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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
 
 
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