ID   NPRE_PAEPO              Reviewed;         590 AA.
AC   P29148;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-NOV-2008, entry version 66.
DE   RecName: Full=Bacillolysin;
DE            EC=3.4.24.28;
DE   AltName: Full=Neutral protease;
DE   Flags: Precursor;
GN   Name=npr;
OS   Paenibacillus polymyxa (Bacillus polymyxa).
OC   Bacteria; Firmicutes; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 287-301.
RC   STRAIN=72;
RX   MEDLINE=92041565; PubMed=1834632;
RA   Takekawa S., Uozumi N., Tsukagoshi N., Udaka S.;
RT   "Proteases involved in generation of beta- and alpha-amylases from a
RT   large amylase precursor in Bacillus polymyxa.";
RL   J. Bacteriol. 173:6820-6825(1991).
CC   -!- FUNCTION: Involved in the generation of beta- and alpha-amylases
CC       from the large amylase precursor.
CC   -!- CATALYTIC ACTIVITY: Similar, but not identical, to that of
CC       thermolysin.
CC   -!- COFACTOR: Binds 4 calcium ions per subunit (Potential).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (Potential).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D00861; BAA00734.1; -; Genomic_DNA.
DR   PIR; A41335; A41335.
DR   HSSP; P05806; 1NPC.
DR   MEROPS; M04.001; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR005075; Pept_M4_propep_PepSY.
DR   InterPro; IPR006025; Pept_M_Zn_BS.
DR   InterPro; IPR013856; Peptidase_M4.
DR   InterPro; IPR001570; Peptidase_M4_C.
DR   InterPro; IPR011096; Propep_M4_M36.
DR   Gene3D; G3DSA:3.10.170.10; Peptidase_M4; 1.
DR   Gene3D; G3DSA:1.10.390.10; Peptidase_M4/M36; 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   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     24       Potential.
FT   PROPEP       25    286       Activation peptide.
FT                                /FTId=PRO_0000028602.
FT   CHAIN       287    590       Bacillolysin.
FT                                /FTId=PRO_0000028603.
FT   ACT_SITE    424    424       By similarity.
FT   ACT_SITE    507    507       Proton donor (By similarity).
FT   METAL       339    339       Calcium 1 (Potential).
FT   METAL       341    341       Calcium 1 (Potential).
FT   METAL       419    419       Calcium 2 (Potential).
FT   METAL       423    423       Zinc; catalytic (By similarity).
FT   METAL       427    427       Zinc; catalytic (By similarity).
FT   METAL       447    447       Zinc; catalytic (By similarity).
FT   METAL       466    466       Calcium 2 (Potential).
FT   METAL       466    466       Calcium 3 (Potential).
FT   METAL       469    469       Calcium 4; via carbonyl oxygen
FT                                (Potential).
FT   METAL       470    470       Calcium 4 (Potential).
FT   METAL       473    473       Calcium 4; via carbonyl oxygen
FT                                (Potential).
FT   METAL       476    476       Calcium 4 (Potential).
FT   CONFLICT    287    289       NEA -> ATG (in Ref. 1; AA sequence).
SQ   SEQUENCE   590 AA;  63529 MW;  4ED303761408F6F3 CRC64;
     MKKVWFSLLG GAMLLGSVAS GASAESSVSG PAQLTPTFHT EQWKAPSSVS GDDIVWSYLN
     RQKKSLLGVD SSSVREQFRI VDRTSDKSGV SHYRLKQYVN GIPVYGAEQT IHVGKSGEVT
     SYLGAVINED QQEEATQGTT PKISASEAVY TAYKEAAARI EALPTSDDTI SKDAEEPSSV
     SKDTYAEAAN NDKTLSVDKD ELSLDKASVL KDSKIEAVEA EKSSIAKIAN LQPEVDPKAE
     LYYYPKGDDL LLVYVTEVNV LEPAPLRTRY IIDANDGSIV FQYDIINEAT GKGVLGDSKS
     FTTTASGSSY QLKDTTRGNG IVTYTASNRQ SIPGTLLTDA DNVWNDPAGV DAHAYAAKTY
     DYYKSKFGRN SIDGRGLQLR STVHYGSRYN NAFWNGSQMT YGDGDGDGST FIAFSGDPDV
     VGHELTHGVT EYTSNLEYYG ESGALNEAFS DVIGNDIQRK NWLVGDDIYT PNICGDALRS
     MSNPTLYDQP HHYSNLYKGS SDNGGVHTNS GIINKAYYLL AQGGTFHGVT VNGIGRDAAV
     QIYYSAFTNY LTSSSDFSNA RAAVIQAAKD LYGANSAEAT AAAKSFDAVG
//