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

P00780 (SUBT_BACLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. 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:
Subtilisin Carlsberg

EC=3.4.21.62
Gene names
Name:apr
OrganismBacillus licheniformis
Taxonomic identifier1402 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length379 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.

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.

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.

Ontologies

Keywords
   Biological processSporulation
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMZymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processnegative regulation of catalytic activity

Inferred from electronic annotation. Source: InterPro

sporulation resulting in formation of a cellular spore

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

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 By similarity
Propeptide30 – 10576
PRO_0000027179
Chain106 – 379274Subtilisin Carlsberg
PRO_0000027180

Sites

Active site1371 By similarity
Active site1681 By similarity
Active site3251 By similarity
Metal binding1071Calcium 1
Metal binding1461Calcium 1
Metal binding1791Calcium 1; via carbonyl oxygen
Metal binding1811Calcium 1
Metal binding1851Calcium 1; via carbonyl oxygen
Metal binding2731Calcium 2; via carbonyl oxygen
Metal binding2751Calcium 2; via carbonyl oxygen
Metal binding2781Calcium 2; via carbonyl oxygen

Experimental info

Sequence conflict2071T → S AA sequence Ref.2
Sequence conflict2331P → A AA sequence Ref.2
Sequence conflict262 – 2654SSGN → NSGS AA sequence Ref.2
Sequence conflict3161S → N AA sequence Ref.2

Secondary structure

.................................................. 379
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00780 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: F19A6DC5761FB504

FASTA37938,908
        10         20         30         40         50         60 
MMRKKSFWLG MLTAFMLVFT MAFSDSASAA QPAKNVEKDY IVGFKSGVKT ASVKKDIIKE 

        70         80         90        100        110        120 
SGGKVDKQFR IINAAKAKLD KEALKEVKND PDVAYVEEDH VAHALAQTVP YGIPLIKADK 

       130        140        150        160        170        180 
VQAQGFKGAN VKVAVLDTGI QASHPDLNVV GGASFVAGEA YNTDGNGHGT HVAGTVAALD 

       190        200        210        220        230        240 
NTTGVLGVAP SVSLYAVKVL NSSGSGTYSG IVSGIEWATT NGMDVINMSL GGPSGSTAMK 

       250        260        270        280        290        300 
QAVDNAYARG VVVVAAAGNS GSSGNTNTIG YPAKYDSVIA VGAVDSNSNR ASFSSVGAEL 

       310        320        330        340        350        360 
EVMAPGAGVY STYPTSTYAT LNGTSMASPH VAGAAALILS KHPNLSASQV RNRLSSTATY 

       370 
LGSSFYYGKG LINVEAAAQ 

« Hide

References

[1]"Cloning, sequencing and expression of subtilisin Carlsberg from Bacillus licheniformis."
Jacobs M., Eliasson M., Uhlen M., Flock J.-I.
Nucleic Acids Res. 13:8913-8926(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NCIMB 6816 / CCM 2182 / NCDO 727.
[2]"Subtilisin Carlsberg. V. The complete sequence; comparison with subtilisin BPN'; evolutionary relationships."
Smith E.L., Delange R.J., Evans W.H., Landon M., Markland F.S.
J. Biol. Chem. 243:2184-2191(1968) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 106-379.
[3]"Crystal structure of selenosubtilisin at 2.0-A resolution."
Syed R., Wu Z.P., Hogle J.M., Hilvert D.
Biochemistry 32:6157-6164(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT WITH SELENOCYSTEINE-325.
[4]"Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes."
Stoll V.S., Eger B.T., Hynes R.C., Martichonok V., Jones J.B., Pai E.F.
Biochemistry 37:451-462(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 106-379.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03341 Genomic DNA. Translation: CAB56500.1.
PIRSUBSCL. A24111.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AF4X-ray2.60A106-379[»]
1AV7X-ray2.60A106-379[»]
1AVTX-ray2.00A106-379[»]
1BE6X-ray2.15A106-379[»]
1BE8X-ray2.20A106-379[»]
1BFKX-ray2.30A106-379[»]
1BFUX-ray2.20A106-379[»]
1C3LX-ray2.16A106-378[»]
1CSEX-ray1.20E106-379[»]
1OYVX-ray2.50A/B106-379[»]
1R0RX-ray1.10E106-378[»]
1SBCX-ray2.50A106-379[»]
1SCAX-ray2.00A106-379[»]
1SCBX-ray2.30A106-379[»]
1SCDX-ray2.30A106-379[»]
1SCNX-ray1.90E106-379[»]
1SELX-ray2.00A/B106-379[»]
1VSBX-ray2.10A106-379[»]
1YU6X-ray1.55A/B106-379[»]
2SECX-ray1.80E106-379[»]
2WUVX-ray2.24A106-379[»]
2WUWX-ray2.23E106-379[»]
3UNXX-ray1.26A106-379[»]
3VSBX-ray2.60A106-379[»]
ProteinModelPortalP00780.
SMRP00780. Positions 37-104, 106-379.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00780. 2 interactions.
MINTMINT-1505000.

Chemistry

BindingDBP00780.
ChEMBLCHEMBL4299.

Protein family/group databases

Allergome8254. Bac li Subtilisin.
MEROPSI09.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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

EvolutionaryTraceP00780.

Entry information

Entry nameSUBT_BACLI
AccessionPrimary (citable) accession number: P00780
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1988
Last modified: July 9, 2014
This is version 117 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