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Protein

Subtilisin

Gene

apr

Organism
Bacillus pumilus (Bacillus mesentericus)
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 bindingi2Calcium 11
Active sitei32By similarity1
Metal bindingi41Calcium 11
Active sitei64By similarity1
Metal bindingi75Calcium 1; via carbonyl oxygen1
Metal bindingi77Calcium 11
Metal bindingi79Calcium 1; via carbonyl oxygen1
Metal bindingi81Calcium 1; via carbonyl oxygen1
Metal bindingi169Calcium 2; via carbonyl oxygen1
Metal bindingi171Calcium 2; via carbonyl oxygen1
Metal bindingi174Calcium 2; via carbonyl oxygen1
Active sitei221By 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

Protein family/group databases

MEROPSiS08.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Subtilisin (EC:3.4.21.62)
Alternative name(s):
Alkaline mesentericopeptidase
Gene namesi
Name:apr
OrganismiBacillus pumilus (Bacillus mesentericus)
Taxonomic identifieri1408 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000764191 – 275SubtilisinAdd BLAST275

Interactioni

Protein-protein interaction databases

MINTiMINT-1504246.

Structurei

Secondary structure

1275
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 10Combined sources5
Helixi13 – 19Combined sources7
Beta strandi27 – 33Combined sources7
Beta strandi44 – 49Combined sources6
Helixi65 – 73Combined sources9
Beta strandi76 – 80Combined sources5
Beta strandi88 – 94Combined sources7
Helixi104 – 116Combined sources13
Beta strandi120 – 124Combined sources5
Beta strandi126 – 130Combined sources5
Helixi133 – 144Combined sources12
Beta strandi148 – 152Combined sources5
Turni168 – 170Combined sources3
Beta strandi174 – 180Combined sources7
Beta strandi198 – 201Combined sources4
Beta strandi203 – 209Combined sources7
Turni210 – 212Combined sources3
Beta strandi213 – 217Combined sources5
Helixi220 – 237Combined sources18
Helixi243 – 252Combined sources10
Helixi260 – 263Combined sources4
Helixi270 – 273Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MEEX-ray2.00A1-275[»]
ProteinModelPortaliP07518.
SMRiP07518.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07518.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 273Peptidase S8Add BLAST247

Sequence similaritiesi

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

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.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07518-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AQSVPYGISQ IKAPALHSQG YTGSNVKVAV IDSGIDSSHP DLNVRGGASF
60 70 80 90 100
VPSETNPYQD GSSHGTHVAG TIAALNNSIG VLGVAPSSAL YAVKVLDSTG
110 120 130 140 150
SGQYSWIING IEWAISNNMD VINMSLGGPT GSTALKTVVD KAVSSGIVVA
160 170 180 190 200
AAAGNEGSSG STSTVGYPAK YPSTIAVGAV NSANQRASFS SAGSELDVMA
210 220 230 240 250
PGVSIQSTLP GGTYGAYNGT SMATPHVAGA AALILSKHPT WTNAQVRDRL
260 270
ESTATYLGSS FYYGKGLINV QAAAQ
Length:275
Mass (Da):27,656
Last modified:April 1, 1988 - v1
Checksum:i33BDA897DBA4170A
GO

Sequence databases

PIRiA23624.

Cross-referencesi

Sequence databases

PIRiA23624.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MEEX-ray2.00A1-275[»]
ProteinModelPortaliP07518.
SMRiP07518.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1504246.

Protein family/group databases

MEROPSiS08.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP07518.

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.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSUBT_BACPU
AccessioniPrimary (citable) accession number: P07518
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: November 2, 2016
This is version 103 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.