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NPRE_BACAM
ID   NPRE_BACAM              Reviewed;         521 AA.
AC   P06832;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Bacillolysin;
DE            EC=3.4.24.28;
DE   AltName: Full=Neutral protease;
DE   Flags: Precursor;
GN   Name=npr;
OS   Bacillus amyloliquefaciens (Bacillus velezensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=1390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23844 / P;
RX   PubMed=6090391; DOI=10.1128/jb.159.3.811-819.1984;
RA   Vasantha N., Thompson L.D., Rhodes C., Banner C., Nagle J., Filpula D.;
RT   "Genes for alkaline protease and neutral protease from Bacillus
RT   amyloliquefaciens contain a large open reading frame between the regions
RT   coding for signal sequence and mature protein.";
RL   J. Bacteriol. 159:811-819(1984).
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}.
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DR   EMBL; K02497; AAB05346.1; -; Genomic_DNA.
DR   PIR; A25415; HYBSN.
DR   RefSeq; WP_014470445.1; NZ_VRTX01000003.1.
DR   AlphaFoldDB; P06832; -.
DR   SMR; P06832; -.
DR   STRING; 692420.BAMF_1546; -.
DR   MEROPS; M04.014; -.
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; 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; Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted;
KW   Signal; Zinc; Zymogen.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..221
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028594"
FT   CHAIN           222..521
FT                   /note="Bacillolysin"
FT                   /id="PRO_0000028595"
FT   ACT_SITE        365
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        449
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         283
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         360
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         364
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         368
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         388
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         399
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         399
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255"
FT   BINDING         402
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         402
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="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         407
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         407
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
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   521 AA;  56840 MW;  9609FA0416222751 CRC64;
     MGLGKKLSVA VAASFMSLTI SLPGVQAAEN PQLKENLTNF VPKHSLVQSE LPSVSDKAIK
     QYLKQNGKVF KGNPSERLKL IDQTTDDLGY KHFRYVPVVN GVPVKDSQVI IHVDKSNNVY
     AINGELNNDV SAKTANSKKL SANQALDHAY KAIGKSPEAV SNGTVANKNK AELKAAATKD
     GKYRLAYDVT IRYIEPEPAN WEVTVDAETG KILKKQNKVE HAATTGTGTT LKGKTVSLNI
     SSESGKYVLR DLSKPTGTQI ITYDLQNREY NLPGTLVSST TNQFTTSSQR AAVDAHYNLG
     KVYDYFYQKF NRNSYDNKGG KIVSSVHYGS RYNNAAWIGD QMIYGDGDGS FFSPLSGSMD
     VTAHEMTHGV TQETANLNYE NQPGALNESF SDVFGYFNDT EDWDIGEDIT VSQPALRSLS
     NPTKYGQPDN FKNYKNLPNT DAGDYGGVHT NSGIPNKAAY NTITKIGVNK AEQIYYRALT
     VYLTPSSTFK DAKAALIQSA RDLYGSQDAA SVEAAWNAVG L
 
 
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