NPRE_BACCE
ID NPRE_BACCE Reviewed; 566 AA.
AC P05806;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Bacillolysin;
DE EC=3.4.24.28;
DE AltName: Full=Neutral protease;
DE Flags: Precursor;
GN Name=npr; Synonyms=nprC;
OS Bacillus cereus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1396;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1495388; DOI=10.1111/j.1365-2958.1992.tb00884.x;
RA Wetmore D.R., Wong S.L., Roche R.S.;
RT "The role of the pro-sequence in the processing and secretion of the
RT thermolysin-like neutral protease from Bacillus cereus.";
RL Mol. Microbiol. 6:1593-1604(1992).
RN [2]
RP PROTEIN SEQUENCE OF 250-566.
RC STRAIN=DSM 3101 / x-3;
RX PubMed=3092843; DOI=10.1515/bchm3.1986.367.2.643;
RA Sidler W., Niederer E., Suter F., Zuber H.;
RT "The primary structure of Bacillus cereus neutral proteinase and comparison
RT with thermolysin and Bacillus subtilis neutral proteinase.";
RL Biol. Chem. Hoppe-Seyler 367:643-657(1986).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=3127592; DOI=10.1016/0022-2836(88)90623-7;
RA Pauptit R.A., Karlsson R., Picot D., Jenkins J.A., Niklaus-Reimer A.-S.,
RA Jansonius J.N.;
RT "Crystal structure of neutral protease from Bacillus cereus refined at 3.0-
RT A resolution and comparison with the homologous but more thermostable
RT enzyme thermolysin.";
RL J. Mol. Biol. 199:525-537(1988).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=1633827; DOI=10.1111/j.1432-1033.1992.tb17109.x;
RA Stark W., Pauptit R.A., Wilson K.S., Jansonius J.N.;
RT "The structure of neutral protease from Bacillus cereus at 0.2-nm
RT resolution.";
RL Eur. J. Biochem. 207:781-791(1992).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT SER-393.
RX PubMed=15299677; DOI=10.1107/s0907444995016684;
RA Lister S.A., Wetmore D.R., Roche R.S., Codding P.W.;
RT "E144S active-site mutant of the Bacillus cereus thermolysin-like neutral
RT protease at 2.8-A resolution.";
RL Acta Crystallogr. D 52:543-550(1996).
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;
CC Note=Binds 4 Ca(2+) ions per subunit.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
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; M83910; AAA22620.1; -; Genomic_DNA.
DR PIR; S22690; HYBSU.
DR RefSeq; WP_000730369.1; NZ_VTRD01000011.1.
DR PDB; 1ESP; X-ray; 2.80 A; A=250-566.
DR PDB; 1NPC; X-ray; 2.00 A; A=250-566.
DR PDBsum; 1ESP; -.
DR PDBsum; 1NPC; -.
DR AlphaFoldDB; P05806; -.
DR SMR; P05806; -.
DR STRING; 1396.DJ87_4515; -.
DR MEROPS; M04.001; -.
DR PATRIC; fig|1396.444.peg.2749; -.
DR eggNOG; COG3227; Bacteria.
DR EvolutionaryTrace; P05806; -.
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 3D-structure; Calcium; Direct protein sequencing; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Secreted; Signal; Zinc.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..249
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:3092843"
FT /id="PRO_0000028598"
FT CHAIN 250..566
FT /note="Bacillolysin"
FT /id="PRO_0000028599"
FT ACT_SITE 393
FT ACT_SITE 481
FT /note="Proton donor"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15299677"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15299677"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15299677"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:15299677"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:15299677"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:15299677"
FT BINDING 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15299677"
FT BINDING 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15299677"
FT BINDING 433
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15299677"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15299677"
FT BINDING 437
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 440
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15299677"
FT BINDING 440
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15299677"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:15299677"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 450
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:15299677"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:1NPC"
FT STRAND 266..274
FT /evidence="ECO:0007829|PDB:1NPC"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:1NPC"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:1NPC"
FT STRAND 289..298
FT /evidence="ECO:0007829|PDB:1NPC"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:1NPC"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:1NPC"
FT HELIX 318..338
FT /evidence="ECO:0007829|PDB:1NPC"
FT TURN 342..345
FT /evidence="ECO:0007829|PDB:1NPC"
FT STRAND 350..359
FT /evidence="ECO:0007829|PDB:1NPC"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:1NPC"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:1NPC"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:1NPC"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:1NPC"
FT HELIX 387..400
FT /evidence="ECO:0007829|PDB:1NPC"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:1NPC"
FT HELIX 409..429
FT /evidence="ECO:0007829|PDB:1NPC"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:1NPC"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:1NPC"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:1ESP"
FT STRAND 452..456
FT /evidence="ECO:0007829|PDB:1NPC"
FT HELIX 458..461
FT /evidence="ECO:0007829|PDB:1NPC"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:1NPC"
FT HELIX 475..496
FT /evidence="ECO:0007829|PDB:1NPC"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:1NPC"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:1NPC"
FT HELIX 510..523
FT /evidence="ECO:0007829|PDB:1NPC"
FT HELIX 531..546
FT /evidence="ECO:0007829|PDB:1NPC"
FT HELIX 551..562
FT /evidence="ECO:0007829|PDB:1NPC"
SQ SEQUENCE 566 AA; 60919 MW; E18B4572C2C4E1D3 CRC64;
MKKKSLALVL ATGMAVTTFG GTGSAFADSK NVLSTKKYNE TVQSPEFISG DLTEATGKKA
ESVVFDYLNA AKGDYKLGEK SAQDSFKVKQ VKKDAVTDST VVRMQQVYEG VPVWGSTQVA
HVSKDGSLKV LSGTVAPDLD KKEKLKNKNK IEGAKAIEIA QQDLGVTPKY EVEPKADLYV
YQNGEETTYA YVVNLNFLDP SPGNYYYFIE ADSGKVLNKF NTIDHVTNDD KSPVKQEAPK
QDAKAVVKPV TGTNKVGTGK GVLGDTKSLN TTLSGSSYYL QDNTRGATIF TYDAKNRSTL
PGTLWADADN VFNAAYDAAA VDAHYYAGKT YDYYKATFNR NSINDAGAPL KSTVHYGSNY
NNAFWNGSQM VYGDGDGVTF TSLSGGIDVI GHELTHAVTE NSSNLIYQNE SGALNEAISD
IFGTLVEFYD NRNPDWEIGE DIYTPGKAGD ALRSMSDPTK YGDPDHYSKR YTGSSDNGGV
HTNSGIINKQ AYLLANGGTH YGVTVTGIGK DKLGAIYYRA NTQYFTQSTT FSQARAGAVQ
AAADLYGANS AEVAAVKQSF SAVGVN
