Skip Header

Contribute Send feedback
Read comments (?) or add your own

P05806 (NPRE_BACCE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bacillolysin
EC=3.4.24.28
Alternative name(s):
Neutral protease
Gene names
Name:npr
Synonyms:nprC
OrganismBacillus cereus
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length566 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Extracellular zinc metalloprotease.

Catalytic activity

Similar, but not identical, to that of thermolysin.

Cofactor

Binds 4 calcium ions per subunit.

Binds 1 zinc ion per subunit.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase M4 family.

Biophysicochemical properties

Temperature dependence:

Thermolabile.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Propeptide28 – 249222Activation peptide
PRO_0000028598
Chain250 – 566317Bacillolysin
PRO_0000028599

Sites

Active site3931
Active site4811Proton donor
Metal binding3071Calcium 1 Ref.5
Metal binding3091Calcium 1 Ref.5
Metal binding3111Calcium 1; via carbonyl oxygen
Metal binding3881Calcium 2 Ref.5
Metal binding3921Zinc; catalytic Ref.5
Metal binding3961Zinc; catalytic Ref.5
Metal binding4161Zinc; catalytic Ref.5
Metal binding4271Calcium 2 Ref.5
Metal binding4271Calcium 3 Ref.5
Metal binding4331Calcium 3; via carbonyl oxygen
Metal binding4351Calcium 2 Ref.5
Metal binding4351Calcium 3 Ref.5
Metal binding4371Calcium 2; via carbonyl oxygen
Metal binding4401Calcium 2 Ref.5
Metal binding4401Calcium 3 Ref.5
Metal binding4431Calcium 4; via carbonyl oxygen
Metal binding4441Calcium 4 Ref.5
Metal binding4471Calcium 4; via carbonyl oxygen
Metal binding4501Calcium 4 Ref.5

Secondary structure

1 ...................................................... 566
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05806 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: E18B4572C2C4E1D3

FASTA56660,919
        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

« Hide

References

[1]"The role of the pro-sequence in the processing and secretion of the thermolysin-like neutral protease from Bacillus cereus."
Wetmore D.R., Wong S.L., Roche R.S.
Mol. Microbiol. 6:1593-1604(1992) [PubMed: 1495388] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The primary structure of Bacillus cereus neutral proteinase and comparison with thermolysin and Bacillus subtilis neutral proteinase."
Sidler W., Niederer E., Suter F., Zuber H.
Biol. Chem. Hoppe-Seyler 367:643-657(1986) [PubMed: 3092843] [Abstract]
Cited for: PROTEIN SEQUENCE OF 250-566.
Strain: DSM 3101.
[3]"Crystal structure of neutral protease from Bacillus cereus refined at 3.0-A resolution and comparison with the homologous but more thermostable enzyme thermolysin."
Pauptit R.A., Karlsson R., Picot D., Jenkins J.A., Niklaus-Reimer A.-S., Jansonius J.N.
J. Mol. Biol. 199:525-537(1988) [PubMed: 3127592] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[4]"The structure of neutral protease from Bacillus cereus at 0.2-nm resolution."
Stark W., Pauptit R.A., Wilson K.S., Jansonius J.N.
Eur. J. Biochem. 207:781-791(1992) [PubMed: 1633827] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]"E144S active-site mutant of the Bacillus cereus thermolysin-like neutral protease at 2.8-A resolution."
Lister S.A., Wetmore D.R., Roche R.S., Codding P.W.
Acta Crystallogr. D 52:543-550(1996) [PubMed: 15299677] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT SER-393.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M83910 Genomic DNA. Translation: AAA22620.1.
PIRHYBSU. S22690.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ESPX-ray2.80A250-566[»]
1NPCX-ray2.00A250-566[»]
ProteinModelPortalP05806.
SMRP05806. Positions 250-566.
ModBaseSearch...

Protein family/group databases

MEROPSM04.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR011096. FTP_domain.
IPR005075. Pept_M4_propep_PepSY.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]
Gene3DG3DSA:3.10.170.10. Peptidase_M4. 1 hit.
G3DSA:1.10.390.10. Peptidase_M4/M36. 1 hit.
PfamPF07504. FTP. 1 hit.
PF03413. PepSY. 1 hit.
PF01447. Peptidase_M4. 1 hit.
PF02868. Peptidase_M4_C. 1 hit.
[Graphical view]
PRINTSPR00730. THERMOLYSIN.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNPRE_BACCE
AccessionPrimary (citable) accession number: P05806
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1996
Last modified: January 25, 2012
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents