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D5DEH5 (NPRM_BACMD) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:nprM
Ordered Locus Names:BMD_2285
OrganismBacillus megaterium (strain DSM 319) [Complete proteome] [HAMAP]
Taxonomic identifier592022 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length562 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Extracellular zinc metalloprotease By similarity.

Catalytic activity

Similar, but not identical, to that of thermolysin.

Cofactor

Binds 4 calcium ions per subunit By similarity.

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the peptidase M4 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMZymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 245221Activation peptide Potential
PRO_0000396525
Chain246 – 562317Bacillolysin
PRO_0000396526

Sites

Active site3891 By similarity
Active site4771Proton donor By similarity
Metal binding3031Calcium 1 By similarity
Metal binding3051Calcium 1 By similarity
Metal binding3841Calcium 2 By similarity
Metal binding3881Zinc; catalytic By similarity
Metal binding3921Zinc; catalytic By similarity
Metal binding4121Zinc; catalytic By similarity
Metal binding4231Calcium 2 By similarity
Metal binding4231Calcium 3 By similarity
Metal binding4291Calcium 3; via carbonyl oxygen By similarity
Metal binding4311Calcium 2 By similarity
Metal binding4311Calcium 3 By similarity
Metal binding4331Calcium 2; via carbonyl oxygen By similarity
Metal binding4361Calcium 2 By similarity
Metal binding4361Calcium 3 By similarity
Metal binding4391Calcium 4; via carbonyl oxygen By similarity
Metal binding4401Calcium 4 By similarity
Metal binding4461Calcium 4 By similarity

Sequences

Sequence LengthMass (Da)Tools
D5DEH5 [UniParc].

Last modified June 15, 2010. Version 1.
Checksum: BE1F088C0844F49A

FASTA56260,862
        10         20         30         40         50         60 
MKKKKQALKV LLSVGILSSS FAFAHTSSAA PNNVLSTEKY NKEIKSPEFI SGKLSGPSSQ 

        70         80         90        100        110        120 
KAQDVVFHYM NTNKDKYKLG NENAQNSFKV TEVVKDPVEQ ATVVRLQQVY NNIPVWGSTQ 

       130        140        150        160        170        180 
LAHVAKDGTL KVVSGTVAPD LDKKEKLKGQ KQVDSKKAIQ AAEKDLGFKP TYEKSPSSEL 

       190        200        210        220        230        240 
YVYQNGSDTT YAYVVNLNFL SPEPGNYYYF VDAISGKVLD KYNTIDSVAG PKADVKQAAK 

       250        260        270        280        290        300 
PAAKPVTGTN AIGSGKGVLG DTKSLKTTLS SSTYYLQDNT RGATIYTYDA KNRTSLPGTL 

       310        320        330        340        350        360 
WTDTDNTYNA TRDAAAVDAH YYAGVTYDYY KNKFNRNSYD NAGAPLKSTV HYSSGYNNAF 

       370        380        390        400        410        420 
WNGSQMVYGD GDGTTFVPLS GGLDVIGHEL THAVTERSSN LIYQYESGAL NEAISDIFGT 

       430        440        450        460        470        480 
LVEYYDNRNP DWEIGEDIYT PGTSGDALRS MSNPAKYGDP DHYSKRYTGS SDNGGVHTNS 

       490        500        510        520        530        540 
GIINKAAYLL ANGGTHYGVT VTGIGGDKLG KIYYRANTLY FTQSTTFSQA RAGLVQAAAD 

       550        560 
LYGSGSQEVI SVGKSFDAVG VQ 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of the leu C and npr M genes and a putative spo IV gene from Bacillus megaterium DSM319."
Meinhardt F., Busskamp M., Wittchen K.D.
Appl. Microbiol. Biotechnol. 41:344-351(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome sequences of the industrial vitamin B12-producers B. megaterium QM B1551 and DSM319 reveal new insights into the Bacillus genome evolution and pan-genome structure."
Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J., Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J., Vary P.S.
Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 319.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75070 Genomic DNA. Translation: CAA52964.1.
CP001982 Genomic DNA. Translation: ADF39133.1.
PIRI40227.
RefSeqYP_003597483.1. NC_014103.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADF39133; ADF39133; BMD_2285.
GeneID9117676.
KEGGbmd:BMD_2285.
PATRIC37254631. VBIBacMeg104484_2238.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000247250.
OMASKYNNAF.

Enzyme and pathway databases

BioCycBMEG592022:GIVX-2285-MONOMER.

Family and domain databases

Gene3D3.10.170.10. 1 hit.
InterProIPR011096. FTP_domain.
IPR025711. PepSY.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]
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 nameNPRM_BACMD
AccessionPrimary (citable) accession number: D5DEH5
Secondary accession number(s): Q00891
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: June 15, 2010
Last modified: October 16, 2013
This is version 21 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