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UniProtKB/Swiss-Prot entry P05806


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NPRE_BACCE
Primary accession number P05806
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on October 1, 1996 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 86)
Name and origin of the protein
Protein name Bacillolysin [Precursor]
Synonyms EC 3.4.24.28
Neutral protease
Gene name
Name: npr
Synonyms: nprC
From
Bacillus cereus [TaxID: 1396] 
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus group.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1495388 [NCBI, ExPASy, EBI, Israel, Japan]
Wetmore D.R., Wong S.L., Roche R.S.;
"The role of the pro-sequence in the processing and secretion of the thermolysin-like neutral protease from Bacillus cereus.";
Mol. Microbiol. 6:1593-1604(1992).
[2]
PROTEIN SEQUENCE OF 250-566.
STRAIN=DSM 3101;
PubMed=3092843 [NCBI, ExPASy, EBI, Israel, Japan]
Sidler W., Niederer E., Suter F., Zuber H.;
"The primary structure of Bacillus cereus neutral proteinase and comparison with thermolysin and Bacillus subtilis neutral proteinase.";
Biol. Chem. Hoppe-Seyler 367:643-657(1986).
[3]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
DOI=10.1016/0022-2836(88)90623-7; PubMed=3127592 [NCBI, ExPASy, EBI, Israel, Japan]
Pauptit R.A., Karlsson R., Picot D., Jenkins J.A., Niklaus-Reimer A.-S., Jansonius J.N.;
"Crystal structure of neutral protease from Bacillus cereus refined at 3.0-A resolution and comparison with the homologous but more thermostable enzyme thermolysin.";
J. Mol. Biol. 199:525-537(1988).
[4]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=1633827 [NCBI, ExPASy, EBI, Israel, Japan]
Stark W., Pauptit R.A., Wilson K.S., Jansonius J.N.;
"The structure of neutral protease from Bacillus cereus at 0.2-nm resolution.";
Eur. J. Biochem. 207:781-791(1992).
[5]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT SER-393.
DOI=10.1107/S0907444995016684; PubMed=15299677 [NCBI, ExPASy, EBI, Israel, Japan]
Lister S.A., Wetmore D.R., Roche R.S., Codding P.W.;
"E144S active-site mutant of the Bacillus cereus thermolysin-like neutral protease at 2.8-A resolution.";
Acta Crystallogr. D 52:543-550(1996).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M83910; AAA22620.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S22690; HYBSU.
3D structure databases
PDB
1ESP; X-ray; 2.80 A; A=250-566.[ExPASy / RCSB / EBI]
1NPC; X-ray; 2.00 A; A=250-566.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ESP; -.
1NPC; -.
ModBase P05806.
Protein family/group databases
MEROPS M04.001; -.
Ontologies
GO
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR005075; Pept_M4_propep_PepSY.
IPR006025; Pept_M_Zn_BS.
IPR013856; Peptidase_M4.
IPR001570; Peptidase_M4_C.
IPR011096; Propep_M4_M36.
Graphical view of domain structure.
Gene3D G3DSA:3.10.170.10; Peptidase_M4; 1.
G3DSA:1.10.390.10; Peptidase_M4/M36; 1.
Pfam PF07504; FTP; 1.
PF03413; PepSY; 1.
PF01447; Peptidase_M4; 1.
PF02868; Peptidase_M4_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00730; THERMOLYSIN.
PROSITE PS00142; ZINC_PROTEASE; 1.
BLOCKS P05806.
ProtoNet P05806.
Other
LinkHub P05806; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    27  27     Potential. 
PROPEP   28   249  222     Activation peptide. PRO_0000028598
CHAIN   250   566  317     Bacillolysin. PRO_0000028599
ACT_SITE   393   393         
ACT_SITE   481   481        Proton donor. 
METAL   307   307        Calcium 1. 
METAL   309   309        Calcium 1. 
METAL   311   311        Calcium 1; via carbonyl oxygen. 
METAL   388   388        Calcium 2. 
METAL   392   392        Zinc; catalytic. 
METAL   396   396        Zinc; catalytic. 
METAL   416   416        Zinc; catalytic. 
METAL   427   427        Calcium 2. 
METAL   427   427        Calcium 3. 
METAL   433   433        Calcium 3; via carbonyl oxygen. 
METAL   435   435        Calcium 2. 
METAL   435   435        Calcium 3. 
METAL   437   437        Calcium 2; via carbonyl oxygen. 
METAL   440   440        Calcium 2. 
METAL   440   440        Calcium 3. 
METAL   443   443        Calcium 4; via carbonyl oxygen. 
METAL   444   444        Calcium 4. 
METAL   447   447        Calcium 4; via carbonyl oxygen. 
METAL   450   450        Calcium 4. 
STRAND   253   260  8      
STRAND   266   274  9      
STRAND   277   282  6      
STRAND   284   287  4      
STRAND   289   298  10      
STRAND   306   312  7      
HELIX   315   317  3      
HELIX   318   338  21      
TURN   342   345  4      
STRAND   350   359  10      
STRAND   363   365  3      
STRAND   367   372  6      
STRAND   377   380  4      
HELIX   383   385  3      
HELIX   387   400  14      
TURN   401   403  3      
HELIX   409   429  21      
STRAND   436   439  4      
TURN   440   442  3      
STRAND   452   456  5      
HELIX   458   461  4      
HELIX   467   469  3      
HELIX   475   496  22      
STRAND   498   500  3      
STRAND   503   505  3      
HELIX   510   523  14      
HELIX   531   546  16      
HELIX   551   562  12      
Sequence information
Length: 566 AA [This is the length of the unprocessed precursor] Molecular weight: 60919 Da [This is the MW of the unprocessed precursor] CRC64: E18B4572C2C4E1D3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKKKSLALVL ATGMAVTTFG GTGSAFADSK NVLSTKKYNE TVQSPEFISG DLTEATGKKA 

        70         80         90        100        110        120 
ESVVFDYLNA AKGDYKLGEK SAQDSFKVKQ VKKDAVTDST VVRMQQVYEG VPVWGSTQVA 

       130        140        150        160        170        180 
HVSKDGSLKV LSGTVAPDLD KKEKLKNKNK IEGAKAIEIA QQDLGVTPKY EVEPKADLYV 

       190        200        210        220        230        240 
YQNGEETTYA YVVNLNFLDP SPGNYYYFIE ADSGKVLNKF NTIDHVTNDD KSPVKQEAPK 

       250        260        270        280        290        300 
QDAKAVVKPV TGTNKVGTGK GVLGDTKSLN TTLSGSSYYL QDNTRGATIF TYDAKNRSTL 

       310        320        330        340        350        360 
PGTLWADADN VFNAAYDAAA VDAHYYAGKT YDYYKATFNR NSINDAGAPL KSTVHYGSNY 

       370        380        390        400        410        420 
NNAFWNGSQM VYGDGDGVTF TSLSGGIDVI GHELTHAVTE NSSNLIYQNE SGALNEAISD 

       430        440        450        460        470        480 
IFGTLVEFYD NRNPDWEIGE DIYTPGKAGD ALRSMSDPTK YGDPDHYSKR YTGSSDNGGV 

       490        500        510        520        530        540 
HTNSGIINKQ AYLLANGGTH YGVTVTGIGK DKLGAIYYRA NTQYFTQSTT FSQARAGAVQ 

       550        560 
AAADLYGANS AEVAAVKQSF SAVGVN 

P05806 in FASTA format

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