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P29148 (NPRE_PAEPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 88. 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

Names and origin

Protein namesRecommended name:
Bacillolysin

EC=3.4.24.28
Alternative name(s):
Neutral protease
Gene names
Name:npr
OrganismPaenibacillus polymyxa (Bacillus polymyxa)
Taxonomic identifier1406 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Protein attributes

Sequence length590 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the generation of beta- and alpha-amylases from the large amylase precursor.

Catalytic activity

Similar, but not identical, to that of thermolysin.

Cofactor

Binds 4 calcium ions per subunit Potential.

Binds 1 zinc ion per subunit Potential.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase M4 family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 286262Activation peptide
PRO_0000028602
Chain287 – 590304Bacillolysin
PRO_0000028603

Sites

Active site4241 By similarity
Active site5071Proton donor By similarity
Metal binding3391Calcium 1 Potential
Metal binding3411Calcium 1 Potential
Metal binding4191Calcium 2 Potential
Metal binding4231Zinc; catalytic By similarity
Metal binding4271Zinc; catalytic By similarity
Metal binding4471Zinc; catalytic By similarity
Metal binding4661Calcium 2 Potential
Metal binding4661Calcium 3 Potential
Metal binding4691Calcium 4; via carbonyl oxygen Potential
Metal binding4701Calcium 4 Potential
Metal binding4731Calcium 4; via carbonyl oxygen Potential
Metal binding4761Calcium 4 Potential

Experimental info

Sequence conflict287 – 2893NEA → ATG AA sequence Ref.1

Secondary structure

..................................................... 590
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29148 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 4ED303761408F6F3

FASTA59063,529
        10         20         30         40         50         60 
MKKVWFSLLG GAMLLGSVAS GASAESSVSG PAQLTPTFHT EQWKAPSSVS GDDIVWSYLN 

        70         80         90        100        110        120 
RQKKSLLGVD SSSVREQFRI VDRTSDKSGV SHYRLKQYVN GIPVYGAEQT IHVGKSGEVT 

       130        140        150        160        170        180 
SYLGAVINED QQEEATQGTT PKISASEAVY TAYKEAAARI EALPTSDDTI SKDAEEPSSV 

       190        200        210        220        230        240 
SKDTYAEAAN NDKTLSVDKD ELSLDKASVL KDSKIEAVEA EKSSIAKIAN LQPEVDPKAE 

       250        260        270        280        290        300 
LYYYPKGDDL LLVYVTEVNV LEPAPLRTRY IIDANDGSIV FQYDIINEAT GKGVLGDSKS 

       310        320        330        340        350        360 
FTTTASGSSY QLKDTTRGNG IVTYTASNRQ SIPGTLLTDA DNVWNDPAGV DAHAYAAKTY 

       370        380        390        400        410        420 
DYYKSKFGRN SIDGRGLQLR STVHYGSRYN NAFWNGSQMT YGDGDGDGST FIAFSGDPDV 

       430        440        450        460        470        480 
VGHELTHGVT EYTSNLEYYG ESGALNEAFS DVIGNDIQRK NWLVGDDIYT PNICGDALRS 

       490        500        510        520        530        540 
MSNPTLYDQP HHYSNLYKGS SDNGGVHTNS GIINKAYYLL AQGGTFHGVT VNGIGRDAAV 

       550        560        570        580        590 
QIYYSAFTNY LTSSSDFSNA RAAVIQAAKD LYGANSAEAT AAAKSFDAVG 

« Hide

References

[1]"Proteases involved in generation of beta- and alpha-amylases from a large amylase precursor in Bacillus polymyxa."
Takekawa S., Uozumi N., Tsukagoshi N., Udaka S.
J. Bacteriol. 173:6820-6825(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 287-301.
Strain: 72.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00861 Genomic DNA. Translation: BAA00734.1.
PIRA41335.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GERX-ray1.59A/B290-590[»]
ProteinModelPortalP29148.
SMRP29148. Positions 289-590.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM04.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.10.170.10. 1 hit.
InterProIPR011096. FTP_domain.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]
PfamPF07504. FTP. 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_PAEPO
AccessionPrimary (citable) accession number: P29148
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: May 14, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references