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Protein

Subtilisin BPN'

Gene

apr

Organism
Bacillus amyloliquefaciens (Bacillus velezensis)
Status
Reviewed-Annotation score: Annotation score: 5 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. Has a high substrate specificity to fibrin.1 Publication

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.

Enzyme 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 keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi109Calcium 11
Active sitei139Charge relay system1 Publication1
Metal bindingi148Calcium 11
Active sitei171Charge relay system1 Publication1
Metal bindingi182Calcium 1; via carbonyl oxygen1
Metal bindingi184Calcium 11
Metal bindingi186Calcium 1; via carbonyl oxygen1
Metal bindingi188Calcium 1; via carbonyl oxygen1
Metal bindingi276Calcium 2; via carbonyl oxygen1
Metal bindingi278Calcium 2; via carbonyl oxygen1
Metal bindingi281Calcium 2; via carbonyl oxygen1
Active sitei328Charge relay system1 Publication1

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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Sporulation

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.21.62. 630.
SABIO-RKP00782.

Protein family/group databases

MEROPSiS08.034.

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
OrganismiBacillus amyloliquefaciens (Bacillus velezensis)
Taxonomic identifieri1390 [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.

Chemistry databases

DrugBankiDB02325. Isopropyl Alcohol.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30By similarityAdd BLAST30
PropeptideiPRO_000002717731 – 1072 PublicationsAdd BLAST77
ChainiPRO_0000027178108 – 382Subtilisin BPN'Add BLAST275

Keywords - PTMi

Zymogen

Miscellaneous databases

PMAP-CutDBP00782.

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Ica-2Q400598EBI-1033955,EBI-1040468From a different organism.

Protein-protein interaction databases

IntActiP00782. 2 interactors.
MINTiMINT-242921.
STRINGi326423.RBAM_010500.

Structurei

Secondary structure

1382
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 44Combined sources6
Turni46 – 49Combined sources4
Helixi53 – 61Combined sources9
Turni62 – 64Combined sources3
Beta strandi66 – 70Combined sources5
Beta strandi72 – 80Combined sources9
Helixi83 – 90Combined sources8
Beta strandi95 – 100Combined sources6
Beta strandi105 – 108Combined sources4
Helixi113 – 117Combined sources5
Helixi120 – 126Combined sources7
Beta strandi134 – 140Combined sources7
Beta strandi146 – 148Combined sources3
Beta strandi151 – 156Combined sources6
Beta strandi158 – 160Combined sources3
Beta strandi168 – 170Combined sources3
Helixi171 – 180Combined sources10
Beta strandi183 – 188Combined sources6
Beta strandi195 – 201Combined sources7
Beta strandi207 – 209Combined sources3
Helixi211 – 223Combined sources13
Beta strandi227 – 231Combined sources5
Beta strandi233 – 236Combined sources4
Helixi240 – 251Combined sources12
Beta strandi255 – 259Combined sources5
Turni275 – 277Combined sources3
Beta strandi281 – 287Combined sources7
Beta strandi289 – 291Combined sources3
Beta strandi305 – 308Combined sources4
Beta strandi310 – 316Combined sources7
Turni317 – 319Combined sources3
Beta strandi320 – 324Combined sources5
Helixi327 – 344Combined sources18
Helixi350 – 358Combined sources9
Beta strandi360 – 362Combined sources3
Helixi367 – 370Combined sources4
Helixi377 – 380Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP00782.
SMRiP00782.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00782.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini134 – 380Peptidase S8Add BLAST247

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1404. 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.

P00782-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:382
Mass (Da):39,181
Last modified:July 21, 1986 - v1
Checksum:iED987DAFA37B8335
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti128Y → F in strain: DC-4. 1 Publication1

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.
PIRiB25415. SUBSN.
RefSeqiWP_013351733.1. NZ_LZZO01000012.1.

Genome annotation databases

GeneIDi9780852.

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.
PIRiB25415. SUBSN.
RefSeqiWP_013351733.1. NZ_LZZO01000012.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP00782.
SMRiP00782.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00782. 2 interactors.
MINTiMINT-242921.
STRINGi326423.RBAM_010500.

Chemistry databases

DrugBankiDB02325. Isopropyl Alcohol.

Protein family/group databases

MEROPSiS08.034.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi9780852.

Phylogenomic databases

eggNOGiCOG1404. LUCA.

Enzyme and pathway databases

BRENDAi3.4.21.62. 630.
SABIO-RKP00782.

Miscellaneous databases

EvolutionaryTraceiP00782.
PMAP-CutDBP00782.

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_BACAM
AccessioniPrimary (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: November 2, 2016
This is version 144 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.