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P68736 (NPRE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. 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 NprE
Gene names
Name:nprE
Ordered Locus Names:BSU14700
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length521 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 Potential.

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secreted By similarity.

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
   PTMZymogen
   Technical termComplete proteome
Reference proteome
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 – 221194Activation peptide By similarity
PRO_0000028606
Chain222 – 521300Bacillolysin
PRO_0000028607

Sites

Active site3651 By similarity
Active site4491Proton donor By similarity
Metal binding3601Calcium 1 Potential
Metal binding3641Zinc; catalytic By similarity
Metal binding3681Zinc; catalytic By similarity
Metal binding3881Zinc; catalytic By similarity
Metal binding3991Calcium 1 Potential
Metal binding3991Calcium 2 Potential
Metal binding4021Calcium 1 Potential
Metal binding4021Calcium 2 Potential
Metal binding4041Calcium 1; via carbonyl oxygen Potential
Metal binding4071Calcium 1 Potential
Metal binding4071Calcium 2 Potential

Experimental info

Sequence conflict101A → R Ref.1
Sequence conflict101A → R Ref.2
Sequence conflict44 – 452NA → KP Ref.1
Sequence conflict44 – 452NA → KP Ref.2
Sequence conflict77 – 782RL → SV Ref.1
Sequence conflict77 – 782RL → SV Ref.2

Sequences

Sequence LengthMass (Da)Tools
P68736 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 439E7B8F19D1E8F4

FASTA52156,522
        10         20         30         40         50         60 
MGLGKKLSVA VAASFMSLSI SLPGVQAAEG HQLKENQTNF LSKNAIAQSE LSAPNDKAVK 

        70         80         90        100        110        120 
QFLKKNSNIF KGDPSKRLKL VESTTDALGY KHFRYAPVVN GVPIKDSQVI VHVDKSDNVY 

       130        140        150        160        170        180 
AVNGELHNQS AAKTDNSQKV SSEKALALAF KAIGKSPDAV SNGAAKNSNK AELKAIETKD 

       190        200        210        220        230        240 
GSYRLAYDVT IRYVEPEPAN WEVLVDAETG SILKQQNKVE HAAATGSGTT LKGATVPLNI 

       250        260        270        280        290        300 
SYEGGKYVLR DLSKPTGTQI ITYDLQNRQS RLPGTLVSST TKTFTSSSQR AAVDAHYNLG 

       310        320        330        340        350        360 
KVYDYFYSNF KRNSYDNKGS KIVSSVHYGT QYNNAAWTGD QMIYGDGDGS FFSPLSGSLD 

       370        380        390        400        410        420 
VTAHEMTHGV TQETANLIYE NQPGALNESF SDVFGYFNDT EDWDIGEDIT VSQPALRSLS 

       430        440        450        460        470        480 
NPTKYNQPDN YANYRNLPNT DEGDYGGVHT NSGIPNKAAY NTITKLGVSK SQQIYYRALT 

       490        500        510        520 
TYLTPSSTFK DAKAALIQSA RDLYGSTDAA KVEAAWNAVG L

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the neutral protease gene of Bacillus subtilis and the use of the cloned gene to create an in vitro-derived deletion mutation."
Yang M.Y., Ferrari E., Henner D.J.
J. Bacteriol. 160:15-21(1984) [PubMed: 6090407] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The ampS-nprE (124 degrees-127 degrees) region of the Bacillus subtilis 168 chromosome: sequencing of a 27 kb segment and identification of several genes in the area."
Winters P., Caldwell R.M., Enfield L., Ferrari E.
Microbiology 142:3033-3037(1996) [PubMed: 8969500] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]Lee S., Yoon K., Nam H., Chae K.
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NS15-4.
[4]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[5]Purnell B., Presecan E., Glaser P., Richou A., Danchin A., Goffeau A.
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-158.
Strain: 168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		K01985 Genomic DNA. Translation: AAA22627.1.
AF012285 Genomic DNA. Translation: AAC24942.1.
U30932 Genomic DNA. Translation: AAA82609.1.
AL009126 Genomic DNA. Translation: CAB13343.1.
Z97025 Genomic DNA. Translation: CAB09705.1.
PIRHYBS. A25414.
JQ2129.
RefSeqNP_389353.1. NC_000964.3.

3D structure databases

ProteinModelPortalP68736.
SMRP68736. Positions 222-521.
ModBaseSearch...

Protein family/group databases

MEROPSM04.014.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001387; EBBACP00000001387; EBBACG00000001385.
GeneID935981.
GenomeReviewsGene locus BSU14700 in contig AL009126_GR.
KEGGbsu:BSU14700.
NMPDRfig|224308.1.peg.1472.
PATRIC18974737. VBIBacSub10457_1560.

Organism-specific databases

GenoListBSU14700. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000000318.
HOGENOMHBG753113.
OMAPSHMKDY.
PhylomeDBP68736.
ProtClustDBCLSK887250.

Enzyme and pathway databases

BioCycBSUB:BSU14700-MONOMER.

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.
KOK01400.
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_BACSU
AccessionPrimary (citable) accession number: P68736
Secondary accession number(s): P06142, P25268
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: August 1, 1988
Last modified: January 25, 2012
This is version 59 of the entry and version 1 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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