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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)DescriptionActionsGraphical viewLength
Metal bindingi107Calcium 11
Active sitei137By similarity1
Metal bindingi146Calcium 11
Active sitei168By similarity1
Metal bindingi179Calcium 1; via carbonyl oxygen1
Metal bindingi181Calcium 11
Metal bindingi185Calcium 1; via carbonyl oxygen1
Metal bindingi273Calcium 2; via carbonyl oxygen1
Metal bindingi275Calcium 2; via carbonyl oxygen1
Metal bindingi278Calcium 2; via carbonyl oxygen1
Active sitei325By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Sporulation

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

SABIO-RKP00780.

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

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.

Chemistry databases

ChEMBLiCHEMBL4299.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29By similarityAdd BLAST29
PropeptideiPRO_000002717930 – 1051 PublicationAdd BLAST76
ChainiPRO_0000027180106 – 379Subtilisin CarlsbergAdd BLAST274

Keywords - PTMi

Zymogen

Interactioni

Protein-protein interaction databases

IntActiP00780. 2 interactors.
MINTiMINT-1505000.
STRINGi279010.BLi01109.

Chemistry databases

BindingDBiP00780.

Structurei

Secondary structure

1379
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi112 – 115Combined sources4
Helixi118 – 123Combined sources6
Beta strandi132 – 138Combined sources7
Beta strandi149 – 154Combined sources6
Beta strandi156 – 158Combined sources3
Beta strandi161 – 163Combined sources3
Beta strandi165 – 167Combined sources3
Helixi168 – 177Combined sources10
Beta strandi180 – 184Combined sources5
Beta strandi192 – 198Combined sources7
Beta strandi204 – 206Combined sources3
Helixi208 – 220Combined sources13
Beta strandi224 – 228Combined sources5
Beta strandi230 – 234Combined sources5
Helixi237 – 248Combined sources12
Beta strandi252 – 256Combined sources5
Turni272 – 274Combined sources3
Beta strandi278 – 284Combined sources7
Beta strandi300 – 305Combined sources6
Beta strandi307 – 313Combined sources7
Turni314 – 316Combined sources3
Beta strandi317 – 321Combined sources5
Helixi324 – 341Combined sources18
Helixi347 – 356Combined sources10
Helixi364 – 367Combined sources4
Helixi374 – 377Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00780.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini132 – 377Peptidase S8Add BLAST246

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105RX7. Bacteria.
COG1404. LUCA.

Family and domain databases

Gene3Di3.30.70.80. 1 hit.
3.40.50.200. 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. Propept_inh.
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)DescriptionActionsGraphical viewLength
Sequence conflicti207T → S AA sequence (PubMed:4967581).Curated1
Sequence conflicti233P → A AA sequence (PubMed:4967581).Curated1
Sequence conflicti262 – 265SSGN → NSGS AA sequence (PubMed:4967581).Curated4
Sequence conflicti316S → N AA sequence (PubMed:4967581).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00780. 2 interactors.
MINTiMINT-1505000.
STRINGi279010.BLi01109.

Chemistry databases

BindingDBiP00780.
ChEMBLiCHEMBL4299.

Protein family/group databases

Allergomei8254. Bac li Subtilisin.
MEROPSiS08.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105RX7. Bacteria.
COG1404. LUCA.

Enzyme and pathway databases

SABIO-RKP00780.

Miscellaneous databases

EvolutionaryTraceiP00780.

Family and domain databases

Gene3Di3.30.70.80. 1 hit.
3.40.50.200. 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. Propept_inh.
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...

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: November 2, 2016
This is version 132 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

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 one 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.