NPRE_BREBE
ID NPRE_BREBE Reviewed; 527 AA.
AC P43263;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Bacillolysin;
DE EC=3.4.24.28;
DE AltName: Full=Neutral protease;
DE Flags: Precursor;
GN Name=npr;
OS Brevibacillus brevis (Bacillus brevis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1393;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=7882;
RX PubMed=2290427;
RA Avakov A.S., Bolotin A.P., Sorokin A.V.;
RT "Structure of the Bacillus brevis metalloprotease gene.";
RL Mol. Biol. (Mosk.) 24:1363-1372(1990).
RN [2]
RP PROTEIN SEQUENCE OF 224-228, AND CHARACTERIZATION.
RX PubMed=2127074;
RA Kaidalova N.V., Akimkina T.V., Khodova O.D., Kostrov S.V., Strongin A.Y.;
RT "Analysis of the structure of Bacillus brevis neutral proteinase and its
RT biosynthesis in Bacillus subtilis cells.";
RL Mol. Biol. (Mosk.) 24:1381-1392(1990).
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}.
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; X61286; CAA43589.1; -; Genomic_DNA.
DR PIR; PN0114; PN0114.
DR AlphaFoldDB; P43263; -.
DR SMR; P43263; -.
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; Direct protein sequencing; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..223
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:2127074"
FT /id="PRO_0000028596"
FT CHAIN 224..527
FT /note="Bacillolysin"
FT /id="PRO_0000028597"
FT ACT_SITE 359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 442
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 401
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="4"
FT /evidence="ECO:0000255"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
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 527 AA; 58646 MW; 8D3704C3C9D8D756 CRC64;
MKKSYLATSL TLSIAVGVSG FTSVPAFAKT KIDYHKQWDT PQYIGEVWEP EGAKGDDVVW
SYLEKYKDEF RIQGNVEDHF EIVNEARNKE TDTKHYRLQE VYNGIPIYGF QQTVHIDADG
NVTSFLGQFI PDLDSNKQLK KKPKLNEQKA VKQAIKDVEG EVGEKPDFIQ DPEAKLYIYV
HEDESYLAYA VELNFLDPEP GRWMYFIDAH SGDVINKYNM LDHVTATGKG VLGDTKQFET
TKQGSTYMLK DTTRGKGIET YTANNRTSLP GTLMTDSDNY WTDGAAVDAH AHAQKTYDYF
RNVHNRNSYD GNGAVIRSTV HYSTRYNNAF WNGSQMVYGD GDGTTFLPLS GGLDVVAHEL
THAVTERTAG LVYQNESGAL NESMSDIFGA MVDNDDWLMG EDIYTPGRSG DALRSLQDPA
AYGDPDHYSK RYTGSQDNGG VHTNSGINNK AAYLLAEGGT HYGVRVNGIG RTDTAKIYYH
ALTHYLTPYS NFSAMRRAAV LSATDLFGAN SRQVQAVNAA YDAVGVK
