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Protein

Subtilisin Carlsberg

Gene

apr

Organism
Bacillus licheniformis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.

Catalytic activityi

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

Cofactori

Ca2+Note: Binds 2 calcium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi107 – 1071Calcium 1
Active sitei137 – 1371By similarity
Metal bindingi146 – 1461Calcium 1
Active sitei168 – 1681By similarity
Metal bindingi179 – 1791Calcium 1; via carbonyl oxygen
Metal bindingi181 – 1811Calcium 1
Metal bindingi185 – 1851Calcium 1; via carbonyl oxygen
Metal bindingi273 – 2731Calcium 2; via carbonyl oxygen
Metal bindingi275 – 2751Calcium 2; via carbonyl oxygen
Metal bindingi278 – 2781Calcium 2; via carbonyl oxygen
Active sitei325 – 3251By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Sporulation

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

MEROPSiS08.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Subtilisin Carlsberg (EC:3.4.21.62)
Gene namesi
Name:apr
OrganismiBacillus licheniformis
Taxonomic identifieri1402 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Biotechnological usei

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

Protein family/group databases

Allergomei8254. Bac li Subtilisin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929By similarityAdd
BLAST
Propeptidei30 – 105761 PublicationPRO_0000027179Add
BLAST
Chaini106 – 379274Subtilisin CarlsbergPRO_0000027180Add
BLAST

Keywords - PTMi

Zymogen

Interactioni

Protein-protein interaction databases

IntActiP00780. 2 interactions.
MINTiMINT-1505000.

Structurei

Secondary structure

1
379
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi112 – 1154Combined sources
Helixi118 – 1236Combined sources
Beta strandi132 – 1387Combined sources
Beta strandi149 – 1546Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi165 – 1673Combined sources
Helixi168 – 17710Combined sources
Beta strandi180 – 1845Combined sources
Beta strandi192 – 1987Combined sources
Beta strandi204 – 2063Combined sources
Helixi208 – 22013Combined sources
Beta strandi224 – 2285Combined sources
Beta strandi230 – 2345Combined sources
Helixi237 – 24812Combined sources
Beta strandi252 – 2565Combined sources
Turni272 – 2743Combined sources
Beta strandi278 – 2847Combined sources
Beta strandi300 – 3056Combined sources
Beta strandi307 – 3137Combined sources
Turni314 – 3163Combined sources
Beta strandi317 – 3215Combined sources
Helixi324 – 34118Combined sources
Helixi347 – 35610Combined sources
Helixi364 – 3674Combined sources
Helixi374 – 3774Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4C3UX-ray2.29A106-379[»]
4C3VX-ray2.26A106-379[»]
ProteinModelPortaliP00780.
SMRiP00780. Positions 37-104, 106-379.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00780.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini132 – 377246Peptidase S8Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S8 family.Curated
Contains 1 peptidase S8 domain.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR000209. 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.
IPR010259. S8pro/Inhibitor_I9.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00780-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMRKKSFWLG MLTAFMLVFT MAFSDSASAA QPAKNVEKDY IVGFKSGVKT
60 70 80 90 100
ASVKKDIIKE SGGKVDKQFR IINAAKAKLD KEALKEVKND PDVAYVEEDH
110 120 130 140 150
VAHALAQTVP YGIPLIKADK VQAQGFKGAN VKVAVLDTGI QASHPDLNVV
160 170 180 190 200
GGASFVAGEA YNTDGNGHGT HVAGTVAALD NTTGVLGVAP SVSLYAVKVL
210 220 230 240 250
NSSGSGTYSG IVSGIEWATT NGMDVINMSL GGPSGSTAMK QAVDNAYARG
260 270 280 290 300
VVVVAAAGNS GSSGNTNTIG YPAKYDSVIA VGAVDSNSNR ASFSSVGAEL
310 320 330 340 350
EVMAPGAGVY STYPTSTYAT LNGTSMASPH VAGAAALILS KHPNLSASQV
360 370
RNRLSSTATY LGSSFYYGKG LINVEAAAQ
Length:379
Mass (Da):38,908
Last modified:August 1, 1988 - v1
Checksum:iF19A6DC5761FB504
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071T → S AA sequence (PubMed:4967581).Curated
Sequence conflicti233 – 2331P → A AA sequence (PubMed:4967581).Curated
Sequence conflicti262 – 2654SSGN → NSGS AA sequence (PubMed:4967581).Curated
Sequence conflicti316 – 3161S → N AA sequence (PubMed:4967581).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03341 Genomic DNA. Translation: CAB56500.1.
PIRiA24111. SUBSCL.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03341 Genomic DNA. Translation: CAB56500.1.
PIRiA24111. SUBSCL.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4C3UX-ray2.29A106-379[»]
4C3VX-ray2.26A106-379[»]
ProteinModelPortaliP00780.
SMRiP00780. Positions 37-104, 106-379.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00780. 2 interactions.
MINTiMINT-1505000.

Chemistry

BindingDBiP00780.
ChEMBLiCHEMBL4299.

Protein family/group databases

Allergomei8254. Bac li Subtilisin.
MEROPSiS08.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00780.

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR000209. 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.
IPR010259. S8pro/Inhibitor_I9.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiSUBT_BACLI
AccessioniPrimary (citable) accession number: P00780
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1988
Last modified: March 4, 2015
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.