NPRE_BACSA
ID NPRE_BACSA Reviewed; 521 AA.
AC P68735; P06142; P25268;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Bacillolysin;
DE EC=3.4.24.28;
DE AltName: Full=MCP 76;
DE AltName: Full=Neutral protease;
DE Flags: Precursor;
GN Name=nprE;
OS Bacillus subtilis subsp. amylosacchariticus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1483;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yoshimoto T., Oyama H., Takeshita T., Higashi H., Xu S., Tsuru D.;
RT "Nucleotide sequence of the neutral protease gene from Bacillus subtillis
RT var, amylosacchariticus.";
RL J. Ferment. Bioeng. 70:370-375(1991).
RN [2]
RP PROTEIN SEQUENCE OF 222-521.
RA Kobayashi R., Yoshimoto T., Tsuru D.;
RT "Complete amino acid sequence of neutral protease from Bacillus subtilis
RT var. amylosacchariticus.";
RL Agric. Biol. Chem. 53:2737-2749(1989).
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:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
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 EMBL; D10773; BAA01604.1; -; Genomic_DNA.
DR AlphaFoldDB; P68735; -.
DR SMR; P68735; -.
DR MEROPS; M04.014; -.
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; Direct protein sequencing; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..221
FT /note="Activation peptide"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000028604"
FT CHAIN 222..521
FT /note="Bacillolysin"
FT /id="PRO_0000028605"
FT ACT_SITE 365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 449
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 360
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 388
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 402
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 402
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 521 AA; 56522 MW; 439E7B8F19D1E8F4 CRC64;
MGLGKKLSVA VAASFMSLSI SLPGVQAAEG HQLKENQTNF LSKNAIAQSE LSAPNDKAVK
QFLKKNSNIF KGDPSKRLKL VESTTDALGY KHFRYAPVVN GVPIKDSQVI VHVDKSDNVY
AVNGELHNQS AAKTDNSQKV SSEKALALAF KAIGKSPDAV SNGAAKNSNK AELKAIETKD
GSYRLAYDVT IRYVEPEPAN WEVLVDAETG SILKQQNKVE HAAATGSGTT LKGATVPLNI
SYEGGKYVLR DLSKPTGTQI ITYDLQNRQS RLPGTLVSST TKTFTSSSQR AAVDAHYNLG
KVYDYFYSNF KRNSYDNKGS KIVSSVHYGT QYNNAAWTGD QMIYGDGDGS FFSPLSGSLD
VTAHEMTHGV TQETANLIYE NQPGALNESF SDVFGYFNDT EDWDIGEDIT VSQPALRSLS
NPTKYNQPDN YANYRNLPNT DEGDYGGVHT NSGIPNKAAY NTITKLGVSK SQQIYYRALT
TYLTPSSTFK DAKAALIQSA RDLYGSTDAA KVEAAWNAVG L
