NPRE_PAEPO
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 03-AUG-2022, entry version 120.
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; 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}.
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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 STRING; 1052684.PPM_4046; -.
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 Gene3D; 1.10.390.10; -; 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 Pfam; PF07504; FTP; 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 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
