Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00782 (SUBT_BACAM) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Subtilisin BPN'

EC=3.4.21.62
Alternative name(s):
Alkaline protease
Subtilisin DFE
Subtilisin Novo
Gene names
Name:apr
OrganismBacillus amyloliquefaciens (Bacillus velezensis)
Taxonomic identifier1390 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin. Ref.4

Catalytic activity

Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.

Cofactor

Binds 2 calcium ions per subunit.

Enzyme regulation

Completely inhibited by phenylmethylsulfony fluoride (PMSF) and partially inhibited by benzamidine hydrochloride, leupeptin, and pepstatin A. Ref.4

Subunit structure

Monomer. Ref.4

Subcellular location

Secreted.

Biotechnological use

Used as a detergent protease. Sold under the name Alcalase by Novozymes.

Miscellaneous

Secretion of subtilisin is associated with onset of sporulation, and many mutations which block sporulation at early stages affect expression levels of subtilisin. However, subtilisin is not necessary for normal sporulation.

Sequence similarities

Belongs to the peptidase S8 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 9.0. Ref.4

Temperature dependence:

Optimum temperature is 48 degrees Celsius.

Sequence caution

The sequence CAA24990.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ica-2Q400598EBI-1033955,EBI-1040468From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 By similarity
Propeptide31 – 10777
PRO_0000027177
Chain108 – 382275Subtilisin BPN'
PRO_0000027178

Sites

Active site1391Charge relay system Ref.9
Active site1711Charge relay system Ref.9
Active site3281Charge relay system Ref.9
Metal binding1091Calcium 1
Metal binding1481Calcium 1
Metal binding1821Calcium 1; via carbonyl oxygen
Metal binding1841Calcium 1
Metal binding1861Calcium 1; via carbonyl oxygen
Metal binding1881Calcium 1; via carbonyl oxygen
Metal binding2761Calcium 2; via carbonyl oxygen
Metal binding2781Calcium 2; via carbonyl oxygen
Metal binding2811Calcium 2; via carbonyl oxygen

Natural variations

Natural variant1281Y → F in strain: DC-4. Ref.4

Secondary structure

....................................................................... 382
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00782 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: ED987DAFA37B8335

FASTA38239,181
        10         20         30         40         50         60 
MRGKKVWISL LFALALIFTM AFGSTSSAQA AGKSNGEKKY IVGFKQTMST MSAAKKKDVI 

        70         80         90        100        110        120 
SEKGGKVQKQ FKYVDAASAT LNEKAVKELK KDPSVAYVEE DHVAHAYAQS VPYGVSQIKA 

       130        140        150        160        170        180 
PALHSQGYTG SNVKVAVIDS GIDSSHPDLK VAGGASMVPS ETNPFQDNNS HGTHVAGTVA 

       190        200        210        220        230        240 
ALNNSIGVLG VAPSASLYAV KVLGADGSGQ YSWIINGIEW AIANNMDVIN MSLGGPSGSA 

       250        260        270        280        290        300 
ALKAAVDKAV ASGVVVVAAA GNEGTSGSSS TVGYPGKYPS VIAVGAVDSS NQRASFSSVG 

       310        320        330        340        350        360 
PELDVMAPGV SIQSTLPGNK YGAYNGTSMA SPHVAGAAAL ILSKHPNWTN TQVRSSLENT 

       370        380 
TTKLGDSFYY GKGLINVQAA AQ 

« Hide

References

[1]"Genes for alkaline protease and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein."
Vasantha N., Thompson L.D., Rhodes C., Banner C., Nagle J., Filpula D.
J. Bacteriol. 159:811-819(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 23844 / P.
[2]"Cloning, sequencing, and secretion of Bacillus amyloliquefaciens subtilisin in Bacillus subtilis."
Wells J.A., Ferrari E., Henner D.J., Estell D.A., Chen E.Y.
Nucleic Acids Res. 11:7911-7925(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-382.
[3]"Subtilisin BPN. VII. Isolation of cyanogen bromide peptides and the complete amino acid sequence."
Markland F.S., Smith E.L.
J. Biol. Chem. 242:5198-5211(1967) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 108-382.
[4]"Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional Chinese soybean food."
Peng Y., Huang Q., Zhang R.-H., Zhang Y.-Z.
Comp. Biochem. Physiol. 134B:45-52(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 108-131, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, VARIANT PHE-128.
Strain: DC-4.
[5]"A hydrogen-bond network at the active site of subtilisin BPN'."
Alden R.A., Wright C.S., Kraut J.
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 257:119-124(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[6]"Crystal structure at 2.6-A resolution of the complex of subtilisin BPN' with streptomyces subtilisin inhibitor."
Hirono S., Akagawa H., Mitsui Y., Iitaka Y.
J. Mol. Biol. 178:389-413(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
[7]"Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding."
Pantoliano M.W., Whitlow M., Wood J.F., Dodd S.W., Hardman K.D., Rollence M.L., Bryan P.N.
Biochemistry 28:7205-7213(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT.
[8]"Subtilisin BPN' at 1.6-A resolution: analysis for discrete disorder and comparison of crystal forms."
Gallagher T., Oliver J., Bott R., Betzel C., Gilliland G.L.
Acta Crystallogr. D 52:1125-1135(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[9]"Identification of histidine 64 in the active site of subtilisin."
Markland F.S., Shaw E., Smith E.L.
Proc. Natl. Acad. Sci. U.S.A. 61:1440-1447(1968) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02496 Genomic DNA. Translation: AAB05345.1.
X00165 Genomic DNA. Translation: CAA24990.1. Different initiation.
PIRSUBSN. B25415.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2QX-ray1.80A108-382[»]
1AK9X-ray1.80A108-382[»]
1AQNX-ray1.80A108-382[»]
1AU9X-ray1.80A108-382[»]
1DUIX-ray2.00A108-382[»]
1GNSX-ray1.80A112-382[»]
1GNVX-ray1.90A108-382[»]
1LW6X-ray1.50E108-382[»]
1S01X-ray1.70A108-382[»]
1S02X-ray1.90A108-382[»]
1SBHX-ray1.80A108-382[»]
1SBIX-ray2.20A108-382[»]
1SBNX-ray2.10E108-382[»]
1SBTX-ray2.50A108-382[»]
1SIBX-ray2.40E108-382[»]
1SPBX-ray2.00P37-107[»]
S108-382[»]
1ST2X-ray2.00A108-382[»]
1SUAX-ray2.10A108-382[»]
1SUBX-ray1.75A108-382[»]
1SUCX-ray1.80A108-382[»]
1SUDX-ray1.90A108-382[»]
1SUEX-ray1.80A108-382[»]
1SUPX-ray1.60A108-382[»]
1TM1X-ray1.70E108-382[»]
1TM3X-ray1.57E108-382[»]
1TM4X-ray1.70E108-382[»]
1TM5X-ray1.45E108-382[»]
1TM7X-ray1.59E108-382[»]
1TMGX-ray1.67E108-382[»]
1TO1X-ray1.68E108-382[»]
1TO2X-ray1.30E108-382[»]
1UBNX-ray2.40A108-382[»]
1V5IX-ray1.50A108-382[»]
1Y1KX-ray1.56E108-382[»]
1Y33X-ray1.80E108-382[»]
1Y34X-ray1.55E108-382[»]
1Y3BX-ray1.80E108-382[»]
1Y3CX-ray1.69E108-382[»]
1Y3DX-ray1.80E108-382[»]
1Y3FX-ray1.72E108-382[»]
1Y48X-ray1.84E108-382[»]
1Y4AX-ray1.60E108-382[»]
1Y4DX-ray2.00E108-382[»]
1YJAX-ray1.80A108-382[»]
1YJBX-ray1.80A108-382[»]
1YJCX-ray1.80A108-382[»]
2SBTX-ray2.80A108-382[»]
2SICX-ray1.80E108-382[»]
2SNIX-ray2.10E108-382[»]
2ST1X-ray1.80A108-382[»]
3BGOX-ray1.80S108-382[»]
3CNQX-ray1.71P32-111[»]
S108-382[»]
3CO0X-ray1.93P32-111[»]
S108-382[»]
3F49X-ray1.70S108-382[»]
3SICX-ray1.80E108-382[»]
5SICX-ray2.20E108-382[»]
ProteinModelPortalP00782.
SMRP00782. Positions 37-382.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00782. 2 interactions.
MINTMINT-242921.

Protein family/group databases

MEROPSI09.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP00782.

Family and domain databases

Gene3D3.40.50.200. 1 hit.
InterProIPR010259. Inhibitor_I9.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
[Graphical view]
PANTHERPTHR10795. PTHR10795. 1 hit.
PfamPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSPR00723. SUBTILISIN.
SUPFAMSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00782.
PMAP-CutDBP00782.

Entry information

Entry nameSUBT_BACAM
AccessionPrimary (citable) accession number: P00782
Secondary accession number(s): P83945, Q44684
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 126 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