NPRM_PRIM2
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-AUG-2022, entry version 44.
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; Firmicutes; 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 9376
RC / 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 Gene3D; 1.10.390.10; -; 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 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 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
