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Protein

Subtilisin E

Gene

aprE

Organism
Bacillus subtilis (strain 168)
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.

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+1 PublicationNote: Binds 2 calcium ions per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi108Calcium 11 Publication1
Active sitei138Charge relay system1 Publication1
Metal bindingi147Calcium 11 Publication1
Active sitei170Charge relay system1 Publication1
Metal bindingi181Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi183Calcium 11 Publication1
Metal bindingi185Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi187Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi275Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi277Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi280Calcium 21 Publication1
Metal bindingi303Calcium 21 Publication1
Active sitei327Charge relay system1 Publication1

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

BioCyciBSUB:BSU10300-MONOMER.
SABIO-RKP04189.

Protein family/group databases

MEROPSiS08.036.

Names & Taxonomyi

Protein namesi
Recommended name:
Subtilisin E (EC:3.4.21.62)
Gene namesi
Name:aprE
Synonyms:apr, aprA, sprE
Ordered Locus Names:BSU10300
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi138D → N: Prevents intramolecular processing to an active enzyme. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 291 PublicationAdd BLAST29
PropeptideiPRO_000002718730 – 106Add BLAST77
ChainiPRO_0000027188107 – 381Subtilisin EAdd BLAST275

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Proteomic databases

PaxDbiP04189.
PRIDEiP04189.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100005716.

Structurei

Secondary structure

1381
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 43Combined sources7
Beta strandi45 – 48Combined sources4
Helixi52 – 60Combined sources9
Turni61 – 63Combined sources3
Beta strandi65 – 69Combined sources5
Beta strandi71 – 80Combined sources10
Helixi82 – 89Combined sources8
Beta strandi94 – 99Combined sources6
Beta strandi102 – 105Combined sources4
Helixi112 – 116Combined sources5
Helixi119 – 125Combined sources7
Beta strandi133 – 139Combined sources7
Beta strandi150 – 155Combined sources6
Beta strandi167 – 169Combined sources3
Helixi170 – 179Combined sources10
Beta strandi183 – 186Combined sources4
Beta strandi195 – 200Combined sources6
Beta strandi206 – 209Combined sources4
Helixi210 – 222Combined sources13
Beta strandi226 – 230Combined sources5
Beta strandi232 – 235Combined sources4
Helixi239 – 250Combined sources12
Beta strandi254 – 258Combined sources5
Turni274 – 276Combined sources3
Beta strandi280 – 286Combined sources7
Beta strandi304 – 307Combined sources4
Beta strandi309 – 315Combined sources7
Turni316 – 318Combined sources3
Beta strandi319 – 323Combined sources5
Helixi326 – 343Combined sources18
Helixi349 – 358Combined sources10
Helixi366 – 369Combined sources4
Helixi376 – 379Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SCJX-ray2.00A107-381[»]
B36-106[»]
3WHIX-ray2.40A/B30-381[»]
DisProtiDP00394.
ProteinModelPortaliP04189.
SMRiP04189.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04189.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 379Peptidase S8Add BLAST247

Domaini

The propeptide functions as an intramolecular chaperone which is essential for the correct folding of the protease domain but is not required for enzymatic function of the folded protein. It is autoprocessed and degraded after completion of the folding process.1 Publication

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105RX7. Bacteria.
COG1404. LUCA.
HOGENOMiHOG000199176.
InParanoidiP04189.
KOiK01342.
OMAiQYSWIIN.
PhylomeDBiP04189.

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.

P04189-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSKKLWISL LFALTLIFTM AFSNMSAQAA GKSSTEKKYI VGFKQTMSAM
60 70 80 90 100
SSAKKKDVIS EKGGKVQKQF KYVNAAAATL DEKAVKELKK DPSVAYVEED
110 120 130 140 150
HIAHEYAQSV PYGISQIKAP ALHSQGYTGS NVKVAVIDSG IDSSHPDLNV
160 170 180 190 200
RGGASFVPSE TNPYQDGSSH GTHVAGTIAA LNNSIGVLGV APSASLYAVK
210 220 230 240 250
VLDSTGSGQY SWIINGIEWA ISNNMDVINM SLGGPTGSTA LKTVVDKAVS
260 270 280 290 300
SGIVVAAAAG NEGSSGSTST VGYPAKYPST IAVGAVNSSN QRASFSSAGS
310 320 330 340 350
ELDVMAPGVS IQSTLPGGTY GAYNGTSMAT PHVAGAAALI LSKHPTWTNA
360 370 380
QVRDRLESTA TYLGNSFYYG KGLINVQAAA Q
Length:381
Mass (Da):39,479
Last modified:June 16, 2009 - v3
Checksum:i5C8A4B0E42FCE83D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti27A → V in CAA74536 (PubMed:9579061).Curated1
Sequence conflicti191A → S in AAA22742 (PubMed:6427178).Curated1
Sequence conflicti191A → S in CAA74536 (PubMed:9579061).Curated1
Sequence conflicti191A → S (PubMed:7589571).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01988 Genomic DNA. Translation: AAA22742.1.
Y14083 Genomic DNA. Translation: CAA74536.1.
AL009126 Genomic DNA. Translation: CAB12870.2.
K01443 Genomic DNA. Translation: AAA22814.1.
M16639 Genomic DNA. Translation: AAA22744.1.
M31060 Genomic DNA. Translation: AAA22246.1.
M19125 Genomic DNA. Translation: AAA22245.1.
PIRiA00972. SUBSI.
RefSeqiNP_388911.2. NC_000964.3.
WP_003233171.1. NZ_JNCM01000035.1.
WP_009966941.1. NZ_CM000487.1.

Genome annotation databases

EnsemblBacteriaiCAB12870; CAB12870; BSU10300.
GeneIDi939313.
KEGGibsu:BSU10300.
PATRICi18973758. VBIBacSub10457_1073.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01988 Genomic DNA. Translation: AAA22742.1.
Y14083 Genomic DNA. Translation: CAA74536.1.
AL009126 Genomic DNA. Translation: CAB12870.2.
K01443 Genomic DNA. Translation: AAA22814.1.
M16639 Genomic DNA. Translation: AAA22744.1.
M31060 Genomic DNA. Translation: AAA22246.1.
M19125 Genomic DNA. Translation: AAA22245.1.
PIRiA00972. SUBSI.
RefSeqiNP_388911.2. NC_000964.3.
WP_003233171.1. NZ_JNCM01000035.1.
WP_009966941.1. NZ_CM000487.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SCJX-ray2.00A107-381[»]
B36-106[»]
3WHIX-ray2.40A/B30-381[»]
DisProtiDP00394.
ProteinModelPortaliP04189.
SMRiP04189.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100005716.

Protein family/group databases

MEROPSiS08.036.

Proteomic databases

PaxDbiP04189.
PRIDEiP04189.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12870; CAB12870; BSU10300.
GeneIDi939313.
KEGGibsu:BSU10300.
PATRICi18973758. VBIBacSub10457_1073.

Phylogenomic databases

eggNOGiENOG4105RX7. Bacteria.
COG1404. LUCA.
HOGENOMiHOG000199176.
InParanoidiP04189.
KOiK01342.
OMAiQYSWIIN.
PhylomeDBiP04189.

Enzyme and pathway databases

BioCyciBSUB:BSU10300-MONOMER.
SABIO-RKP04189.

Miscellaneous databases

EvolutionaryTraceiP04189.

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_BACSU
AccessioniPrimary (citable) accession number: P04189
Secondary accession number(s): O07613, P70989
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: June 16, 2009
Last modified: November 2, 2016
This is version 150 of the entry and version 3 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.