UniProtKB - P00782 (SUBT_BACAM)
Protein
Subtilisin BPN'
Gene
apr
Organism
Bacillus amyloliquefaciens (Bacillus velezensis)
Status
Functioni
Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.1 Publication
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.
Catalytic activityi
- Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides. EC:3.4.21.62
Cofactori
Ca2+Note: Binds 2 calcium ions per subunit.
Activity regulationi
Completely inhibited by phenylmethylsulfony fluoride (PMSF) and partially inhibited by benzamidine hydrochloride, leupeptin, and pepstatin A.1 Publication
pH dependencei
Optimum pH is 9.0.1 Publication
Temperature dependencei
Optimum temperature is 48 degrees Celsius.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 109 | Calcium 1 | 1 | |
Active sitei | 139 | Charge relay systemPROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 148 | Calcium 1 | 1 | |
Active sitei | 171 | Charge relay systemPROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 182 | Calcium 1; via carbonyl oxygen | 1 | |
Metal bindingi | 184 | Calcium 1 | 1 | |
Metal bindingi | 186 | Calcium 1; via carbonyl oxygen | 1 | |
Metal bindingi | 188 | Calcium 1; via carbonyl oxygen | 1 | |
Metal bindingi | 276 | Calcium 2; via carbonyl oxygen | 1 | |
Metal bindingi | 278 | Calcium 2; via carbonyl oxygen | 1 | |
Metal bindingi | 281 | Calcium 2; via carbonyl oxygen | 1 | |
Active sitei | 328 | Charge relay systemPROSITE-ProRule annotation1 Publication | 1 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- serine-type endopeptidase activity Source: UniProtKB
GO - Biological processi
- fibrinolysis Source: UniProtKB
- proteolysis Source: UniProtKB
- sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
Keywordsi
Molecular function | Hydrolase, Protease, Serine protease |
Biological process | Sporulation |
Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
BRENDAi | 3.4.21.62, 630 |
SABIO-RKi | P00782 |
Protein family/group databases
MEROPSi | S08.034 |
Names & Taxonomyi
Protein namesi | Recommended name: Subtilisin BPN' (EC:3.4.21.62)Alternative name(s): Alkaline protease Subtilisin DFE Subtilisin Novo |
Gene namesi | Name:apr |
Organismi | Bacillus amyloliquefaciens (Bacillus velezensis) |
Taxonomic identifieri | 1390 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus amyloliquefaciens group |
Subcellular locationi
Extracellular region or secreted
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Keywords - Cellular componenti
SecretedPathology & Biotechi
Biotechnological usei
Used as a detergent protease. Sold under the name Alcalase by Novozymes.
Chemistry databases
DrugBanki | DB03297, Benzylsulfonic acid DB04491, Diisopropylphosphono Group DB02442, Dioxyselenocysteine DB01805, Monoisopropylphosphorylserine DB01915, S-Hydroxycysteine |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 30 | By similarityAdd BLAST | 30 | |
PropeptideiPRO_0000027177 | 31 – 107 | 2 PublicationsAdd BLAST | 77 | |
ChainiPRO_0000027178 | 108 – 382 | Subtilisin BPN'Add BLAST | 275 |
Keywords - PTMi
ZymogenProteomic databases
PRIDEi | P00782 |
Interactioni
Subunit structurei
Monomer.
1 PublicationBinary interactionsi
P00782
With | #Exp. | IntAct |
---|---|---|
Ica-2 [Q40059] from Hordeum vulgare. | 8 | EBI-1033955,EBI-1040468 |
Protein-protein interaction databases
IntActi | P00782, 2 interactors |
MINTi | P00782 |
STRINGi | 326423.RBAM_010500 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P00782 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P00782 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 39 – 105 | Inhibitor I9Sequence analysisAdd BLAST | 67 | |
Domaini | 112 – 381 | Peptidase S8PROSITE-ProRule annotationAdd BLAST | 270 |
Sequence similaritiesi
Belongs to the peptidase S8 family.Curated
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | COG1404, Bacteria |
Family and domain databases
CDDi | cd07477, Peptidases_S8_Subtilisin_subset, 1 hit |
Gene3Di | 3.30.70.80, 1 hit 3.40.50.200, 1 hit |
InterProi | View protein in InterPro IPR000209, Peptidase_S8/S53_dom IPR036852, Peptidase_S8/S53_dom_sf IPR023827, Peptidase_S8_Asp-AS IPR022398, Peptidase_S8_His-AS IPR023828, Peptidase_S8_Ser-AS IPR015500, Peptidase_S8_subtilisin-rel IPR010259, S8pro/Inhibitor_I9 IPR037045, S8pro/Inhibitor_I9_sf IPR034202, Subtilisin_Carlsberg-like |
Pfami | View protein in Pfam PF05922, Inhibitor_I9, 1 hit PF00082, Peptidase_S8, 1 hit |
PRINTSi | PR00723, SUBTILISIN |
SUPFAMi | SSF52743, SSF52743, 1 hit |
PROSITEi | View protein in PROSITE PS51892, SUBTILASE, 1 hit PS00136, SUBTILASE_ASP, 1 hit PS00137, SUBTILASE_HIS, 1 hit PS00138, SUBTILASE_SER, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P00782-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MRGKKVWISL LFALALIFTM AFGSTSSAQA AGKSNGEKKY IVGFKQTMST
60 70 80 90 100
MSAAKKKDVI SEKGGKVQKQ FKYVDAASAT LNEKAVKELK KDPSVAYVEE
110 120 130 140 150
DHVAHAYAQS VPYGVSQIKA PALHSQGYTG SNVKVAVIDS GIDSSHPDLK
160 170 180 190 200
VAGGASMVPS ETNPFQDNNS HGTHVAGTVA ALNNSIGVLG VAPSASLYAV
210 220 230 240 250
KVLGADGSGQ YSWIINGIEW AIANNMDVIN MSLGGPSGSA ALKAAVDKAV
260 270 280 290 300
ASGVVVVAAA GNEGTSGSSS TVGYPGKYPS VIAVGAVDSS NQRASFSSVG
310 320 330 340 350
PELDVMAPGV SIQSTLPGNK YGAYNGTSMA SPHVAGAAAL ILSKHPNWTN
360 370 380
TQVRSSLENT TTKLGDSFYY GKGLINVQAA AQ
Sequence cautioni
The sequence CAA24990 differs from that shown. Reason: Erroneous initiation.Curated
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 128 | Y → F in strain: DC-4. 1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | K02496 Genomic DNA Translation: AAB05345.1 X00165 Genomic DNA Translation: CAA24990.1 Different initiation. |
PIRi | B25415, SUBSN |
RefSeqi | WP_013351733.1, NZ_VRTX01000004.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | K02496 Genomic DNA Translation: AAB05345.1 X00165 Genomic DNA Translation: CAA24990.1 Different initiation. |
PIRi | B25415, SUBSN |
RefSeqi | WP_013351733.1, NZ_VRTX01000004.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1A2Q | X-ray | 1.80 | A | 108-382 | [»] | |
1AK9 | X-ray | 1.80 | A | 108-382 | [»] | |
1AQN | X-ray | 1.80 | A | 108-382 | [»] | |
1AU9 | X-ray | 1.80 | A | 108-382 | [»] | |
1DUI | X-ray | 2.00 | A | 108-382 | [»] | |
1GNS | X-ray | 1.80 | A | 112-382 | [»] | |
1GNV | X-ray | 1.90 | A | 108-382 | [»] | |
1LW6 | X-ray | 1.50 | E | 108-382 | [»] | |
1S01 | X-ray | 1.70 | A | 108-382 | [»] | |
1S02 | X-ray | 1.90 | A | 108-382 | [»] | |
1SBH | X-ray | 1.80 | A | 108-382 | [»] | |
1SBI | X-ray | 2.20 | A | 108-382 | [»] | |
1SBN | X-ray | 2.10 | E | 108-382 | [»] | |
1SBT | X-ray | 2.50 | A | 108-382 | [»] | |
1SIB | X-ray | 2.40 | E | 108-382 | [»] | |
1SPB | X-ray | 2.00 | P | 37-107 | [»] | |
S | 108-382 | [»] | ||||
1ST2 | X-ray | 2.00 | A | 108-382 | [»] | |
1SUA | X-ray | 2.10 | A | 108-382 | [»] | |
1SUB | X-ray | 1.75 | A | 108-382 | [»] | |
1SUC | X-ray | 1.80 | A | 108-382 | [»] | |
1SUD | X-ray | 1.90 | A | 108-382 | [»] | |
1SUE | X-ray | 1.80 | A | 108-382 | [»] | |
1SUP | X-ray | 1.60 | A | 108-382 | [»] | |
1TM1 | X-ray | 1.70 | E | 108-382 | [»] | |
1TM3 | X-ray | 1.57 | E | 108-382 | [»] | |
1TM4 | X-ray | 1.70 | E | 108-382 | [»] | |
1TM5 | X-ray | 1.45 | E | 108-382 | [»] | |
1TM7 | X-ray | 1.59 | E | 108-382 | [»] | |
1TMG | X-ray | 1.67 | E | 108-382 | [»] | |
1TO1 | X-ray | 1.68 | E | 108-382 | [»] | |
1TO2 | X-ray | 1.30 | E | 108-382 | [»] | |
1UBN | X-ray | 2.40 | A | 108-382 | [»] | |
1V5I | X-ray | 1.50 | A | 108-382 | [»] | |
1Y1K | X-ray | 1.56 | E | 108-382 | [»] | |
1Y33 | X-ray | 1.80 | E | 108-382 | [»] | |
1Y34 | X-ray | 1.55 | E | 108-382 | [»] | |
1Y3B | X-ray | 1.80 | E | 108-382 | [»] | |
1Y3C | X-ray | 1.69 | E | 108-382 | [»] | |
1Y3D | X-ray | 1.80 | E | 108-382 | [»] | |
1Y3F | X-ray | 1.72 | E | 108-382 | [»] | |
1Y48 | X-ray | 1.84 | E | 108-382 | [»] | |
1Y4A | X-ray | 1.60 | E | 108-382 | [»] | |
1Y4D | X-ray | 2.00 | E | 108-382 | [»] | |
1YJA | X-ray | 1.80 | A | 108-382 | [»] | |
1YJB | X-ray | 1.80 | A | 108-382 | [»] | |
1YJC | X-ray | 1.80 | A | 108-382 | [»] | |
2SBT | X-ray | 2.80 | A | 108-382 | [»] | |
2SIC | X-ray | 1.80 | E | 108-382 | [»] | |
2SNI | X-ray | 2.10 | E | 108-382 | [»] | |
2ST1 | X-ray | 1.80 | A | 108-382 | [»] | |
3BGO | X-ray | 1.80 | P | 32-111 | [»] | |
S | 108-382 | [»] | ||||
3CNQ | X-ray | 1.71 | P | 32-111 | [»] | |
S | 108-382 | [»] | ||||
3CO0 | X-ray | 1.93 | P | 32-111 | [»] | |
S | 108-382 | [»] | ||||
3F49 | X-ray | 1.70 | S | 108-382 | [»] | |
3SIC | X-ray | 1.80 | E | 108-382 | [»] | |
5OX2 | X-ray | 2.24 | A | 108-382 | [»] | |
5SIC | X-ray | 2.20 | E | 108-382 | [»] | |
SMRi | P00782 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P00782, 2 interactors |
MINTi | P00782 |
STRINGi | 326423.RBAM_010500 |
Chemistry databases
DrugBanki | DB03297, Benzylsulfonic acid DB04491, Diisopropylphosphono Group DB02442, Dioxyselenocysteine DB01805, Monoisopropylphosphorylserine DB01915, S-Hydroxycysteine |
Protein family/group databases
MEROPSi | S08.034 |
Proteomic databases
PRIDEi | P00782 |
Phylogenomic databases
eggNOGi | COG1404, Bacteria |
Enzyme and pathway databases
BRENDAi | 3.4.21.62, 630 |
SABIO-RKi | P00782 |
Miscellaneous databases
EvolutionaryTracei | P00782 |
Family and domain databases
CDDi | cd07477, Peptidases_S8_Subtilisin_subset, 1 hit |
Gene3Di | 3.30.70.80, 1 hit 3.40.50.200, 1 hit |
InterProi | View protein in InterPro IPR000209, Peptidase_S8/S53_dom IPR036852, Peptidase_S8/S53_dom_sf IPR023827, Peptidase_S8_Asp-AS IPR022398, Peptidase_S8_His-AS IPR023828, Peptidase_S8_Ser-AS IPR015500, Peptidase_S8_subtilisin-rel IPR010259, S8pro/Inhibitor_I9 IPR037045, S8pro/Inhibitor_I9_sf IPR034202, Subtilisin_Carlsberg-like |
Pfami | View protein in Pfam PF05922, Inhibitor_I9, 1 hit PF00082, Peptidase_S8, 1 hit |
PRINTSi | PR00723, SUBTILISIN |
SUPFAMi | SSF52743, SSF52743, 1 hit |
PROSITEi | View protein in PROSITE PS51892, SUBTILASE, 1 hit PS00136, SUBTILASE_ASP, 1 hit PS00137, SUBTILASE_HIS, 1 hit PS00138, SUBTILASE_SER, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | SUBT_BACAM | |
Accessioni | P00782Primary (citable) accession number: P00782 Secondary accession number(s): P83945, Q44684 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | July 21, 1986 | |
Last modified: | April 7, 2021 | |
This is version 169 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- Peptidase families
Classification of peptidase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families