NPRE_BACAM
ID NPRE_BACAM Reviewed; 521 AA.
AC P06832;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Bacillolysin;
DE EC=3.4.24.28;
DE AltName: Full=Neutral protease;
DE Flags: Precursor;
GN Name=npr;
OS Bacillus amyloliquefaciens (Bacillus velezensis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=1390;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23844 / P;
RX PubMed=6090391; DOI=10.1128/jb.159.3.811-819.1984;
RA Vasantha N., Thompson L.D., Rhodes C., Banner C., Nagle J., Filpula D.;
RT "Genes for alkaline protease and neutral protease from Bacillus
RT amyloliquefaciens contain a large open reading frame between the regions
RT coding for signal sequence and mature protein.";
RL J. Bacteriol. 159:811-819(1984).
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; K02497; AAB05346.1; -; Genomic_DNA.
DR PIR; A25415; HYBSN.
DR RefSeq; WP_014470445.1; NZ_VRTX01000003.1.
DR AlphaFoldDB; P06832; -.
DR SMR; P06832; -.
DR STRING; 692420.BAMF_1546; -.
DR MEROPS; M04.014; -.
DR eggNOG; COG3227; Bacteria.
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..27
FT /evidence="ECO:0000255"
FT PROPEP 28..221
FT /note="Activation peptide"
FT /id="PRO_0000028594"
FT CHAIN 222..521
FT /note="Bacillolysin"
FT /id="PRO_0000028595"
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 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 360
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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="2"
FT /evidence="ECO:0000255"
FT BINDING 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
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 402
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255"
SQ SEQUENCE 521 AA; 56840 MW; 9609FA0416222751 CRC64;
MGLGKKLSVA VAASFMSLTI SLPGVQAAEN PQLKENLTNF VPKHSLVQSE LPSVSDKAIK
QYLKQNGKVF KGNPSERLKL IDQTTDDLGY KHFRYVPVVN GVPVKDSQVI IHVDKSNNVY
AINGELNNDV SAKTANSKKL SANQALDHAY KAIGKSPEAV SNGTVANKNK AELKAAATKD
GKYRLAYDVT IRYIEPEPAN WEVTVDAETG KILKKQNKVE HAATTGTGTT LKGKTVSLNI
SSESGKYVLR DLSKPTGTQI ITYDLQNREY NLPGTLVSST TNQFTTSSQR AAVDAHYNLG
KVYDYFYQKF NRNSYDNKGG KIVSSVHYGS RYNNAAWIGD QMIYGDGDGS FFSPLSGSMD
VTAHEMTHGV TQETANLNYE NQPGALNESF SDVFGYFNDT EDWDIGEDIT VSQPALRSLS
NPTKYGQPDN FKNYKNLPNT DAGDYGGVHT NSGIPNKAAY NTITKIGVNK AEQIYYRALT
VYLTPSSTFK DAKAALIQSA RDLYGSQDAA SVEAAWNAVG L
