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 24-JAN-2024, entry version 123. 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; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus. OX NCBI_TaxID=1406; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 287-301. RC STRAIN=72; RX PubMed=1834632; DOI=10.1128/jb.173.21.6820-6825.1991; RA Takekawa S., Uozumi N., Tsukagoshi N., Udaka S.; RT "Proteases involved in generation of beta- and alpha-amylases from a large RT amylase precursor in Bacillus polymyxa."; RL J. Bacteriol. 173:6820-6825(1991). CC -!- FUNCTION: Involved in the generation of beta- and alpha-amylases from CC the large amylase precursor. 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 -!- 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; D00861; BAA00734.1; -; Genomic_DNA. DR PIR; A41335; A41335. DR PDB; 4GER; X-ray; 1.59 A; A/B=290-590. DR PDBsum; 4GER; -. DR AlphaFoldDB; P29148; -. DR SMR; P29148; -. DR MEROPS; M04.018; -. 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 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; 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; 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 1: Evidence at protein level; KW 3D-structure; Calcium; Direct protein sequencing; Hydrolase; Metal-binding; KW Metalloprotease; Protease; Secreted; Signal; Zinc; Zymogen. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT PROPEP 25..286 FT /note="Activation peptide" FT /evidence="ECO:0000269|PubMed:1834632" FT /id="PRO_0000028602" FT CHAIN 287..590 FT /note="Bacillolysin" FT /id="PRO_0000028603" FT ACT_SITE 424 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT ACT_SITE 507 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT BINDING 339 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255" FT BINDING 341 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255" FT BINDING 419 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255" FT BINDING 423 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT BINDING 427 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT BINDING 447 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT BINDING 466 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255" FT BINDING 466 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255" FT BINDING 469 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255" FT BINDING 470 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255" FT BINDING 473 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255" FT BINDING 476 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255" FT CONFLICT 287..289 FT /note="NEA -> ATG (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 289..292 FT /evidence="ECO:0007829|PDB:4GER" FT STRAND 298..302 FT /evidence="ECO:0007829|PDB:4GER" FT STRAND 304..306 FT /evidence="ECO:0007829|PDB:4GER" FT STRAND 309..314 FT /evidence="ECO:0007829|PDB:4GER" FT STRAND 321..325 FT /evidence="ECO:0007829|PDB:4GER" FT STRAND 338..344 FT /evidence="ECO:0007829|PDB:4GER" FT HELIX 347..367 FT /evidence="ECO:0007829|PDB:4GER" FT TURN 371..373 FT /evidence="ECO:0007829|PDB:4GER" FT STRAND 379..388 FT /evidence="ECO:0007829|PDB:4GER" FT STRAND 392..394 FT /evidence="ECO:0007829|PDB:4GER" FT STRAND 399..402 FT /evidence="ECO:0007829|PDB:4GER" FT STRAND 408..411 FT /evidence="ECO:0007829|PDB:4GER" FT HELIX 414..416 FT /evidence="ECO:0007829|PDB:4GER" FT HELIX 418..431 FT /evidence="ECO:0007829|PDB:4GER" FT TURN 432..434 FT /evidence="ECO:0007829|PDB:4GER" FT HELIX 440..458 FT /evidence="ECO:0007829|PDB:4GER" FT STRAND 460..465 FT /evidence="ECO:0007829|PDB:4GER" FT HELIX 466..468 FT /evidence="ECO:0007829|PDB:4GER" FT STRAND 478..482 FT /evidence="ECO:0007829|PDB:4GER" FT HELIX 484..487 FT /evidence="ECO:0007829|PDB:4GER" FT HELIX 493..495 FT /evidence="ECO:0007829|PDB:4GER" FT HELIX 501..522 FT /evidence="ECO:0007829|PDB:4GER" FT STRAND 524..526 FT /evidence="ECO:0007829|PDB:4GER" FT STRAND 529..531 FT /evidence="ECO:0007829|PDB:4GER" FT HELIX 536..549 FT /evidence="ECO:0007829|PDB:4GER" FT HELIX 557..572 FT /evidence="ECO:0007829|PDB:4GER" FT HELIX 577..589 FT /evidence="ECO:0007829|PDB:4GER" 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 //