAYLL ANGGTHYGVT VTGIGGDKLG KIYYRANTLY FTQSTTFSQA RAGLVQAAAD
     LYGSGSQEVI SVGKSFDAVG VQ
//