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NPRT_GEOSE
ID   NPRT_GEOSE              Reviewed;         548 AA.
AC   P06874;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Thermostable neutral protease NprT;
DE            Short=Thermostable neutral proteinase;
DE            EC=3.4.24.-;
DE   AltName: Full=Stearolysin;
DE   AltName: Full=Thermolysin-like protease;
DE   Flags: Precursor;
GN   Name=nprT;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 230-243, AND
RP   DETERMINATION OF TRANSCRIPTIONAL START SITE.
RC   STRAIN=CU21;
RX   PubMed=2993245; DOI=10.1128/jb.163.3.824-831.1985;
RA   Takagi M., Imanaka T., Aiba S.;
RT   "Nucleotide sequence and promoter region for the neutral protease gene from
RT   Bacillus stearothermophilus.";
RL   J. Bacteriol. 163:824-831(1985).
RN   [2]
RP   FUNCTION AS A PROTEASE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=CU21;
RX   PubMed=6302083; DOI=10.1128/jb.154.2.831-837.1983;
RA   Fujii M., Takagi M., Imanaka T., Aiba S.;
RT   "Molecular cloning of a thermostable neutral protease gene from Bacillus
RT   stearothermophilus in a vector plasmid and its expression in Bacillus
RT   stearothermophilus and Bacillus subtilis.";
RL   J. Bacteriol. 154:831-837(1983).
CC   -!- FUNCTION: Extracellular zinc metalloprotease.
CC       {ECO:0000269|PubMed:6302083}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000305|PubMed:6302083};
CC       Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000305|PubMed:6302083};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000305|PubMed:6302083};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305|PubMed:6302083};
CC   -!- ACTIVITY REGULATION: Its casein hydrolytic activity is inhibited almost
CC       completely by a chelating agent (EDTA), whereas neither diisopropyl
CC       fluorophosphate nor phenylmethylsulfonyl fluoride inhibit the
CC       proteolytic activity in vitro.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is about 7. {ECO:0000269|PubMed:6302083};
CC       Temperature dependence:
CC         Thermostable. Retains about 80% of its activity after treatment of 65
CC         degrees Celsius for 30 minutes. {ECO:0000269|PubMed:6302083};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6302083}.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR   EMBL; M11446; AAA22621.1; -; Genomic_DNA.
DR   PIR; A24924; HYBSS.
DR   AlphaFoldDB; P06874; -.
DR   SMR; P06874; -.
DR   MEROPS; M04.018; -.
DR   KEGG; ag:AAA22621; -.
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; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..229
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:2993245"
FT                   /id="PRO_0000028590"
FT   CHAIN           230..548
FT                   /note="Thermostable neutral protease NprT"
FT                   /id="PRO_0000028591"
FT   ACT_SITE        375
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        463
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         289
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         291
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         293
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         370
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         374
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         378
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         398
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         409
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         409
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         415
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         417
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         417
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         419
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         422
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         422
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         425
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         426
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         429
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         432
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   548 AA;  59580 MW;  5B4D2C1D7910539D CRC64;
     MNKRAMLGAI GLAFGLLAAP IGASAKGESI VWNEQWKTPS FVSGSLLNGG EQALEELVYQ
     YVDRENGTFR LGGRARDRLA LIGKQTDELG HTVMRFEQRH HGIPVYGTML AAHVKDGELI
     ALSGSLIPNL DGQPRLKKAK TVTVQQAEAI AEQDVTETVT KERPTTENGE RTRLVIYPTD
     GTARLAYEVN VRFLTPVPGN WVYIIDATDG AILNKFNQID SRQPGGGQPV AGASTVGVGR
     GVLGDQKYIN TTYSSYYGYY YLQDNTRGSG IFTYDGRNRT VLPGSLWTDG DNQFTASYDA
     AAVDAHYYAG VVYDYYKNVH GRLSYDGSNA AIRSTVHYGR GYNNAFWNGS QMVYGDGDGQ
     TFLPFSGGID VVGHELTHAV TDYTAGLVYQ NESGAINEAM SDIFGTLVEF YANRNPDWEI
     GEDIYTPGVA GDALRSMSDP AKYGDPDHYS KRYTGTQDNG GVHTNSGIIN KAAYLLSQGG
     VHYGVSVNGI GRDKMGKIFY RALVYYLTPT SNFSQLRAAC VQAAADLYGS TSQEVNSVKQ
     AFNAVGVY
 
 
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