ID NPRM_PRIM3 Reviewed; 562 AA.
AC D5DEH5; Q00891;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Bacillolysin;
DE EC=3.4.24.28;
DE AltName: Full=Neutral protease;
DE Flags: Precursor;
GN Name=nprM; OrderedLocusNames=BMD_2285;
OS Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=592022;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7764969; DOI=10.1007/bf00221230;
RA Meinhardt F., Busskamp M., Wittchen K.D.;
RT "Cloning and sequencing of the leu C and npr M genes and a putative spo IV
RT gene from Bacillus megaterium DSM319.";
RL Appl. Microbiol. Biotechnol. 41:344-351(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 319 / IMG 1521;
RX PubMed=21705586; DOI=10.1128/jb.00449-11;
RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA Bremer E., Jahn D., Ravel J., Vary P.S.;
RT "Genome sequences of the biotechnologically important Bacillus megaterium
RT strains QM B1551 and DSM319.";
RL J. Bacteriol. 193:4199-4213(2011).
CC -!- FUNCTION: Extracellular zinc metalloprotease. {ECO:0000250}.
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:0000250};
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X75070; CAA52964.1; -; Genomic_DNA.
DR EMBL; CP001982; ADF39133.1; -; Genomic_DNA.
DR PIR; I40227; I40227.
DR RefSeq; WP_013083132.1; NZ_CP120609.1.
DR AlphaFoldDB; D5DEH5; -.
DR SMR; D5DEH5; -.
DR MEROPS; M04.001; -.
DR KEGG; bmd:BMD_2285; -.
DR HOGENOM; CLU_008590_5_2_9; -.
DR Proteomes; UP000002365; Chromosome.
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 3: Inferred from homology;
KW Calcium; Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted;
KW Signal; Zinc; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..245
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000396525"
FT CHAIN 246..562
FT /note="Bacillolysin"
FT /id="PRO_0000396526"
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; 60862 MW; BE1F088C0844F49A CRC64;
MKKKKQALKV LLSVGILSSS FAFAHTSSAA PNNVLSTEKY NKEIKSPEFI SGKLSGPSSQ
KAQDVVFHYM NTNKDKYKLG NENAQNSFKV TEVVKDPVEQ ATVVRLQQVY NNIPVWGSTQ
LAHVAKDGTL KVVSGTVAPD LDKKEKLKGQ KQVDSKKAIQ AAEKDLGFKP TYEKSPSSEL
YVYQNGSDTT YAYVVNLNFL SPEPGNYYYF VDAISGKVLD KYNTIDSVAG PKADVKQAAK
PAAKPVTGTN AIGSGKGVLG DTKSLKTTLS SSTYYLQDNT RGATIYTYDA KNRTSLPGTL
WTDTDNTYNA TRDAAAVDAH YYAGVTYDYY KNKFNRNSYD NAGAPLKSTV HYSSGYNNAF
WNGSQMVYGD GDGTTFVPLS GGLDVIGHEL THAVTERSSN LIYQYESGAL NEAISDIFGT
LVEYYDNRNP DWEIGEDIYT PGTSGDALRS MSNPAKYGDP DHYSKRYTGS SDNGGVHTNS
GIINKAAYLL ANGGTHYGVT VTGIGGDKLG KIYYRANTLY FTQSTTFSQA RAGLVQAAAD
LYGSGSQEVI SVGKSFDAVG VQ
//
